HEADER ELECTRON TRANSPORT 19-MAR-90 2TRX TITLE CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT 1.68 TITLE 2 ANGSTROMS RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: THIOREDOXIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562 KEYWDS ELECTRON TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR S.K.KATTI,D.M.LEMASTER,H.EKLUND REVDAT 5 13-JUL-11 2TRX 1 VERSN REVDAT 4 24-FEB-09 2TRX 1 VERSN REVDAT 3 01-APR-03 2TRX 1 JRNL REVDAT 2 15-JAN-93 2TRX 1 HEADER COMPND REVDAT 1 15-OCT-91 2TRX 0 JRNL AUTH S.K.KATTI,D.M.LEMASTER,H.EKLUND JRNL TITL CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT JRNL TITL 2 1.68 A RESOLUTION. JRNL REF J.MOL.BIOL. V. 212 167 1990 JRNL REFN ISSN 0022-2836 JRNL PMID 2181145 JRNL DOI 10.1016/0022-2836(90)90313-B REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.HOLMGREN,B.-O.SODERBERG,H.EKLUND,C.-I.BRANDEN REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI REMARK 1 TITL 2 THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 72 2305 1975 REMARK 1 REFN ISSN 0027-8424 REMARK 1 REFERENCE 2 REMARK 1 AUTH B.-O.SODERBERG,A.HOLMGREN,C.-I.BRANDEN REMARK 1 TITL STRUCTURE OF OXIDIZED THIOREDOXIN TO 4.5 ANGSTROMS REMARK 1 TITL 2 RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 90 143 1974 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 3 REMARK 1 AUTH A.HOLMGREN,B.-O.SODERBERG REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA FOR REMARK 1 TITL 2 THIOREDOXIN FROM ESCHERICHIA COLI B REMARK 1 REF J.MOL.BIOL. V. 54 387 1970 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROFFT REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 25969 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.165 REMARK 3 R VALUE (WORKING SET) : NULL REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1644 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 58 REMARK 3 SOLVENT ATOMS : 140 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.015 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.035 ; 0.030 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.055 ; 0.050 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.021 ; 0.020 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.131 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.165 ; 0.500 REMARK 3 MULTIPLE TORSION (A) : 0.174 ; 0.500 REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : 0.180 ; 0.500 REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 4.000 ; 3.000 REMARK 3 STAGGERED (DEGREES) : 16.300; 15.000 REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.380 ; 1.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.280 ; 1.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 1.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.270 ; 1.500 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2TRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 44.75000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.53000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.75000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.53000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA,PQS REMARK 350 TOTAL BURIED SURFACE AREA: 3680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 89.50000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 65.39562 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 55.43628 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 13 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 TYR A 70 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES REMARK 500 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 GLU A 85 OE1 - CD - OE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 GLU A 101 OE1 - CD - OE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 PHE B 12 CB - CA - C ANGL. DEV. = 15.5 DEGREES REMARK 500 ASP B 20 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES REMARK 500 GLU B 85 CA - CB - CG ANGL. DEV. = 13.6 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP B 13 20.75 144.15 REMARK 500 THR B 14 -88.88 -162.21 REMARK 500 VAL B 16 -40.16 -132.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU A 109 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 1 N REMARK 620 2 ASP A 2 N 86.5 REMARK 620 3 ASP A 2 OD1 172.6 86.0 REMARK 620 4 HOH A 405 O 89.2 92.0 91.5 REMARK 620 5 ASP A 10 OD1 96.3 174.7 91.1 92.5 REMARK 620 6 ASP A 10 OD2 98.6 120.4 84.8 146.9 54.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU B 109 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 2 N REMARK 620 2 HOH B 478 O 88.9 REMARK 620 3 ASP B 2 OD1 89.5 87.8 REMARK 620 4 SER B 1 N 86.9 87.8 174.4 REMARK 620 5 ASP B 10 OD1 172.0 97.4 85.7 98.3 REMARK 620 6 ASP B 10 OD2 117.6 151.2 81.6 103.9 55.4 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 109 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 109 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 607 DBREF 2TRX A 1 108 UNP P0AA25 THIO_ECOLI 1 108 DBREF 2TRX B 1 108 UNP P0AA25 THIO_ECOLI 1 108 SEQRES 1 A 108 SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP SEQRES 2 A 108 THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP SEQRES 3 A 108 PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA SEQRES 4 A 108 PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS SEQRES 5 A 108 LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY SEQRES 6 A 108 THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU SEQRES 7 A 108 LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL SEQRES 8 A 108 GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP SEQRES 9 A 108 ALA ASN LEU ALA SEQRES 1 B 108 SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP SEQRES 2 B 108 THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP SEQRES 3 B 108 PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA SEQRES 4 B 108 PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS SEQRES 5 B 108 LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY SEQRES 6 B 108 THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU SEQRES 7 B 108 LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL SEQRES 8 B 108 GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP SEQRES 9 B 108 ALA ASN LEU ALA HET CU A 109 1 HET CU B 109 1 HET MPD A 601 8 HET MPD B 602 8 HET MPD B 603 8 HET MPD B 604 8 HET MPD A 605 8 HET MPD A 606 8 HET MPD A 607 8 HETNAM CU COPPER (II) ION HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL FORMUL 3 CU 2(CU 2+) FORMUL 5 MPD 7(C6 H14 O2) FORMUL 12 HOH *140(H2 O) HELIX 1 A1A SER A 11 LEU A 17 1DISORDERED IN MOLECULE B 7 HELIX 2 A2A CYS A 32 TYR A 49 1BENT BY 30 DEGREES AT RES 39 18 HELIX 3 A3A ASN A 59 ASN A 63 1 5 HELIX 4 31A THR A 66 TYR A 70 5DISTORTED H-BONDING C-TERMINS 5 HELIX 5 A4A SER A 95 LEU A 107 1 13 HELIX 6 A1B SER B 11 LEU B 17 1DISORDERED IN MOLECULE B 7 HELIX 7 A2B CYS B 32 TYR B 49 1BENT BY 30 DEGREES AT RES 39 18 HELIX 8 A3B ASN B 59 ASN B 63 1 5 HELIX 9 31B THR B 66 TYR B 70 5DISTORTED H-BONDING C-TERMINS 5 HELIX 10 A4B SER B 95 LEU B 107 1 13 SHEET 1 B1A 5 LYS A 3 THR A 8 0 SHEET 2 B1A 5 LEU A 53 ASN A 59 1 O VAL A 55 N ILE A 5 SHEET 3 B1A 5 GLY A 21 TRP A 28 1 N TRP A 28 O LEU A 58 SHEET 4 B1A 5 PRO A 76 LYS A 82 -1 O THR A 77 N PHE A 27 SHEET 5 B1A 5 VAL A 86 GLY A 92 -1 O ALA A 87 N LEU A 80 SHEET 1 B1B 5 LYS B 3 THR B 8 0 SHEET 2 B1B 5 LEU B 53 ASN B 59 1 O VAL B 55 N ILE B 5 SHEET 3 B1B 5 GLY B 21 TRP B 28 1 N TRP B 28 O LEU B 58 SHEET 4 B1B 5 PRO B 76 LYS B 82 -1 O THR B 77 N PHE B 27 SHEET 5 B1B 5 VAL B 86 GLY B 92 -1 O ALA B 87 N LEU B 80 SSBOND 1 CYS A 32 CYS A 35 1555 1555 2.09 SSBOND 2 CYS B 32 CYS B 35 1555 1555 2.05 LINK CU CU A 109 N SER A 1 1555 1555 2.05 LINK CU CU A 109 N ASP A 2 1555 1555 2.06 LINK CU CU A 109 OD1 ASP A 2 1555 1555 2.00 LINK CU CU A 109 O HOH A 405 1555 1555 2.65 LINK CU CU B 109 N ASP B 2 1555 1555 2.05 LINK CU CU B 109 O HOH B 478 1555 1555 2.63 LINK CU CU B 109 OD1 ASP B 2 1555 1555 2.06 LINK CU CU B 109 N SER B 1 1555 1555 2.09 LINK CU CU A 109 OD1 ASP A 10 1555 4545 1.97 LINK CU CU A 109 OD2 ASP A 10 1555 4545 2.62 LINK CU CU B 109 OD1 ASP B 10 1555 4546 2.08 LINK CU CU B 109 OD2 ASP B 10 1555 4546 2.54 CISPEP 1 ILE A 75 PRO A 76 0 0.60 CISPEP 2 ILE B 75 PRO B 76 0 -2.42 SITE 1 AC1 5 SER A 1 ASP A 2 LYS A 3 ASP A 10 SITE 2 AC1 5 HOH A 405 SITE 1 AC2 5 SER B 1 ASP B 2 LYS B 3 ASP B 10 SITE 2 AC2 5 HOH B 478 SITE 1 AC3 4 ASP A 10 ASP A 43 GLU A 44 HOH A 442 SITE 1 AC4 6 GLU A 44 HOH A 524 GLU B 30 TRP B 31 SITE 2 AC4 6 GLY B 33 LYS B 36 SITE 1 AC5 5 TYR B 70 ILE B 72 THR B 77 THR B 89 SITE 2 AC5 5 VAL B 91 SITE 1 AC6 3 ILE B 60 ALA B 67 ILE B 72 SITE 1 AC7 4 MET A 37 ILE A 38 ALA A 93 LEU A 94 SITE 1 AC8 4 TYR A 70 GLY A 71 THR A 89 VAL A 91 SITE 1 AC9 8 ILE A 60 ALA A 67 ILE A 72 ARG A 73 SITE 2 AC9 8 GLY A 74 ILE A 75 HOH A 494 HOH B 528 CRYST1 89.500 51.060 60.450 90.00 113.50 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011173 0.000000 0.004858 0.00000 SCALE2 0.000000 0.019585 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018039 0.00000 ATOM 1 N SER A 1 21.389 25.406 -4.628 1.00 23.22 N ATOM 2 CA SER A 1 21.628 26.691 -3.983 1.00 24.42 C ATOM 3 C SER A 1 20.937 26.944 -2.679 1.00 24.21 C ATOM 4 O SER A 1 21.072 28.079 -2.093 1.00 24.97 O ATOM 5 CB SER A 1 21.117 27.770 -5.002 1.00 28.27 C ATOM 6 OG SER A 1 22.276 27.925 -5.861 1.00 32.61 O ATOM 7 N ASP A 2 20.173 26.028 -2.163 1.00 21.39 N ATOM 8 CA ASP A 2 19.395 26.125 -0.949 1.00 21.57 C ATOM 9 C ASP A 2 20.264 26.214 0.297 1.00 20.89 C ATOM 10 O ASP A 2 19.760 26.575 1.371 1.00 21.49 O ATOM 11 CB ASP A 2 18.439 24.914 -0.856 1.00 22.14 C ATOM 12 CG ASP A 2 19.199 23.629 -0.576 1.00 23.23 C ATOM 13 OD1 ASP A 2 20.107 23.371 -1.387 1.00 22.71 O ATOM 14 OD2 ASP A 2 18.905 22.959 0.420 1.00 23.61 O ATOM 15 N LYS A 3 21.530 25.857 0.207 1.00 19.20 N ATOM 16 CA LYS A 3 22.310 25.875 1.488 1.00 18.91 C ATOM 17 C LYS A 3 23.353 26.982 1.459 1.00 18.43 C ATOM 18 O LYS A 3 24.203 26.950 2.370 1.00 20.34 O ATOM 19 CB LYS A 3 23.006 24.540 1.741 1.00 20.31 C ATOM 20 CG LYS A 3 21.971 23.407 1.921 1.00 22.14 C ATOM 21 CD LYS A 3 22.677 22.143 2.401 1.00 24.45 C ATOM 22 CE LYS A 3 21.620 21.104 2.844 1.00 25.84 C ATOM 23 NZ LYS A 3 20.830 20.757 1.615 1.00 25.55 N ATOM 24 N ILE A 4 23.299 27.821 0.461 1.00 17.03 N ATOM 25 CA ILE A 4 24.287 28.908 0.332 1.00 17.28 C ATOM 26 C ILE A 4 23.779 30.213 0.927 1.00 17.70 C ATOM 27 O ILE A 4 22.691 30.658 0.487 1.00 19.79 O ATOM 28 CB ILE A 4 24.592 29.122 -1.211 1.00 19.04 C ATOM 29 CG1 ILE A 4 24.953 27.791 -1.886 1.00 19.62 C ATOM 30 CG2 ILE A 4 25.689 30.221 -1.338 1.00 19.70 C ATOM 31 CD1 ILE A 4 26.177 27.022 -1.384 1.00 21.32 C ATOM 32 N ILE A 5 24.492 30.834 1.831 1.00 15.41 N ATOM 33 CA ILE A 5 24.075 32.125 2.372 1.00 15.87 C ATOM 34 C AILE A 5 24.236 33.234 1.335 0.50 15.03 C ATOM 35 C BILE A 5 24.313 33.238 1.361 0.50 16.09 C ATOM 36 O AILE A 5 25.272 33.309 0.663 0.50 13.96 O ATOM 37 O BILE A 5 25.462 33.388 0.927 0.50 14.70 O ATOM 38 CB ILE A 5 24.924 32.461 3.665 1.00 16.00 C ATOM 39 CG1 ILE A 5 24.887 31.389 4.747 1.00 18.03 C ATOM 40 CG2 ILE A 5 24.470 33.816 4.263 1.00 17.59 C ATOM 41 CD1 ILE A 5 23.522 30.765 5.027 1.00 20.49 C ATOM 42 N AHIS A 6 23.224 34.086 1.266 0.50 14.20 N ATOM 43 N BHIS A 6 23.274 34.014 1.074 0.50 16.67 N ATOM 44 CA AHIS A 6 23.209 35.260 0.397 0.50 14.45 C ATOM 45 CA BHIS A 6 23.503 35.160 0.168 0.50 17.84 C ATOM 46 C AHIS A 6 23.812 36.444 1.141 0.50 14.31 C ATOM 47 C BHIS A 6 23.912 36.330 1.048 0.50 16.77 C ATOM 48 O AHIS A 6 23.166 36.915 2.118 0.50 15.33 O ATOM 49 O BHIS A 6 23.254 36.640 2.072 0.50 17.88 O ATOM 50 CB AHIS A 6 21.751 35.617 -0.024 0.50 14.98 C ATOM 51 CB BHIS A 6 22.288 35.441 -0.746 0.50 21.08 C ATOM 52 CG AHIS A 6 21.706 36.884 -0.816 0.50 15.04 C ATOM 53 CG BHIS A 6 22.340 34.470 -1.906 0.50 24.32 C ATOM 54 ND1AHIS A 6 22.017 36.971 -2.134 0.50 16.10 N ATOM 55 ND1BHIS A 6 21.839 33.188 -1.917 0.50 25.17 N ATOM 56 CD2AHIS A 6 21.382 38.136 -0.410 0.50 16.04 C ATOM 57 CD2BHIS A 6 22.959 34.649 -3.112 0.50 24.89 C ATOM 58 CE1AHIS A 6 21.896 38.232 -2.528 0.50 15.49 C ATOM 59 CE1BHIS A 6 22.106 32.643 -3.097 0.50 25.92 C ATOM 60 NE2AHIS A 6 21.539 38.966 -1.497 0.50 15.68 N ATOM 61 NE2BHIS A 6 22.800 33.502 -3.827 0.50 26.06 N ATOM 62 N ALEU A 7 24.994 36.916 0.777 0.50 12.47 N ATOM 63 N BLEU A 7 25.049 36.926 0.732 0.50 13.88 N ATOM 64 CA LEU A 7 25.574 38.061 1.494 1.00 12.40 C ATOM 65 C LEU A 7 25.330 39.373 0.782 1.00 13.24 C ATOM 66 O LEU A 7 25.161 39.412 -0.444 1.00 14.99 O ATOM 67 CB LEU A 7 27.099 37.857 1.598 1.00 11.31 C ATOM 68 CG LEU A 7 27.558 36.609 2.362 1.00 11.75 C ATOM 69 CD1 LEU A 7 29.082 36.516 2.268 1.00 12.20 C ATOM 70 CD2 LEU A 7 27.079 36.752 3.805 1.00 12.86 C ATOM 71 N THR A 8 25.419 40.434 1.561 1.00 13.46 N ATOM 72 CA THR A 8 25.457 41.807 1.037 1.00 14.06 C ATOM 73 C THR A 8 26.594 42.530 1.702 1.00 13.52 C ATOM 74 O THR A 8 27.142 42.063 2.682 1.00 12.78 O ATOM 75 CB THR A 8 24.093 42.610 1.254 1.00 14.54 C ATOM 76 OG1 THR A 8 24.005 42.860 2.687 1.00 14.25 O ATOM 77 CG2 THR A 8 22.905 41.853 0.697 1.00 14.70 C ATOM 78 N ASP A 9 26.892 43.714 1.150 1.00 14.17 N ATOM 79 CA ASP A 9 27.926 44.559 1.745 1.00 15.20 C ATOM 80 C ASP A 9 27.605 44.869 3.223 1.00 14.96 C ATOM 81 O ASP A 9 28.482 44.846 4.093 1.00 14.69 O ATOM 82 CB ASP A 9 28.201 45.815 0.929 1.00 17.36 C ATOM 83 CG ASP A 9 29.028 45.578 -0.331 1.00 19.48 C ATOM 84 OD1 ASP A 9 28.836 46.359 -1.294 1.00 21.20 O ATOM 85 OD2 ASP A 9 29.843 44.606 -0.368 1.00 19.52 O ATOM 86 N ASP A 10 26.354 45.192 3.500 1.00 14.77 N ATOM 87 CA ASP A 10 25.970 45.537 4.868 1.00 15.43 C ATOM 88 C ASP A 10 25.875 44.351 5.800 1.00 15.15 C ATOM 89 O ASP A 10 26.087 44.573 7.016 1.00 17.24 O ATOM 90 CB ASP A 10 24.603 46.236 4.902 1.00 15.60 C ATOM 91 CG ASP A 10 24.631 47.626 4.316 1.00 17.69 C ATOM 92 OD1 ASP A 10 23.552 48.046 3.857 1.00 18.65 O ATOM 93 OD2 ASP A 10 25.688 48.266 4.284 1.00 17.68 O ATOM 94 N SER A 11 25.599 43.185 5.285 1.00 14.29 N ATOM 95 CA SER A 11 25.473 42.022 6.151 1.00 14.24 C ATOM 96 C SER A 11 26.792 41.291 6.383 1.00 13.53 C ATOM 97 O SER A 11 26.799 40.365 7.215 1.00 13.75 O ATOM 98 CB SER A 11 24.415 41.069 5.651 1.00 14.74 C ATOM 99 OG SER A 11 24.842 40.228 4.595 1.00 16.10 O ATOM 100 N PHE A 12 27.829 41.695 5.688 1.00 13.49 N ATOM 101 CA PHE A 12 29.099 40.933 5.759 1.00 13.10 C ATOM 102 C PHE A 12 29.645 40.748 7.165 1.00 12.77 C ATOM 103 O PHE A 12 30.072 39.616 7.530 1.00 12.54 O ATOM 104 CB PHE A 12 30.098 41.557 4.781 1.00 13.34 C ATOM 105 CG PHE A 12 31.198 40.585 4.370 1.00 14.53 C ATOM 106 CD1 PHE A 12 31.018 39.815 3.237 1.00 14.81 C ATOM 107 CD2 PHE A 12 32.361 40.512 5.103 1.00 15.14 C ATOM 108 CE1 PHE A 12 32.027 38.934 2.830 1.00 16.88 C ATOM 109 CE2 PHE A 12 33.396 39.631 4.718 1.00 15.90 C ATOM 110 CZ PHE A 12 33.194 38.843 3.569 1.00 15.90 C ATOM 111 N ASP A 13 29.678 41.854 7.928 1.00 12.51 N ATOM 112 CA ASP A 13 30.284 41.748 9.265 1.00 15.59 C ATOM 113 C ASP A 13 29.469 40.770 10.123 1.00 15.56 C ATOM 114 O ASP A 13 30.025 39.861 10.738 1.00 15.68 O ATOM 115 CB ASP A 13 30.347 43.160 9.875 1.00 19.09 C ATOM 116 CG ASP A 13 30.724 43.120 11.344 1.00 24.45 C ATOM 117 OD1 ASP A 13 29.952 43.444 12.268 1.00 28.65 O ATOM 118 OD2 ASP A 13 31.876 42.704 11.618 1.00 27.06 O ATOM 119 N THR A 14 28.183 40.973 10.177 1.00 14.97 N ATOM 120 CA THR A 14 27.293 40.140 10.978 1.00 15.48 C ATOM 121 C THR A 14 27.334 38.666 10.591 1.00 15.63 C ATOM 122 O THR A 14 27.340 37.786 11.453 1.00 15.60 O ATOM 123 CB THR A 14 25.790 40.636 10.866 1.00 15.81 C ATOM 124 OG1 THR A 14 25.759 42.020 11.288 1.00 17.67 O ATOM 125 CG2 THR A 14 24.779 39.741 11.614 1.00 16.68 C ATOM 126 N ASP A 15 27.296 38.408 9.265 1.00 13.34 N ATOM 127 CA ASP A 15 27.199 37.020 8.811 1.00 13.51 C ATOM 128 C ASP A 15 28.523 36.287 8.697 1.00 13.42 C ATOM 129 O ASP A 15 28.547 35.054 8.868 1.00 15.24 O ATOM 130 CB ASP A 15 26.537 36.983 7.405 1.00 14.64 C ATOM 131 CG ASP A 15 25.058 37.319 7.424 1.00 18.00 C ATOM 132 OD1 ASP A 15 24.557 37.630 6.322 1.00 20.58 O ATOM 133 OD2 ASP A 15 24.429 37.363 8.483 1.00 19.92 O ATOM 134 N VAL A 16 29.566 36.993 8.398 1.00 11.68 N ATOM 135 CA VAL A 16 30.879 36.363 8.141 1.00 11.15 C ATOM 136 C VAL A 16 31.831 36.654 9.285 1.00 11.18 C ATOM 137 O VAL A 16 32.400 35.661 9.800 1.00 11.31 O ATOM 138 CB VAL A 16 31.447 36.826 6.782 1.00 11.48 C ATOM 139 CG1 VAL A 16 32.817 36.213 6.498 1.00 11.71 C ATOM 140 CG2 VAL A 16 30.481 36.479 5.629 1.00 12.46 C ATOM 141 N LEU A 17 32.031 37.909 9.621 1.00 10.68 N ATOM 142 CA LEU A 17 33.084 38.203 10.586 1.00 12.88 C ATOM 143 C LEU A 17 32.761 37.703 11.989 1.00 13.68 C ATOM 144 O LEU A 17 33.688 37.310 12.719 1.00 13.80 O ATOM 145 CB LEU A 17 33.486 39.659 10.464 1.00 14.73 C ATOM 146 CG LEU A 17 33.956 40.160 9.085 1.00 16.37 C ATOM 147 CD1 LEU A 17 34.544 41.569 9.307 1.00 17.08 C ATOM 148 CD2 LEU A 17 35.017 39.223 8.541 1.00 17.02 C ATOM 149 N LYS A 18 31.486 37.640 12.298 1.00 13.46 N ATOM 150 CA LYS A 18 31.081 37.133 13.628 1.00 14.85 C ATOM 151 C LYS A 18 30.549 35.736 13.530 1.00 15.99 C ATOM 152 O LYS A 18 29.879 35.275 14.472 1.00 16.78 O ATOM 153 CB LYS A 18 30.038 38.137 14.184 1.00 17.08 C ATOM 154 CG LYS A 18 30.836 39.352 14.640 1.00 19.68 C ATOM 155 CD LYS A 18 30.337 40.702 14.460 1.00 23.81 C ATOM 156 CE LYS A 18 31.259 41.802 14.961 1.00 24.60 C ATOM 157 NZ LYS A 18 32.517 42.012 14.212 1.00 24.76 N ATOM 158 N ALA A 19 30.851 35.020 12.422 1.00 15.05 N ATOM 159 CA ALA A 19 30.364 33.655 12.255 1.00 15.02 C ATOM 160 C ALA A 19 30.972 32.709 13.295 1.00 14.79 C ATOM 161 O ALA A 19 32.090 32.873 13.739 1.00 14.02 O ATOM 162 CB ALA A 19 30.724 33.065 10.875 1.00 15.30 C ATOM 163 N ASP A 20 30.145 31.684 13.574 1.00 15.36 N ATOM 164 CA ASP A 20 30.660 30.591 14.430 1.00 17.32 C ATOM 165 C ASP A 20 31.286 29.548 13.504 1.00 19.00 C ATOM 166 O ASP A 20 30.536 29.074 12.611 1.00 23.43 O ATOM 167 CB ASP A 20 29.450 30.052 15.203 1.00 18.57 C ATOM 168 CG ASP A 20 29.806 29.030 16.240 1.00 20.00 C ATOM 169 OD1 ASP A 20 28.915 28.243 16.643 1.00 21.68 O ATOM 170 OD2 ASP A 20 30.949 29.001 16.711 1.00 22.14 O ATOM 171 N GLY A 21 32.511 29.171 13.557 1.00 19.06 N ATOM 172 CA GLY A 21 32.919 28.079 12.606 1.00 18.13 C ATOM 173 C GLY A 21 33.401 28.709 11.285 1.00 17.12 C ATOM 174 O GLY A 21 33.314 29.904 11.008 1.00 18.02 O ATOM 175 N ALA A 22 33.904 27.787 10.464 1.00 15.23 N ATOM 176 CA ALA A 22 34.544 28.218 9.195 1.00 14.16 C ATOM 177 C ALA A 22 33.486 28.594 8.194 1.00 12.92 C ATOM 178 O ALA A 22 32.452 27.923 8.145 1.00 13.79 O ATOM 179 CB ALA A 22 35.336 26.994 8.711 1.00 14.83 C ATOM 180 N ILE A 23 33.736 29.626 7.426 1.00 12.08 N ATOM 181 CA ILE A 23 32.783 30.040 6.369 1.00 10.46 C ATOM 182 C ILE A 23 33.583 30.266 5.094 1.00 10.02 C ATOM 183 O ILE A 23 34.567 31.001 5.117 1.00 10.16 O ATOM 184 CB ILE A 23 31.970 31.283 6.860 1.00 12.23 C ATOM 185 CG1AILE A 23 30.906 31.626 5.768 0.50 10.89 C ATOM 186 CG1BILE A 23 30.940 30.954 7.951 0.50 13.56 C ATOM 187 CG2AILE A 23 32.782 32.444 7.408 0.50 10.84 C ATOM 188 CG2BILE A 23 31.342 32.043 5.633 0.50 12.98 C ATOM 189 CD1AILE A 23 29.783 32.535 6.339 0.50 9.53 C ATOM 190 CD1BILE A 23 29.669 31.852 7.991 0.50 15.60 C ATOM 191 N LEU A 24 33.114 29.721 3.978 1.00 8.44 N ATOM 192 CA LEU A 24 33.785 29.852 2.683 1.00 7.85 C ATOM 193 C LEU A 24 32.958 30.889 1.883 1.00 9.05 C ATOM 194 O LEU A 24 31.755 30.609 1.708 1.00 11.52 O ATOM 195 CB LEU A 24 33.818 28.464 2.034 1.00 9.81 C ATOM 196 CG LEU A 24 34.477 28.439 0.625 1.00 10.54 C ATOM 197 CD1 LEU A 24 35.962 28.722 0.715 1.00 11.74 C ATOM 198 CD2 LEU A 24 34.190 27.053 0.016 1.00 11.91 C ATOM 199 N VAL A 25 33.599 31.917 1.389 1.00 7.73 N ATOM 200 CA VAL A 25 32.859 32.997 0.714 1.00 7.72 C ATOM 201 C VAL A 25 33.271 32.975 -0.769 1.00 9.49 C ATOM 202 O VAL A 25 34.480 33.087 -1.047 1.00 10.05 O ATOM 203 CB VAL A 25 33.089 34.369 1.368 1.00 8.36 C ATOM 204 CG1 VAL A 25 32.361 35.403 0.557 1.00 8.76 C ATOM 205 CG2 VAL A 25 32.644 34.345 2.821 1.00 8.36 C ATOM 206 N ASP A 26 32.297 32.856 -1.644 1.00 8.75 N ATOM 207 CA ASP A 26 32.520 32.871 -3.108 1.00 9.06 C ATOM 208 C ASP A 26 32.197 34.250 -3.668 1.00 10.31 C ATOM 209 O ASP A 26 31.007 34.641 -3.565 1.00 11.97 O ATOM 210 CB ASP A 26 31.619 31.811 -3.710 1.00 9.90 C ATOM 211 CG ASP A 26 31.571 31.778 -5.235 1.00 13.37 C ATOM 212 OD1 ASP A 26 30.538 31.381 -5.797 1.00 14.34 O ATOM 213 OD2 ASP A 26 32.575 32.139 -5.860 1.00 15.28 O ATOM 214 N PHE A 27 33.138 34.929 -4.262 1.00 9.89 N ATOM 215 CA PHE A 27 32.981 36.242 -4.921 1.00 11.01 C ATOM 216 C PHE A 27 32.738 35.935 -6.408 1.00 12.27 C ATOM 217 O PHE A 27 33.564 35.282 -7.054 1.00 12.96 O ATOM 218 CB PHE A 27 34.230 37.080 -4.680 1.00 11.31 C ATOM 219 CG PHE A 27 34.327 37.604 -3.278 1.00 13.55 C ATOM 220 CD1 PHE A 27 33.871 38.881 -2.952 1.00 14.15 C ATOM 221 CD2 PHE A 27 34.865 36.779 -2.287 1.00 14.05 C ATOM 222 CE1 PHE A 27 34.000 39.377 -1.651 1.00 15.13 C ATOM 223 CE2 PHE A 27 34.963 37.240 -0.976 1.00 15.37 C ATOM 224 CZ PHE A 27 34.500 38.530 -0.650 1.00 14.70 C ATOM 225 N TRP A 28 31.585 36.341 -6.910 1.00 12.01 N ATOM 226 CA TRP A 28 31.164 35.958 -8.285 1.00 14.29 C ATOM 227 C TRP A 28 30.376 37.102 -8.923 1.00 14.75 C ATOM 228 O TRP A 28 30.045 38.100 -8.308 1.00 14.36 O ATOM 229 CB TRP A 28 30.355 34.649 -8.238 1.00 15.01 C ATOM 230 CG TRP A 28 28.981 34.857 -7.680 1.00 16.81 C ATOM 231 CD1 TRP A 28 28.653 35.218 -6.401 1.00 16.45 C ATOM 232 CD2 TRP A 28 27.746 34.811 -8.398 1.00 18.37 C ATOM 233 NE1 TRP A 28 27.295 35.358 -6.253 1.00 18.08 N ATOM 234 CE2 TRP A 28 26.724 35.127 -7.496 1.00 19.33 C ATOM 235 CE3 TRP A 28 27.430 34.524 -9.725 1.00 20.65 C ATOM 236 CZ2 TRP A 28 25.384 35.178 -7.858 1.00 20.07 C ATOM 237 CZ3 TRP A 28 26.095 34.583 -10.085 1.00 20.67 C ATOM 238 CH2 TRP A 28 25.077 34.876 -9.187 1.00 21.38 C ATOM 239 N ALA A 29 30.038 36.848 -10.185 1.00 16.64 N ATOM 240 CA ALA A 29 29.211 37.767 -11.005 1.00 18.79 C ATOM 241 C ALA A 29 28.628 36.901 -12.122 1.00 20.47 C ATOM 242 O ALA A 29 29.160 35.860 -12.517 1.00 19.75 O ATOM 243 CB ALA A 29 29.995 38.903 -11.591 1.00 17.90 C ATOM 244 N GLU A 30 27.476 37.381 -12.590 1.00 23.83 N ATOM 245 CA GLU A 30 26.743 36.601 -13.583 1.00 27.43 C ATOM 246 C GLU A 30 27.450 36.460 -14.930 1.00 25.88 C ATOM 247 O GLU A 30 27.282 35.429 -15.592 1.00 26.00 O ATOM 248 CB GLU A 30 25.320 37.161 -13.789 1.00 32.09 C ATOM 249 CG GLU A 30 24.288 36.065 -13.452 1.00 37.84 C ATOM 250 CD GLU A 30 23.051 36.496 -12.731 1.00 42.35 C ATOM 251 OE1 GLU A 30 22.192 37.253 -13.233 1.00 45.04 O ATOM 252 OE2 GLU A 30 22.954 35.959 -11.597 1.00 44.11 O ATOM 253 N TRP A 31 28.229 37.428 -15.272 1.00 25.14 N ATOM 254 CA TRP A 31 28.977 37.467 -16.522 1.00 24.91 C ATOM 255 C TRP A 31 30.202 36.571 -16.434 1.00 25.00 C ATOM 256 O TRP A 31 30.873 36.415 -17.457 1.00 25.76 O ATOM 257 CB TRP A 31 29.458 38.875 -16.817 1.00 26.12 C ATOM 258 CG TRP A 31 29.976 39.705 -15.701 1.00 27.47 C ATOM 259 CD1 TRP A 31 29.258 40.617 -14.957 1.00 27.56 C ATOM 260 CD2 TRP A 31 31.312 39.768 -15.179 1.00 27.86 C ATOM 261 NE1 TRP A 31 30.055 41.230 -14.014 1.00 27.19 N ATOM 262 CE2 TRP A 31 31.313 40.737 -14.130 1.00 28.18 C ATOM 263 CE3 TRP A 31 32.488 39.082 -15.497 1.00 28.42 C ATOM 264 CZ2 TRP A 31 32.456 41.032 -13.393 1.00 27.99 C ATOM 265 CZ3 TRP A 31 33.623 39.373 -14.764 1.00 28.14 C ATOM 266 CH2 TRP A 31 33.601 40.333 -13.748 1.00 28.64 C ATOM 267 N CYS A 32 30.492 36.041 -15.250 1.00 22.22 N ATOM 268 CA CYS A 32 31.749 35.264 -15.067 1.00 20.24 C ATOM 269 C CYS A 32 31.532 33.814 -15.354 1.00 19.15 C ATOM 270 O CYS A 32 30.902 33.016 -14.643 1.00 18.30 O ATOM 271 CB CYS A 32 32.291 35.603 -13.649 1.00 18.86 C ATOM 272 SG CYS A 32 33.555 34.457 -13.062 1.00 17.52 S ATOM 273 N GLY A 33 32.097 33.354 -16.498 1.00 18.02 N ATOM 274 CA GLY A 33 31.923 31.972 -16.915 1.00 19.03 C ATOM 275 C GLY A 33 32.459 30.955 -15.935 1.00 18.76 C ATOM 276 O GLY A 33 31.737 30.037 -15.501 1.00 20.52 O ATOM 277 N PRO A 34 33.727 31.073 -15.538 1.00 18.13 N ATOM 278 CA PRO A 34 34.309 30.133 -14.577 1.00 17.65 C ATOM 279 C PRO A 34 33.551 30.135 -13.246 1.00 17.40 C ATOM 280 O PRO A 34 33.583 29.113 -12.542 1.00 16.57 O ATOM 281 CB PRO A 34 35.769 30.547 -14.439 1.00 17.81 C ATOM 282 CG PRO A 34 36.037 31.217 -15.761 1.00 19.11 C ATOM 283 CD PRO A 34 34.728 32.036 -16.012 1.00 18.53 C ATOM 284 N CYS A 35 32.981 31.281 -12.915 1.00 17.05 N ATOM 285 CA CYS A 35 32.187 31.344 -11.645 1.00 16.98 C ATOM 286 C CYS A 35 30.993 30.419 -11.728 1.00 18.73 C ATOM 287 O CYS A 35 30.668 29.740 -10.780 1.00 17.87 O ATOM 288 CB CYS A 35 31.674 32.747 -11.366 1.00 16.47 C ATOM 289 SG CYS A 35 32.923 33.992 -11.125 1.00 17.50 S ATOM 290 N LYS A 36 30.305 30.469 -12.886 1.00 20.01 N ATOM 291 CA LYS A 36 29.144 29.598 -13.084 1.00 22.48 C ATOM 292 C LYS A 36 29.594 28.167 -13.165 1.00 22.05 C ATOM 293 O LYS A 36 28.882 27.273 -12.653 1.00 21.89 O ATOM 294 CB LYS A 36 28.263 30.084 -14.256 1.00 25.07 C ATOM 295 CG LYS A 36 27.682 31.463 -13.811 1.00 29.51 C ATOM 296 CD LYS A 36 26.744 32.109 -14.816 1.00 33.00 C ATOM 297 CE LYS A 36 27.465 32.446 -16.116 1.00 35.46 C ATOM 298 NZ LYS A 36 26.497 32.984 -17.135 1.00 37.89 N ATOM 299 N MET A 37 30.763 27.876 -13.678 1.00 22.43 N ATOM 300 CA MET A 37 31.237 26.464 -13.698 1.00 23.47 C ATOM 301 C MET A 37 31.420 25.847 -12.336 1.00 21.76 C ATOM 302 O MET A 37 31.286 24.633 -12.113 1.00 21.64 O ATOM 303 CB MET A 37 32.546 26.467 -14.523 1.00 27.28 C ATOM 304 CG MET A 37 32.706 25.229 -15.353 1.00 32.69 C ATOM 305 SD MET A 37 33.860 25.627 -16.719 1.00 37.76 S ATOM 306 CE MET A 37 35.422 25.696 -15.895 1.00 35.87 C ATOM 307 N ILE A 38 31.814 26.635 -11.313 1.00 19.09 N ATOM 308 CA ILE A 38 32.052 26.055 -9.983 1.00 17.03 C ATOM 309 C ILE A 38 30.802 26.102 -9.113 1.00 15.22 C ATOM 310 O ILE A 38 30.824 25.543 -8.005 1.00 14.78 O ATOM 311 CB ILE A 38 33.274 26.678 -9.220 1.00 17.68 C ATOM 312 CG1 ILE A 38 32.962 28.149 -8.873 1.00 17.93 C ATOM 313 CG2 ILE A 38 34.586 26.463 -10.041 1.00 18.86 C ATOM 314 CD1 ILE A 38 34.024 28.763 -7.912 1.00 20.51 C ATOM 315 N ALA A 39 29.755 26.788 -9.558 1.00 15.45 N ATOM 316 CA ALA A 39 28.531 26.837 -8.702 1.00 15.05 C ATOM 317 C ALA A 39 28.045 25.493 -8.258 1.00 16.18 C ATOM 318 O ALA A 39 27.771 25.243 -7.052 1.00 14.78 O ATOM 319 CB ALA A 39 27.453 27.672 -9.399 1.00 16.65 C ATOM 320 N PRO A 40 27.905 24.467 -9.129 1.00 15.41 N ATOM 321 CA PRO A 40 27.440 23.173 -8.654 1.00 15.14 C ATOM 322 C PRO A 40 28.355 22.518 -7.664 1.00 14.74 C ATOM 323 O PRO A 40 27.918 21.732 -6.807 1.00 15.66 O ATOM 324 CB PRO A 40 27.374 22.260 -9.914 1.00 16.37 C ATOM 325 CG PRO A 40 27.364 23.253 -11.016 1.00 17.16 C ATOM 326 CD PRO A 40 28.136 24.515 -10.576 1.00 16.10 C ATOM 327 N ILE A 41 29.667 22.780 -7.864 1.00 13.63 N ATOM 328 CA ILE A 41 30.634 22.130 -6.925 1.00 14.40 C ATOM 329 C ILE A 41 30.441 22.746 -5.538 1.00 12.89 C ATOM 330 O ILE A 41 30.553 21.978 -4.583 1.00 14.10 O ATOM 331 CB ILE A 41 32.094 22.367 -7.392 1.00 15.66 C ATOM 332 CG1 ILE A 41 32.272 21.737 -8.808 1.00 16.98 C ATOM 333 CG2 ILE A 41 33.141 21.918 -6.344 1.00 17.36 C ATOM 334 CD1 ILE A 41 33.639 22.193 -9.428 1.00 17.51 C ATOM 335 N LEU A 42 30.140 24.023 -5.469 1.00 12.45 N ATOM 336 CA LEU A 42 29.875 24.631 -4.150 1.00 13.12 C ATOM 337 C LEU A 42 28.632 24.012 -3.501 1.00 14.26 C ATOM 338 O LEU A 42 28.556 23.833 -2.277 1.00 13.56 O ATOM 339 CB LEU A 42 29.777 26.151 -4.301 1.00 14.88 C ATOM 340 CG LEU A 42 31.108 26.853 -4.547 1.00 17.19 C ATOM 341 CD1 LEU A 42 30.847 28.363 -4.712 1.00 19.17 C ATOM 342 CD2 LEU A 42 32.043 26.610 -3.384 1.00 17.60 C ATOM 343 N ASP A 43 27.614 23.697 -4.291 1.00 13.25 N ATOM 344 CA ASP A 43 26.436 23.023 -3.719 1.00 14.20 C ATOM 345 C ASP A 43 26.773 21.658 -3.164 1.00 14.45 C ATOM 346 O ASP A 43 26.298 21.269 -2.111 1.00 14.66 O ATOM 347 CB ASP A 43 25.347 22.853 -4.793 1.00 15.32 C ATOM 348 CG ASP A 43 24.669 24.136 -5.146 1.00 17.51 C ATOM 349 OD1 ASP A 43 24.202 24.189 -6.311 1.00 19.16 O ATOM 350 OD2 ASP A 43 24.534 25.032 -4.296 1.00 16.41 O ATOM 351 N GLU A 44 27.602 20.898 -3.914 1.00 14.18 N ATOM 352 CA GLU A 44 28.024 19.586 -3.382 1.00 15.12 C ATOM 353 C GLU A 44 28.805 19.702 -2.086 1.00 15.75 C ATOM 354 O GLU A 44 28.620 18.913 -1.158 1.00 16.09 O ATOM 355 CB GLU A 44 28.955 18.888 -4.383 1.00 17.56 C ATOM 356 CG GLU A 44 28.326 18.714 -5.779 1.00 19.86 C ATOM 357 CD GLU A 44 29.239 17.976 -6.722 1.00 23.23 C ATOM 358 OE1 GLU A 44 29.292 16.752 -6.688 1.00 25.21 O ATOM 359 OE2 GLU A 44 29.904 18.712 -7.486 1.00 24.23 O ATOM 360 N ILE A 45 29.699 20.697 -2.061 1.00 14.65 N ATOM 361 CA ILE A 45 30.540 20.890 -0.844 1.00 15.35 C ATOM 362 C ILE A 45 29.646 21.324 0.307 1.00 14.09 C ATOM 363 O ILE A 45 29.876 20.931 1.457 1.00 14.26 O ATOM 364 CB ILE A 45 31.663 21.938 -1.165 1.00 17.37 C ATOM 365 CG1 ILE A 45 32.836 21.317 -1.947 1.00 18.51 C ATOM 366 CG2 ILE A 45 32.184 22.704 0.090 1.00 18.76 C ATOM 367 CD1 ILE A 45 33.458 20.023 -1.445 1.00 19.79 C ATOM 368 N ALA A 46 28.680 22.180 0.041 1.00 13.61 N ATOM 369 CA ALA A 46 27.741 22.632 1.117 1.00 14.18 C ATOM 370 C ALA A 46 27.034 21.437 1.762 1.00 16.26 C ATOM 371 O ALA A 46 26.827 21.425 3.005 1.00 16.75 O ATOM 372 CB ALA A 46 26.770 23.670 0.573 1.00 13.19 C ATOM 373 N ASP A 47 26.633 20.487 0.934 1.00 16.20 N ATOM 374 CA ASP A 47 25.998 19.256 1.488 1.00 18.29 C ATOM 375 C ASP A 47 27.007 18.387 2.223 1.00 18.48 C ATOM 376 O ASP A 47 26.779 17.932 3.366 1.00 20.01 O ATOM 377 CB ASP A 47 25.239 18.534 0.367 1.00 20.25 C ATOM 378 CG AASP A 47 23.877 19.132 0.076 0.50 19.52 C ATOM 379 CG BASP A 47 24.860 17.102 0.699 0.50 22.33 C ATOM 380 OD1AASP A 47 23.048 19.368 0.965 0.50 19.93 O ATOM 381 OD1BASP A 47 25.027 16.146 -0.078 0.50 24.28 O ATOM 382 OD2AASP A 47 23.521 19.424 -1.092 0.50 20.78 O ATOM 383 OD2BASP A 47 24.356 16.903 1.815 0.50 24.21 O ATOM 384 N GLU A 48 28.133 18.128 1.612 1.00 18.19 N ATOM 385 CA GLU A 48 29.133 17.236 2.160 1.00 20.03 C ATOM 386 C GLU A 48 29.727 17.767 3.452 1.00 20.36 C ATOM 387 O GLU A 48 30.065 16.922 4.320 1.00 19.98 O ATOM 388 CB GLU A 48 30.288 16.881 1.222 1.00 22.08 C ATOM 389 CG AGLU A 48 29.878 16.097 0.001 0.50 23.22 C ATOM 390 CG BGLU A 48 31.372 15.982 1.785 0.50 24.50 C ATOM 391 CD AGLU A 48 30.874 15.856 -1.084 0.50 24.57 C ATOM 392 CD BGLU A 48 32.387 15.377 0.888 0.50 25.93 C ATOM 393 OE1AGLU A 48 30.500 15.474 -2.178 0.50 25.49 O ATOM 394 OE1BGLU A 48 33.384 14.801 1.307 0.50 26.62 O ATOM 395 OE2AGLU A 48 32.049 16.115 -0.781 0.50 25.61 O ATOM 396 OE2BGLU A 48 32.104 15.515 -0.318 0.50 27.54 O ATOM 397 N TYR A 49 29.815 19.077 3.589 1.00 18.36 N ATOM 398 CA TYR A 49 30.521 19.621 4.781 1.00 19.05 C ATOM 399 C TYR A 49 29.521 20.270 5.720 1.00 19.83 C ATOM 400 O TYR A 49 29.927 21.012 6.600 1.00 20.19 O ATOM 401 CB TYR A 49 31.633 20.574 4.366 1.00 18.28 C ATOM 402 CG TYR A 49 32.898 19.961 3.818 1.00 19.11 C ATOM 403 CD1 TYR A 49 32.952 19.443 2.543 1.00 20.12 C ATOM 404 CD2 TYR A 49 34.093 19.919 4.573 1.00 20.77 C ATOM 405 CE1 TYR A 49 34.097 18.868 2.024 1.00 21.72 C ATOM 406 CE2 TYR A 49 35.275 19.347 4.060 1.00 20.41 C ATOM 407 CZ TYR A 49 35.274 18.844 2.787 1.00 22.29 C ATOM 408 OH TYR A 49 36.397 18.294 2.200 1.00 23.76 O ATOM 409 N GLN A 50 28.257 19.959 5.495 1.00 21.00 N ATOM 410 CA GLN A 50 27.179 20.532 6.346 1.00 23.89 C ATOM 411 C GLN A 50 27.481 20.263 7.806 1.00 24.87 C ATOM 412 O GLN A 50 27.843 19.159 8.243 1.00 25.36 O ATOM 413 CB GLN A 50 25.855 19.960 5.899 1.00 26.01 C ATOM 414 CG GLN A 50 24.635 20.600 6.512 1.00 29.12 C ATOM 415 CD GLN A 50 23.410 19.936 5.876 1.00 31.71 C ATOM 416 OE1 GLN A 50 23.517 18.792 5.390 1.00 34.06 O ATOM 417 NE2 GLN A 50 22.329 20.705 5.892 1.00 31.60 N ATOM 418 N GLY A 51 27.342 21.298 8.614 1.00 25.01 N ATOM 419 CA GLY A 51 27.738 21.106 10.023 1.00 26.18 C ATOM 420 C GLY A 51 29.189 21.425 10.288 1.00 27.45 C ATOM 421 O GLY A 51 29.497 21.693 11.469 1.00 29.49 O ATOM 422 N LYS A 52 30.113 21.446 9.355 1.00 26.17 N ATOM 423 CA LYS A 52 31.510 21.764 9.590 1.00 25.10 C ATOM 424 C LYS A 52 31.934 23.047 8.862 1.00 22.67 C ATOM 425 O LYS A 52 33.017 23.598 9.177 1.00 23.03 O ATOM 426 CB LYS A 52 32.459 20.704 8.966 1.00 29.07 C ATOM 427 CG LYS A 52 31.968 19.269 9.129 1.00 33.45 C ATOM 428 CD LYS A 52 32.647 18.337 8.103 1.00 35.54 C ATOM 429 CE LYS A 52 31.932 16.979 8.126 1.00 37.91 C ATOM 430 NZ LYS A 52 31.800 16.419 6.753 1.00 38.70 N ATOM 431 N LEU A 53 31.106 23.442 7.898 1.00 18.68 N ATOM 432 CA LEU A 53 31.450 24.605 7.068 1.00 16.96 C ATOM 433 C LEU A 53 30.151 25.264 6.592 1.00 15.56 C ATOM 434 O LEU A 53 29.272 24.454 6.279 1.00 16.53 O ATOM 435 CB LEU A 53 32.228 24.022 5.866 1.00 17.08 C ATOM 436 CG LEU A 53 32.651 25.042 4.832 1.00 18.17 C ATOM 437 CD1 LEU A 53 33.842 25.892 5.310 1.00 18.51 C ATOM 438 CD2 LEU A 53 33.022 24.328 3.525 1.00 19.30 C ATOM 439 N THR A 54 30.109 26.568 6.584 1.00 13.07 N ATOM 440 CA THR A 54 29.052 27.341 5.928 1.00 12.96 C ATOM 441 C THR A 54 29.579 27.892 4.598 1.00 13.26 C ATOM 442 O THR A 54 30.717 28.358 4.553 1.00 13.02 O ATOM 443 CB THR A 54 28.557 28.544 6.830 1.00 16.39 C ATOM 444 OG1 THR A 54 28.055 27.907 8.061 1.00 18.27 O ATOM 445 CG2 THR A 54 27.431 29.360 6.198 1.00 18.67 C ATOM 446 N VAL A 55 28.769 27.770 3.550 1.00 11.70 N ATOM 447 CA VAL A 55 29.222 28.360 2.267 1.00 11.55 C ATOM 448 C VAL A 55 28.350 29.584 1.997 1.00 11.22 C ATOM 449 O VAL A 55 27.137 29.566 2.233 1.00 12.29 O ATOM 450 CB VAL A 55 29.093 27.286 1.166 1.00 12.00 C ATOM 451 CG1 VAL A 55 29.543 27.820 -0.190 1.00 13.57 C ATOM 452 CG2 VAL A 55 29.809 25.980 1.537 1.00 12.95 C ATOM 453 N ALA A 56 28.967 30.634 1.486 1.00 8.60 N ATOM 454 CA ALA A 56 28.230 31.880 1.209 1.00 8.68 C ATOM 455 C ALA A 56 28.670 32.478 -0.123 1.00 10.46 C ATOM 456 O ALA A 56 29.781 32.160 -0.565 1.00 10.51 O ATOM 457 CB ALA A 56 28.512 32.816 2.410 1.00 10.56 C ATOM 458 N LYS A 57 27.846 33.338 -0.695 1.00 11.12 N ATOM 459 CA LYS A 57 28.140 34.021 -1.952 1.00 12.26 C ATOM 460 C LYS A 57 27.946 35.530 -1.868 1.00 12.22 C ATOM 461 O LYS A 57 26.974 35.978 -1.228 1.00 13.38 O ATOM 462 CB LYS A 57 27.194 33.542 -3.092 1.00 14.21 C ATOM 463 CG LYS A 57 27.596 32.160 -3.606 1.00 17.04 C ATOM 464 CD LYS A 57 26.558 31.676 -4.639 1.00 18.97 C ATOM 465 CE LYS A 57 27.070 30.401 -5.313 1.00 21.48 C ATOM 466 NZ LYS A 57 26.036 29.830 -6.273 1.00 23.94 N ATOM 467 N LEU A 58 28.826 36.221 -2.583 1.00 9.80 N ATOM 468 CA LEU A 58 28.691 37.690 -2.664 1.00 10.88 C ATOM 469 C LEU A 58 28.857 38.050 -4.145 1.00 13.04 C ATOM 470 O LEU A 58 29.933 37.847 -4.690 1.00 11.67 O ATOM 471 CB LEU A 58 29.665 38.408 -1.747 1.00 11.30 C ATOM 472 CG LEU A 58 29.460 39.945 -1.761 1.00 12.68 C ATOM 473 CD1ALEU A 58 29.506 40.469 -0.336 0.50 11.88 C ATOM 474 CD1BLEU A 58 28.350 40.432 -0.847 0.50 11.43 C ATOM 475 CD2ALEU A 58 30.461 40.624 -2.663 0.50 11.17 C ATOM 476 CD2BLEU A 58 30.779 40.575 -1.341 0.50 13.77 C ATOM 477 N ASN A 59 27.733 38.539 -4.680 1.00 12.95 N ATOM 478 CA ASN A 59 27.741 38.998 -6.102 1.00 14.64 C ATOM 479 C ASN A 59 28.373 40.374 -6.128 1.00 15.71 C ATOM 480 O ASN A 59 27.835 41.349 -5.540 1.00 16.49 O ATOM 481 CB ASN A 59 26.271 38.978 -6.564 1.00 15.92 C ATOM 482 CG ASN A 59 26.208 39.429 -8.032 1.00 17.45 C ATOM 483 OD1 ASN A 59 26.661 40.532 -8.311 1.00 18.79 O ATOM 484 ND2 ASN A 59 25.700 38.534 -8.850 1.00 21.56 N ATOM 485 N ILE A 60 29.501 40.517 -6.826 1.00 15.51 N ATOM 486 CA ILE A 60 30.230 41.784 -6.828 1.00 17.36 C ATOM 487 C ILE A 60 29.594 42.892 -7.703 1.00 16.71 C ATOM 488 O ILE A 60 30.062 44.009 -7.506 1.00 18.88 O ATOM 489 CB ILE A 60 31.732 41.539 -7.247 1.00 16.96 C ATOM 490 CG1 ILE A 60 31.791 40.998 -8.707 1.00 18.62 C ATOM 491 CG2 ILE A 60 32.426 40.634 -6.195 1.00 17.73 C ATOM 492 CD1 ILE A 60 33.206 41.362 -9.299 1.00 21.03 C ATOM 493 N ASP A 61 28.660 42.559 -8.533 1.00 17.84 N ATOM 494 CA ASP A 61 27.982 43.600 -9.348 1.00 19.93 C ATOM 495 C ASP A 61 26.996 44.318 -8.413 1.00 20.41 C ATOM 496 O ASP A 61 26.880 45.548 -8.474 1.00 21.40 O ATOM 497 CB ASP A 61 27.224 43.002 -10.515 1.00 20.73 C ATOM 498 CG ASP A 61 28.155 42.578 -11.643 1.00 22.29 C ATOM 499 OD1 ASP A 61 29.275 43.023 -11.776 1.00 24.32 O ATOM 500 OD2 ASP A 61 27.652 41.731 -12.396 1.00 25.39 O ATOM 501 N GLN A 62 26.348 43.477 -7.609 1.00 20.64 N ATOM 502 CA GLN A 62 25.316 44.023 -6.688 1.00 20.92 C ATOM 503 C GLN A 62 25.887 44.593 -5.422 1.00 20.79 C ATOM 504 O GLN A 62 25.228 45.439 -4.768 1.00 21.69 O ATOM 505 CB GLN A 62 24.305 42.932 -6.357 1.00 23.27 C ATOM 506 CG GLN A 62 23.513 42.535 -7.599 1.00 26.91 C ATOM 507 CD GLN A 62 22.927 41.163 -7.442 1.00 29.51 C ATOM 508 OE1 GLN A 62 22.889 40.574 -6.367 1.00 30.66 O ATOM 509 NE2 GLN A 62 22.437 40.593 -8.558 1.00 32.21 N ATOM 510 N ASN A 63 27.059 44.181 -4.989 1.00 18.99 N ATOM 511 CA ASN A 63 27.725 44.603 -3.750 1.00 17.84 C ATOM 512 C ASN A 63 29.180 44.894 -4.070 1.00 19.71 C ATOM 513 O ASN A 63 30.044 44.018 -3.875 1.00 19.31 O ATOM 514 CB ASN A 63 27.592 43.470 -2.724 1.00 16.90 C ATOM 515 CG ASN A 63 26.143 43.165 -2.397 1.00 16.09 C ATOM 516 OD1 ASN A 63 25.615 43.912 -1.540 1.00 16.23 O ATOM 517 ND2 ASN A 63 25.548 42.140 -2.957 1.00 15.51 N ATOM 518 N PRO A 64 29.452 46.060 -4.566 1.00 21.61 N ATOM 519 CA PRO A 64 30.824 46.384 -4.999 1.00 23.16 C ATOM 520 C PRO A 64 31.760 46.805 -3.907 1.00 23.19 C ATOM 521 O PRO A 64 32.952 47.008 -4.208 1.00 25.21 O ATOM 522 CB PRO A 64 30.589 47.552 -5.961 1.00 23.16 C ATOM 523 CG PRO A 64 29.371 48.241 -5.391 1.00 23.54 C ATOM 524 CD PRO A 64 28.450 47.059 -5.018 1.00 22.42 C ATOM 525 N GLY A 65 31.322 46.971 -2.677 1.00 22.26 N ATOM 526 CA GLY A 65 32.139 47.479 -1.593 1.00 21.33 C ATOM 527 C GLY A 65 33.026 46.472 -0.910 1.00 21.65 C ATOM 528 O GLY A 65 34.080 46.911 -0.398 1.00 23.20 O ATOM 529 N THR A 66 32.689 45.181 -0.915 1.00 18.95 N ATOM 530 CA THR A 66 33.471 44.241 -0.136 1.00 19.29 C ATOM 531 C THR A 66 34.785 43.766 -0.811 1.00 18.41 C ATOM 532 O THR A 66 35.771 43.733 -0.049 1.00 17.22 O ATOM 533 CB THR A 66 32.665 42.975 0.357 1.00 19.44 C ATOM 534 OG1 THR A 66 31.598 43.518 1.177 1.00 19.00 O ATOM 535 CG2 THR A 66 33.500 41.987 1.203 1.00 19.24 C ATOM 536 N ALA A 67 34.711 43.426 -2.064 1.00 18.41 N ATOM 537 CA ALA A 67 35.904 42.817 -2.726 1.00 20.02 C ATOM 538 C ALA A 67 37.179 43.665 -2.537 1.00 21.19 C ATOM 539 O ALA A 67 38.247 43.146 -2.213 1.00 19.61 O ATOM 540 CB ALA A 67 35.583 42.592 -4.193 1.00 19.09 C ATOM 541 N PRO A 68 37.050 44.959 -2.751 1.00 23.12 N ATOM 542 CA PRO A 68 38.199 45.868 -2.643 1.00 24.69 C ATOM 543 C PRO A 68 38.812 45.855 -1.267 1.00 25.21 C ATOM 544 O PRO A 68 40.047 46.056 -1.176 1.00 25.99 O ATOM 545 CB PRO A 68 37.691 47.243 -3.032 1.00 25.48 C ATOM 546 CG PRO A 68 36.385 47.009 -3.737 1.00 25.53 C ATOM 547 CD PRO A 68 35.891 45.627 -3.363 1.00 24.38 C ATOM 548 N LYS A 69 38.025 45.610 -0.227 1.00 25.30 N ATOM 549 CA LYS A 69 38.624 45.544 1.106 1.00 26.12 C ATOM 550 C LYS A 69 39.521 44.351 1.320 1.00 25.65 C ATOM 551 O LYS A 69 40.323 44.428 2.261 1.00 26.00 O ATOM 552 CB LYS A 69 37.573 45.467 2.226 1.00 28.52 C ATOM 553 CG LYS A 69 36.479 46.535 2.056 1.00 31.48 C ATOM 554 CD LYS A 69 35.465 46.325 3.192 1.00 33.78 C ATOM 555 CE LYS A 69 34.137 46.964 2.896 1.00 35.78 C ATOM 556 NZ LYS A 69 33.166 46.536 3.962 1.00 38.12 N ATOM 557 N TYR A 70 39.368 43.314 0.509 1.00 23.09 N ATOM 558 CA TYR A 70 40.164 42.083 0.661 1.00 23.75 C ATOM 559 C TYR A 70 41.205 41.961 -0.442 1.00 23.36 C ATOM 560 O TYR A 70 41.861 40.924 -0.606 1.00 25.05 O ATOM 561 CB TYR A 70 39.155 40.893 0.729 1.00 23.13 C ATOM 562 CG TYR A 70 38.431 40.964 2.096 1.00 21.93 C ATOM 563 CD1 TYR A 70 37.192 41.519 2.274 1.00 21.08 C ATOM 564 CD2 TYR A 70 39.125 40.485 3.205 1.00 21.65 C ATOM 565 CE1 TYR A 70 36.601 41.591 3.530 1.00 21.72 C ATOM 566 CE2 TYR A 70 38.563 40.542 4.483 1.00 22.51 C ATOM 567 CZ TYR A 70 37.319 41.120 4.626 1.00 21.52 C ATOM 568 OH TYR A 70 36.832 41.147 5.891 1.00 24.23 O ATOM 569 N GLY A 71 41.293 43.022 -1.238 1.00 23.22 N ATOM 570 CA GLY A 71 42.279 43.098 -2.325 1.00 24.01 C ATOM 571 C GLY A 71 41.971 42.096 -3.428 1.00 23.93 C ATOM 572 O GLY A 71 42.913 41.672 -4.147 1.00 25.05 O ATOM 573 N ILE A 72 40.706 41.776 -3.625 1.00 22.22 N ATOM 574 CA ILE A 72 40.344 40.806 -4.673 1.00 23.02 C ATOM 575 C ILE A 72 40.559 41.485 -6.012 1.00 24.82 C ATOM 576 O ILE A 72 40.107 42.616 -6.136 1.00 25.78 O ATOM 577 CB ILE A 72 38.859 40.339 -4.474 1.00 22.80 C ATOM 578 CG1 ILE A 72 38.868 39.478 -3.147 1.00 23.61 C ATOM 579 CG2 ILE A 72 38.275 39.580 -5.684 1.00 22.39 C ATOM 580 CD1 ILE A 72 37.457 39.211 -2.618 1.00 23.95 C ATOM 581 N ARG A 73 41.138 40.764 -6.940 1.00 25.70 N ATOM 582 CA ARG A 73 41.505 41.354 -8.233 1.00 28.72 C ATOM 583 C ARG A 73 40.815 40.627 -9.364 1.00 26.64 C ATOM 584 O ARG A 73 40.729 41.187 -10.480 1.00 28.31 O ATOM 585 CB ARG A 73 43.057 41.284 -8.392 1.00 33.96 C ATOM 586 CG ARG A 73 43.712 42.658 -8.585 1.00 39.79 C ATOM 587 CD ARG A 73 44.921 42.718 -9.463 1.00 42.75 C ATOM 588 NE ARG A 73 44.607 43.038 -10.873 1.00 46.10 N ATOM 589 CZ ARG A 73 45.527 43.222 -11.821 1.00 47.31 C ATOM 590 NH1 ARG A 73 45.307 43.365 -13.138 1.00 47.57 N ATOM 591 NH2 ARG A 73 46.814 43.298 -11.412 1.00 48.24 N ATOM 592 N GLY A 74 40.347 39.410 -9.153 1.00 22.67 N ATOM 593 CA GLY A 74 39.693 38.627 -10.211 1.00 20.30 C ATOM 594 C GLY A 74 38.665 37.693 -9.552 1.00 19.13 C ATOM 595 O GLY A 74 38.682 37.542 -8.309 1.00 20.32 O ATOM 596 N ILE A 75 37.797 37.119 -10.360 1.00 17.88 N ATOM 597 CA ILE A 75 36.772 36.178 -9.880 1.00 15.70 C ATOM 598 C ILE A 75 36.777 34.937 -10.769 1.00 16.22 C ATOM 599 O ILE A 75 37.087 35.045 -11.993 1.00 16.90 O ATOM 600 CB ILE A 75 35.389 36.898 -9.741 1.00 15.91 C ATOM 601 CG1 ILE A 75 34.935 37.634 -11.013 1.00 16.44 C ATOM 602 CG2 ILE A 75 35.415 37.871 -8.520 1.00 15.23 C ATOM 603 CD1 ILE A 75 33.394 37.923 -11.020 1.00 17.79 C ATOM 604 N PRO A 76 36.424 33.786 -10.258 1.00 14.73 N ATOM 605 CA PRO A 76 36.002 33.584 -8.873 1.00 14.69 C ATOM 606 C PRO A 76 37.212 33.655 -7.942 1.00 12.99 C ATOM 607 O PRO A 76 38.316 33.247 -8.305 1.00 13.87 O ATOM 608 CB PRO A 76 35.410 32.162 -8.835 1.00 15.07 C ATOM 609 CG PRO A 76 36.121 31.464 -9.950 1.00 15.09 C ATOM 610 CD PRO A 76 36.447 32.515 -10.980 1.00 16.18 C ATOM 611 N THR A 77 36.905 34.167 -6.757 1.00 10.97 N ATOM 612 CA THR A 77 37.919 34.083 -5.649 1.00 10.60 C ATOM 613 C THR A 77 37.182 33.451 -4.461 1.00 10.97 C ATOM 614 O THR A 77 36.013 33.905 -4.258 1.00 9.68 O ATOM 615 CB THR A 77 38.591 35.429 -5.274 1.00 11.88 C ATOM 616 OG1 THR A 77 39.464 35.757 -6.397 1.00 12.88 O ATOM 617 CG2 THR A 77 39.486 35.277 -4.019 1.00 12.63 C ATOM 618 N LEU A 78 37.807 32.521 -3.793 1.00 8.99 N ATOM 619 CA LEU A 78 37.209 31.885 -2.606 1.00 8.94 C ATOM 620 C LEU A 78 38.006 32.393 -1.399 1.00 9.92 C ATOM 621 O LEU A 78 39.246 32.269 -1.360 1.00 10.31 O ATOM 622 CB LEU A 78 37.189 30.360 -2.681 1.00 11.07 C ATOM 623 CG LEU A 78 36.389 29.720 -3.835 1.00 13.40 C ATOM 624 CD1 LEU A 78 36.714 28.233 -3.912 1.00 15.30 C ATOM 625 CD2 LEU A 78 34.922 29.990 -3.582 1.00 14.61 C ATOM 626 N LEU A 79 37.313 32.936 -0.398 1.00 10.15 N ATOM 627 CA LEU A 79 37.980 33.300 0.873 1.00 9.35 C ATOM 628 C LEU A 79 37.477 32.361 1.950 1.00 9.49 C ATOM 629 O LEU A 79 36.248 32.217 2.097 1.00 10.84 O ATOM 630 CB LEU A 79 37.648 34.766 1.234 1.00 11.68 C ATOM 631 CG LEU A 79 38.653 35.845 0.863 1.00 14.83 C ATOM 632 CD1 LEU A 79 39.135 35.800 -0.526 1.00 16.15 C ATOM 633 CD2 LEU A 79 38.069 37.222 1.183 1.00 15.30 C ATOM 634 N LEU A 80 38.371 31.774 2.732 1.00 9.17 N ATOM 635 CA LEU A 80 37.997 30.904 3.860 1.00 9.93 C ATOM 636 C LEU A 80 38.238 31.724 5.150 1.00 10.65 C ATOM 637 O LEU A 80 39.398 32.062 5.413 1.00 11.34 O ATOM 638 CB LEU A 80 38.784 29.574 3.858 1.00 10.60 C ATOM 639 CG LEU A 80 38.448 28.615 4.995 1.00 11.90 C ATOM 640 CD1ALEU A 80 36.958 28.211 4.920 0.50 9.78 C ATOM 641 CD1BLEU A 80 38.001 27.284 4.372 0.50 15.59 C ATOM 642 CD2ALEU A 80 39.362 27.404 4.944 0.50 9.34 C ATOM 643 CD2BLEU A 80 39.706 28.263 5.756 0.50 14.05 C ATOM 644 N PHE A 81 37.170 32.068 5.844 1.00 10.35 N ATOM 645 CA PHE A 81 37.268 32.831 7.107 1.00 11.21 C ATOM 646 C PHE A 81 37.107 31.869 8.286 1.00 12.37 C ATOM 647 O PHE A 81 36.328 30.907 8.298 1.00 12.89 O ATOM 648 CB PHE A 81 36.150 33.876 7.203 1.00 12.17 C ATOM 649 CG PHE A 81 36.301 35.089 6.339 1.00 12.31 C ATOM 650 CD1 PHE A 81 36.835 36.291 6.815 1.00 12.86 C ATOM 651 CD2 PHE A 81 35.865 35.026 5.007 1.00 11.60 C ATOM 652 CE1 PHE A 81 36.983 37.397 5.987 1.00 12.87 C ATOM 653 CE2 PHE A 81 36.037 36.114 4.190 1.00 13.00 C ATOM 654 CZ PHE A 81 36.555 37.335 4.645 1.00 13.70 C ATOM 655 N LYS A 82 37.910 32.197 9.316 1.00 14.04 N ATOM 656 CA LYS A 82 37.779 31.529 10.629 1.00 17.14 C ATOM 657 C LYS A 82 38.029 32.608 11.697 1.00 16.20 C ATOM 658 O LYS A 82 38.972 33.361 11.520 1.00 14.23 O ATOM 659 CB LYS A 82 38.751 30.427 10.930 1.00 19.17 C ATOM 660 CG LYS A 82 38.532 29.183 10.117 1.00 23.77 C ATOM 661 CD LYS A 82 39.760 28.268 10.306 1.00 27.67 C ATOM 662 CE LYS A 82 39.342 27.001 11.031 1.00 30.63 C ATOM 663 NZ LYS A 82 40.531 26.057 10.908 1.00 32.49 N ATOM 664 N ASN A 83 37.147 32.680 12.690 1.00 16.95 N ATOM 665 CA ASN A 83 37.409 33.656 13.781 1.00 16.48 C ATOM 666 C ASN A 83 37.595 35.057 13.331 1.00 15.43 C ATOM 667 O ASN A 83 38.470 35.755 13.902 1.00 15.74 O ATOM 668 CB ASN A 83 38.619 33.151 14.611 1.00 18.87 C ATOM 669 CG ASN A 83 38.424 31.748 15.095 1.00 20.65 C ATOM 670 OD1 ASN A 83 37.302 31.326 15.456 1.00 23.64 O ATOM 671 ND2 ASN A 83 39.470 30.925 15.052 1.00 21.65 N ATOM 672 N GLY A 84 36.886 35.550 12.318 1.00 13.73 N ATOM 673 CA GLY A 84 36.897 36.914 11.872 1.00 14.74 C ATOM 674 C GLY A 84 38.041 37.329 10.970 1.00 16.70 C ATOM 675 O GLY A 84 38.177 38.548 10.670 1.00 19.22 O ATOM 676 N GLU A 85 38.785 36.333 10.523 1.00 16.70 N ATOM 677 CA GLU A 85 39.942 36.663 9.678 1.00 19.63 C ATOM 678 C GLU A 85 40.069 35.681 8.524 1.00 16.02 C ATOM 679 O GLU A 85 39.611 34.561 8.671 1.00 15.75 O ATOM 680 CB GLU A 85 41.201 36.499 10.560 1.00 24.65 C ATOM 681 CG GLU A 85 42.142 37.572 10.330 1.00 30.62 C ATOM 682 CD GLU A 85 43.338 37.479 11.268 1.00 33.38 C ATOM 683 OE1 GLU A 85 43.191 37.262 12.461 1.00 34.87 O ATOM 684 OE2 GLU A 85 44.369 37.655 10.564 1.00 35.34 O ATOM 685 N VAL A 86 40.707 36.171 7.457 1.00 14.67 N ATOM 686 CA VAL A 86 40.964 35.221 6.333 1.00 13.47 C ATOM 687 C VAL A 86 41.995 34.197 6.738 1.00 13.45 C ATOM 688 O VAL A 86 43.132 34.561 7.146 1.00 15.92 O ATOM 689 CB VAL A 86 41.359 36.050 5.094 1.00 14.39 C ATOM 690 CG1 VAL A 86 41.802 35.113 3.961 1.00 16.21 C ATOM 691 CG2 VAL A 86 40.248 36.963 4.594 1.00 15.87 C ATOM 692 N ALA A 87 41.715 32.919 6.611 1.00 11.40 N ATOM 693 CA ALA A 87 42.602 31.835 6.921 1.00 11.11 C ATOM 694 C ALA A 87 43.286 31.334 5.632 1.00 10.68 C ATOM 695 O ALA A 87 44.438 30.854 5.697 1.00 10.35 O ATOM 696 CB ALA A 87 41.818 30.688 7.546 1.00 12.23 C ATOM 697 N ALA A 88 42.610 31.459 4.502 1.00 10.16 N ATOM 698 CA ALA A 88 43.226 30.914 3.248 1.00 10.02 C ATOM 699 C ALA A 88 42.413 31.468 2.098 1.00 10.01 C ATOM 700 O ALA A 88 41.243 31.795 2.307 1.00 9.15 O ATOM 701 CB ALA A 88 43.265 29.405 3.240 1.00 10.15 C ATOM 702 N THR A 89 43.029 31.514 0.922 1.00 9.31 N ATOM 703 CA THR A 89 42.279 31.994 -0.245 1.00 9.33 C ATOM 704 C THR A 89 42.665 31.122 -1.457 1.00 10.66 C ATOM 705 O THR A 89 43.752 30.540 -1.444 1.00 8.29 O ATOM 706 CB THR A 89 42.486 33.488 -0.557 1.00 11.86 C ATOM 707 OG1 THR A 89 43.850 33.625 -1.060 1.00 14.41 O ATOM 708 CG2 THR A 89 42.319 34.444 0.612 1.00 10.53 C ATOM 709 N LYS A 90 41.766 31.139 -2.414 1.00 9.83 N ATOM 710 CA LYS A 90 42.043 30.413 -3.677 1.00 12.40 C ATOM 711 C LYS A 90 41.429 31.219 -4.803 1.00 12.13 C ATOM 712 O LYS A 90 40.231 31.565 -4.772 1.00 12.88 O ATOM 713 CB LYS A 90 41.542 28.998 -3.639 1.00 13.92 C ATOM 714 CG LYS A 90 42.280 28.042 -4.648 1.00 18.71 C ATOM 715 CD LYS A 90 41.774 28.232 -6.032 1.00 20.82 C ATOM 716 CE LYS A 90 42.572 27.446 -7.107 1.00 21.79 C ATOM 717 NZ LYS A 90 43.823 28.243 -7.408 1.00 21.88 N ATOM 718 N VAL A 91 42.254 31.573 -5.775 1.00 11.97 N ATOM 719 CA VAL A 91 41.773 32.339 -6.936 1.00 13.03 C ATOM 720 C VAL A 91 41.590 31.432 -8.159 1.00 14.74 C ATOM 721 O VAL A 91 42.479 30.601 -8.447 1.00 15.31 O ATOM 722 CB VAL A 91 42.808 33.448 -7.245 1.00 12.85 C ATOM 723 CG1 VAL A 91 42.346 34.297 -8.423 1.00 14.18 C ATOM 724 CG2 VAL A 91 43.129 34.344 -6.073 1.00 14.09 C ATOM 725 N GLY A 92 40.469 31.564 -8.838 1.00 15.11 N ATOM 726 CA GLY A 92 40.292 30.805 -10.092 1.00 14.98 C ATOM 727 C GLY A 92 39.498 29.557 -9.912 1.00 16.83 C ATOM 728 O GLY A 92 39.301 29.052 -8.774 1.00 18.24 O ATOM 729 N ALA A 93 38.954 29.048 -11.025 1.00 16.71 N ATOM 730 CA ALA A 93 38.185 27.789 -10.910 1.00 17.49 C ATOM 731 C ALA A 93 39.076 26.617 -10.531 1.00 17.11 C ATOM 732 O ALA A 93 40.320 26.619 -10.672 1.00 16.52 O ATOM 733 CB ALA A 93 37.507 27.529 -12.243 1.00 19.35 C ATOM 734 N LEU A 94 38.448 25.591 -10.015 1.00 17.22 N ATOM 735 CA LEU A 94 39.082 24.368 -9.525 1.00 18.27 C ATOM 736 C LEU A 94 38.034 23.257 -9.531 1.00 18.29 C ATOM 737 O LEU A 94 36.834 23.558 -9.610 1.00 20.10 O ATOM 738 CB LEU A 94 39.698 24.549 -8.135 1.00 18.90 C ATOM 739 CG LEU A 94 38.835 24.570 -6.899 1.00 20.71 C ATOM 740 CD1 LEU A 94 39.671 24.836 -5.646 1.00 21.10 C ATOM 741 CD2 LEU A 94 37.739 25.625 -7.024 1.00 21.42 C ATOM 742 N SER A 95 38.509 22.049 -9.458 1.00 17.77 N ATOM 743 CA SER A 95 37.643 20.852 -9.439 1.00 19.03 C ATOM 744 C SER A 95 37.182 20.559 -8.028 1.00 19.50 C ATOM 745 O SER A 95 37.769 21.083 -7.044 1.00 17.85 O ATOM 746 CB SER A 95 38.459 19.679 -10.001 1.00 19.60 C ATOM 747 OG SER A 95 39.380 19.220 -9.029 1.00 20.61 O ATOM 748 N LYS A 96 36.127 19.737 -7.927 1.00 18.38 N ATOM 749 CA LYS A 96 35.701 19.325 -6.580 1.00 18.50 C ATOM 750 C LYS A 96 36.822 18.695 -5.757 1.00 18.03 C ATOM 751 O LYS A 96 36.933 18.969 -4.545 1.00 16.89 O ATOM 752 CB LYS A 96 34.541 18.331 -6.661 1.00 20.54 C ATOM 753 CG LYS A 96 33.998 17.930 -5.266 1.00 23.16 C ATOM 754 CD LYS A 96 32.933 16.840 -5.525 1.00 26.86 C ATOM 755 CE LYS A 96 32.488 16.116 -4.292 1.00 29.09 C ATOM 756 NZ LYS A 96 31.232 15.343 -4.606 1.00 32.67 N ATOM 757 N GLY A 97 37.644 17.832 -6.375 1.00 17.44 N ATOM 758 CA GLY A 97 38.720 17.180 -5.608 1.00 17.45 C ATOM 759 C GLY A 97 39.731 18.213 -5.104 1.00 17.05 C ATOM 760 O GLY A 97 40.186 18.049 -3.967 1.00 19.29 O ATOM 761 N GLN A 98 40.049 19.185 -5.879 1.00 15.92 N ATOM 762 CA GLN A 98 41.003 20.249 -5.490 1.00 16.85 C ATOM 763 C GLN A 98 40.380 21.063 -4.375 1.00 15.24 C ATOM 764 O GLN A 98 41.075 21.406 -3.413 1.00 14.70 O ATOM 765 CB GLN A 98 41.349 21.149 -6.665 1.00 18.99 C ATOM 766 CG GLN A 98 42.139 20.418 -7.756 1.00 21.85 C ATOM 767 CD GLN A 98 42.299 21.343 -8.946 1.00 24.29 C ATOM 768 OE1 GLN A 98 41.395 21.919 -9.505 1.00 25.13 O ATOM 769 NE2 GLN A 98 43.592 21.527 -9.277 1.00 27.89 N ATOM 770 N LEU A 99 39.074 21.339 -4.498 1.00 14.52 N ATOM 771 CA LEU A 99 38.435 22.146 -3.424 1.00 13.74 C ATOM 772 C LEU A 99 38.480 21.419 -2.087 1.00 14.21 C ATOM 773 O LEU A 99 38.739 21.957 -0.980 1.00 14.39 O ATOM 774 CB LEU A 99 37.028 22.567 -3.879 1.00 14.07 C ATOM 775 CG LEU A 99 36.233 23.382 -2.826 1.00 15.28 C ATOM 776 CD1 LEU A 99 37.011 24.596 -2.327 1.00 15.20 C ATOM 777 CD2 LEU A 99 34.920 23.852 -3.468 1.00 16.76 C ATOM 778 N LYS A 100 38.178 20.117 -2.134 1.00 14.83 N ATOM 779 CA LYS A 100 38.195 19.291 -0.926 1.00 17.25 C ATOM 780 C LYS A 100 39.570 19.305 -0.292 1.00 16.19 C ATOM 781 O LYS A 100 39.711 19.449 0.926 1.00 15.40 O ATOM 782 CB LYS A 100 37.752 17.840 -1.139 1.00 19.67 C ATOM 783 CG LYS A 100 36.229 17.877 -1.349 1.00 24.84 C ATOM 784 CD LYS A 100 35.667 16.524 -1.723 1.00 28.62 C ATOM 785 CE LYS A 100 35.866 15.550 -0.542 1.00 31.48 C ATOM 786 NZ LYS A 100 34.870 14.428 -0.766 1.00 34.70 N ATOM 787 N GLU A 101 40.601 19.184 -1.129 1.00 17.16 N ATOM 788 CA GLU A 101 41.969 19.195 -0.546 1.00 18.15 C ATOM 789 C GLU A 101 42.315 20.538 0.086 1.00 16.50 C ATOM 790 O GLU A 101 42.960 20.633 1.143 1.00 16.77 O ATOM 791 CB GLU A 101 42.979 18.945 -1.641 1.00 22.32 C ATOM 792 CG GLU A 101 43.199 17.512 -2.062 1.00 27.45 C ATOM 793 CD GLU A 101 44.530 17.385 -2.812 1.00 30.43 C ATOM 794 OE1 GLU A 101 45.505 16.966 -2.193 1.00 32.98 O ATOM 795 OE2 GLU A 101 44.405 17.834 -3.964 1.00 31.71 O ATOM 796 N PHE A 102 41.901 21.595 -0.587 1.00 14.76 N ATOM 797 CA PHE A 102 42.101 22.950 -0.063 1.00 13.09 C ATOM 798 C PHE A 102 41.367 23.076 1.276 1.00 13.38 C ATOM 799 O PHE A 102 41.949 23.650 2.209 1.00 14.41 O ATOM 800 CB PHE A 102 41.643 23.981 -1.084 1.00 13.54 C ATOM 801 CG PHE A 102 41.539 25.386 -0.613 1.00 13.43 C ATOM 802 CD1 PHE A 102 40.329 25.914 -0.147 1.00 14.79 C ATOM 803 CD2 PHE A 102 42.676 26.182 -0.631 1.00 14.85 C ATOM 804 CE1 PHE A 102 40.247 27.240 0.266 1.00 15.75 C ATOM 805 CE2 PHE A 102 42.606 27.522 -0.215 1.00 14.75 C ATOM 806 CZ PHE A 102 41.415 28.037 0.263 1.00 15.61 C ATOM 807 N LEU A 103 40.120 22.586 1.350 1.00 13.41 N ATOM 808 CA LEU A 103 39.410 22.700 2.656 1.00 14.15 C ATOM 809 C LEU A 103 40.055 21.873 3.740 1.00 15.45 C ATOM 810 O LEU A 103 40.251 22.311 4.896 1.00 16.18 O ATOM 811 CB LEU A 103 37.932 22.366 2.474 1.00 13.82 C ATOM 812 CG LEU A 103 37.181 23.342 1.578 1.00 15.30 C ATOM 813 CD1 LEU A 103 35.830 22.720 1.212 1.00 14.22 C ATOM 814 CD2 LEU A 103 37.030 24.669 2.306 1.00 15.21 C ATOM 815 N ASP A 104 40.362 20.632 3.377 1.00 17.99 N ATOM 816 CA ASP A 104 40.924 19.710 4.407 1.00 19.48 C ATOM 817 C ASP A 104 42.228 20.243 4.975 1.00 20.07 C ATOM 818 O ASP A 104 42.499 20.025 6.159 1.00 20.72 O ATOM 819 CB ASP A 104 41.059 18.289 3.858 1.00 21.94 C ATOM 820 CG ASP A 104 39.666 17.719 3.612 1.00 24.56 C ATOM 821 OD1 ASP A 104 38.631 18.256 4.015 1.00 25.10 O ATOM 822 OD2 ASP A 104 39.677 16.690 2.876 1.00 27.45 O ATOM 823 N ALA A 105 43.038 20.916 4.183 1.00 19.24 N ATOM 824 CA ALA A 105 44.278 21.547 4.617 1.00 19.04 C ATOM 825 C ALA A 105 44.054 22.641 5.643 1.00 21.27 C ATOM 826 O ALA A 105 45.012 22.973 6.371 1.00 20.85 O ATOM 827 CB ALA A 105 45.048 22.144 3.421 1.00 18.17 C ATOM 828 N ASN A 106 42.843 23.210 5.657 1.00 20.25 N ATOM 829 CA ASN A 106 42.587 24.329 6.538 1.00 22.59 C ATOM 830 C ASN A 106 41.570 24.027 7.617 1.00 25.74 C ATOM 831 O ASN A 106 41.434 24.979 8.427 1.00 27.14 O ATOM 832 CB ASN A 106 42.041 25.562 5.767 1.00 21.45 C ATOM 833 CG ASN A 106 43.074 26.085 4.824 1.00 21.12 C ATOM 834 OD1 ASN A 106 43.982 26.759 5.351 1.00 22.28 O ATOM 835 ND2 ASN A 106 43.055 25.826 3.528 1.00 21.39 N ATOM 836 N LEU A 107 40.919 22.900 7.599 1.00 29.33 N ATOM 837 CA LEU A 107 39.812 22.787 8.605 1.00 34.50 C ATOM 838 C LEU A 107 40.275 22.037 9.847 1.00 39.17 C ATOM 839 O LEU A 107 39.571 22.111 10.885 1.00 41.13 O ATOM 840 CB LEU A 107 38.573 22.199 7.965 1.00 33.33 C ATOM 841 CG LEU A 107 37.838 23.048 6.951 1.00 33.80 C ATOM 842 CD1 LEU A 107 36.655 22.236 6.405 1.00 33.67 C ATOM 843 CD2 LEU A 107 37.366 24.327 7.605 1.00 33.80 C ATOM 844 N ALA A 108 41.357 21.341 9.676 1.00 42.93 N ATOM 845 CA ALA A 108 42.151 20.619 10.674 1.00 46.31 C ATOM 846 C ALA A 108 42.632 19.312 10.013 1.00 48.21 C ATOM 847 O ALA A 108 41.703 18.483 9.767 1.00 49.54 O ATOM 848 CB ALA A 108 41.441 20.369 11.988 1.00 46.65 C ATOM 849 OXT ALA A 108 43.857 19.249 9.766 1.00 49.19 O TER 850 ALA A 108 ATOM 851 N SER B 1 9.147 31.220 23.823 1.00 28.73 N ATOM 852 CA SER B 1 9.382 32.527 24.427 1.00 30.33 C ATOM 853 C SER B 1 8.629 32.863 25.689 1.00 29.90 C ATOM 854 O SER B 1 8.743 34.011 26.208 1.00 30.15 O ATOM 855 CB SER B 1 9.073 33.599 23.355 1.00 32.50 C ATOM 856 OG SER B 1 9.769 33.144 22.172 1.00 36.47 O ATOM 857 N ASP B 2 7.883 31.951 26.267 1.00 28.77 N ATOM 858 CA ASP B 2 7.110 32.139 27.471 1.00 27.48 C ATOM 859 C ASP B 2 8.046 32.352 28.660 1.00 25.85 C ATOM 860 O ASP B 2 7.596 32.992 29.606 1.00 26.04 O ATOM 861 CB ASP B 2 6.172 30.931 27.676 1.00 29.16 C ATOM 862 CG ASP B 2 6.940 29.664 27.972 1.00 29.86 C ATOM 863 OD1 ASP B 2 7.791 29.210 27.188 1.00 30.68 O ATOM 864 OD2 ASP B 2 6.754 29.090 29.071 1.00 30.62 O ATOM 865 N LYS B 3 9.274 31.864 28.610 1.00 24.79 N ATOM 866 CA LYS B 3 10.143 32.018 29.811 1.00 25.00 C ATOM 867 C LYS B 3 11.253 33.059 29.615 1.00 24.31 C ATOM 868 O LYS B 3 12.170 33.065 30.435 1.00 24.69 O ATOM 869 CB LYS B 3 10.778 30.698 30.247 1.00 26.05 C ATOM 870 CG LYS B 3 9.738 29.706 30.773 1.00 28.33 C ATOM 871 CD LYS B 3 10.289 28.323 31.108 1.00 30.13 C ATOM 872 CE LYS B 3 9.118 27.342 31.326 1.00 31.62 C ATOM 873 NZ LYS B 3 8.753 26.735 30.022 1.00 32.41 N ATOM 874 N ILE B 4 11.123 33.874 28.621 1.00 23.10 N ATOM 875 CA ILE B 4 12.111 34.962 28.375 1.00 22.91 C ATOM 876 C ILE B 4 11.612 36.321 28.792 1.00 22.37 C ATOM 877 O ILE B 4 10.453 36.664 28.426 1.00 23.92 O ATOM 878 CB ILE B 4 12.557 34.804 26.875 1.00 23.31 C ATOM 879 CG1 ILE B 4 13.229 33.424 26.789 1.00 24.24 C ATOM 880 CG2 ILE B 4 13.480 35.995 26.497 1.00 22.00 C ATOM 881 CD1 ILE B 4 13.937 32.992 25.520 1.00 26.30 C ATOM 882 N ILE B 5 12.367 37.081 29.554 1.00 21.10 N ATOM 883 CA ILE B 5 12.027 38.440 29.972 1.00 23.29 C ATOM 884 C ILE B 5 12.372 39.429 28.838 1.00 23.28 C ATOM 885 O ILE B 5 13.474 39.356 28.267 1.00 21.93 O ATOM 886 CB ILE B 5 12.795 38.902 31.264 1.00 24.85 C ATOM 887 CG1 ILE B 5 12.724 37.963 32.455 1.00 27.62 C ATOM 888 CG2 ILE B 5 12.349 40.346 31.673 1.00 27.13 C ATOM 889 CD1 ILE B 5 11.346 37.388 32.799 1.00 28.69 C ATOM 890 N AHIS B 6 11.446 40.298 28.479 0.50 23.56 N ATOM 891 N BHIS B 6 11.456 40.335 28.600 0.50 23.88 N ATOM 892 CA AHIS B 6 11.783 41.302 27.424 0.50 23.82 C ATOM 893 CA BHIS B 6 11.499 41.454 27.655 0.50 24.43 C ATOM 894 C AHIS B 6 12.112 42.569 28.198 0.50 23.83 C ATOM 895 C BHIS B 6 12.099 42.667 28.345 0.50 24.22 C ATOM 896 O AHIS B 6 11.293 43.004 29.019 0.50 24.90 O ATOM 897 O BHIS B 6 11.409 43.240 29.220 0.50 25.13 O ATOM 898 CB AHIS B 6 10.723 41.492 26.337 0.50 25.05 C ATOM 899 CB BHIS B 6 10.083 41.863 27.152 0.50 26.02 C ATOM 900 CG AHIS B 6 10.753 40.389 25.310 0.50 25.47 C ATOM 901 CG BHIS B 6 10.031 43.189 26.458 0.50 27.28 C ATOM 902 ND1AHIS B 6 10.205 39.140 25.505 0.50 25.64 N ATOM 903 ND1BHIS B 6 10.441 43.381 25.160 0.50 28.24 N ATOM 904 CD2AHIS B 6 11.291 40.384 24.070 0.50 25.75 C ATOM 905 CD2BHIS B 6 9.615 44.403 26.911 0.50 27.64 C ATOM 906 CE1AHIS B 6 10.408 38.411 24.421 0.50 25.78 C ATOM 907 CE1BHIS B 6 10.271 44.649 24.848 0.50 27.81 C ATOM 908 NE2AHIS B 6 11.070 39.138 23.542 0.50 26.15 N ATOM 909 NE2BHIS B 6 9.778 45.294 25.877 0.50 27.98 N ATOM 910 N LEU B 7 13.299 43.080 27.978 1.00 22.96 N ATOM 911 CA LEU B 7 13.863 44.251 28.660 1.00 21.75 C ATOM 912 C LEU B 7 13.666 45.510 27.788 1.00 22.36 C ATOM 913 O LEU B 7 13.390 45.374 26.588 1.00 21.99 O ATOM 914 CB LEU B 7 15.336 44.010 28.935 1.00 21.16 C ATOM 915 CG LEU B 7 15.746 42.851 29.806 1.00 21.24 C ATOM 916 CD1 LEU B 7 17.266 42.779 29.919 1.00 20.64 C ATOM 917 CD2 LEU B 7 15.148 43.035 31.208 1.00 22.44 C ATOM 918 N THR B 8 13.846 46.641 28.484 1.00 23.64 N ATOM 919 CA THR B 8 13.814 47.943 27.774 1.00 23.56 C ATOM 920 C THR B 8 14.959 48.762 28.296 1.00 23.75 C ATOM 921 O THR B 8 15.655 48.358 29.271 1.00 23.54 O ATOM 922 CB THR B 8 12.425 48.698 27.922 1.00 23.99 C ATOM 923 OG1 THR B 8 12.325 49.049 29.323 1.00 25.13 O ATOM 924 CG2 THR B 8 11.212 47.933 27.427 1.00 24.53 C ATOM 925 N ASP B 9 15.161 49.941 27.696 1.00 23.67 N ATOM 926 CA ASP B 9 16.280 50.793 28.171 1.00 24.42 C ATOM 927 C ASP B 9 16.145 51.125 29.656 1.00 25.42 C ATOM 928 O ASP B 9 17.187 51.347 30.308 1.00 25.84 O ATOM 929 CB ASP B 9 16.421 52.028 27.283 1.00 25.00 C ATOM 930 CG ASP B 9 17.108 51.709 25.964 1.00 26.51 C ATOM 931 OD1 ASP B 9 16.781 52.371 24.953 1.00 25.75 O ATOM 932 OD2 ASP B 9 17.970 50.789 25.891 1.00 25.82 O ATOM 933 N ASP B 10 14.961 51.165 30.191 1.00 27.35 N ATOM 934 CA ASP B 10 14.725 51.490 31.621 1.00 29.00 C ATOM 935 C ASP B 10 15.036 50.362 32.601 1.00 30.33 C ATOM 936 O ASP B 10 14.916 50.561 33.840 1.00 29.31 O ATOM 937 CB ASP B 10 13.297 52.052 31.738 1.00 28.66 C ATOM 938 CG ASP B 10 13.137 53.452 31.119 1.00 29.28 C ATOM 939 OD1 ASP B 10 11.971 53.755 30.734 1.00 28.41 O ATOM 940 OD2 ASP B 10 14.085 54.248 30.968 1.00 28.39 O ATOM 941 N SER B 11 15.528 49.207 32.157 1.00 31.34 N ATOM 942 CA SER B 11 15.883 48.030 32.953 1.00 32.46 C ATOM 943 C SER B 11 17.272 48.047 33.588 1.00 33.52 C ATOM 944 O SER B 11 17.735 47.184 34.340 1.00 32.70 O ATOM 945 CB SER B 11 15.916 46.836 31.976 1.00 31.90 C ATOM 946 OG SER B 11 14.538 46.575 31.754 1.00 32.01 O ATOM 947 N PHE B 12 17.955 49.052 33.132 1.00 35.22 N ATOM 948 CA PHE B 12 19.393 49.232 33.506 1.00 39.37 C ATOM 949 C PHE B 12 19.233 50.378 34.510 1.00 44.08 C ATOM 950 O PHE B 12 19.282 51.562 34.205 1.00 44.75 O ATOM 951 CB PHE B 12 20.244 49.258 32.262 1.00 35.57 C ATOM 952 CG PHE B 12 20.263 47.918 31.537 1.00 32.41 C ATOM 953 CD1 PHE B 12 19.211 47.535 30.713 1.00 30.40 C ATOM 954 CD2 PHE B 12 21.338 47.046 31.715 1.00 31.15 C ATOM 955 CE1 PHE B 12 19.223 46.311 30.069 1.00 29.36 C ATOM 956 CE2 PHE B 12 21.381 45.823 31.060 1.00 29.58 C ATOM 957 CZ PHE B 12 20.312 45.448 30.230 1.00 29.00 C ATOM 958 N ASP B 13 18.857 49.806 35.646 1.00 49.90 N ATOM 959 CA ASP B 13 18.489 50.349 36.947 1.00 54.42 C ATOM 960 C ASP B 13 17.366 49.469 37.532 1.00 55.98 C ATOM 961 O ASP B 13 16.664 50.017 38.431 1.00 56.85 O ATOM 962 CB ASP B 13 18.081 51.821 36.843 1.00 56.28 C ATOM 963 CG ASP B 13 18.222 52.724 38.044 1.00 57.90 C ATOM 964 OD1 ASP B 13 17.254 52.984 38.798 1.00 58.64 O ATOM 965 OD2 ASP B 13 19.358 53.249 38.229 1.00 58.64 O ATOM 966 N THR B 14 17.171 48.215 37.096 1.00 56.82 N ATOM 967 CA THR B 14 15.955 47.514 37.600 1.00 57.90 C ATOM 968 C THR B 14 15.967 45.998 37.448 1.00 58.03 C ATOM 969 O THR B 14 16.352 45.228 38.352 1.00 57.15 O ATOM 970 CB THR B 14 14.629 48.105 36.945 1.00 58.39 C ATOM 971 OG1 THR B 14 14.517 49.533 37.254 1.00 59.28 O ATOM 972 CG2 THR B 14 13.324 47.405 37.368 1.00 58.42 C ATOM 973 N ASP B 15 15.478 45.565 36.289 1.00 57.93 N ATOM 974 CA ASP B 15 15.365 44.178 35.865 1.00 58.36 C ATOM 975 C ASP B 15 16.733 43.509 35.667 1.00 57.97 C ATOM 976 O ASP B 15 16.749 42.261 35.470 1.00 58.43 O ATOM 977 CB ASP B 15 14.532 44.014 34.586 1.00 58.90 C ATOM 978 CG ASP B 15 13.040 44.088 34.751 1.00 59.73 C ATOM 979 OD1 ASP B 15 12.476 43.913 35.835 1.00 59.94 O ATOM 980 OD2 ASP B 15 12.411 44.356 33.694 1.00 60.52 O ATOM 981 N VAL B 16 17.837 44.240 35.646 1.00 57.05 N ATOM 982 CA VAL B 16 19.140 43.552 35.516 1.00 55.61 C ATOM 983 C VAL B 16 20.120 44.096 36.551 1.00 55.40 C ATOM 984 O VAL B 16 20.825 43.252 37.151 1.00 55.79 O ATOM 985 CB VAL B 16 19.717 43.502 34.107 1.00 55.03 C ATOM 986 CG1 VAL B 16 20.631 42.275 33.964 1.00 54.62 C ATOM 987 CG2 VAL B 16 18.673 43.496 33.012 1.00 54.86 C ATOM 988 N LEU B 17 20.130 45.390 36.794 1.00 54.05 N ATOM 989 CA LEU B 17 21.151 45.828 37.785 1.00 53.84 C ATOM 990 C LEU B 17 20.629 45.718 39.200 1.00 54.29 C ATOM 991 O LEU B 17 21.348 45.449 40.202 1.00 53.78 O ATOM 992 CB LEU B 17 21.601 47.195 37.284 1.00 54.03 C ATOM 993 CG LEU B 17 21.728 47.374 35.777 1.00 53.38 C ATOM 994 CD1 LEU B 17 22.276 48.763 35.507 1.00 53.41 C ATOM 995 CD2 LEU B 17 22.647 46.303 35.213 1.00 52.70 C ATOM 996 N LYS B 18 19.303 45.975 39.283 1.00 54.33 N ATOM 997 CA LYS B 18 18.682 45.827 40.644 1.00 53.18 C ATOM 998 C LYS B 18 18.474 44.310 40.791 1.00 50.91 C ATOM 999 O LYS B 18 18.732 43.733 41.855 1.00 51.64 O ATOM 1000 CB LYS B 18 17.408 46.587 40.850 1.00 54.78 C ATOM 1001 CG LYS B 18 17.340 48.081 41.049 1.00 56.27 C ATOM 1002 CD LYS B 18 18.523 48.890 40.582 1.00 57.49 C ATOM 1003 CE LYS B 18 19.562 49.192 41.628 1.00 58.73 C ATOM 1004 NZ LYS B 18 19.988 48.032 42.458 1.00 59.16 N ATOM 1005 N ALA B 19 18.042 43.764 39.644 1.00 47.12 N ATOM 1006 CA ALA B 19 17.785 42.334 39.562 1.00 43.51 C ATOM 1007 C ALA B 19 19.040 41.584 40.037 1.00 41.07 C ATOM 1008 O ALA B 19 20.108 41.836 39.456 1.00 40.82 O ATOM 1009 CB ALA B 19 17.516 41.850 38.179 1.00 43.27 C ATOM 1010 N ASP B 20 18.787 40.740 41.008 1.00 36.80 N ATOM 1011 CA ASP B 20 19.888 39.898 41.514 1.00 33.96 C ATOM 1012 C ASP B 20 19.881 38.628 40.646 1.00 29.83 C ATOM 1013 O ASP B 20 19.143 38.530 39.626 1.00 31.26 O ATOM 1014 CB ASP B 20 19.734 39.659 43.003 1.00 34.57 C ATOM 1015 CG ASP B 20 18.705 38.592 43.318 1.00 36.60 C ATOM 1016 OD1 ASP B 20 18.831 37.718 44.181 1.00 37.32 O ATOM 1017 OD2 ASP B 20 17.681 38.610 42.576 1.00 38.18 O ATOM 1018 N GLY B 21 20.675 37.664 41.060 1.00 25.13 N ATOM 1019 CA GLY B 21 20.759 36.386 40.383 1.00 20.45 C ATOM 1020 C GLY B 21 21.557 36.567 39.065 1.00 17.60 C ATOM 1021 O GLY B 21 22.094 37.635 38.764 1.00 16.99 O ATOM 1022 N ALA B 22 21.617 35.450 38.397 1.00 15.06 N ATOM 1023 CA ALA B 22 22.410 35.350 37.142 1.00 13.28 C ATOM 1024 C ALA B 22 21.386 35.532 36.005 1.00 13.13 C ATOM 1025 O ALA B 22 20.373 34.831 35.948 1.00 13.37 O ATOM 1026 CB ALA B 22 23.102 34.015 37.078 1.00 13.83 C ATOM 1027 N ILE B 23 21.692 36.457 35.117 1.00 11.03 N ATOM 1028 CA ILE B 23 20.818 36.806 34.011 1.00 12.13 C ATOM 1029 C ILE B 23 21.646 36.846 32.701 1.00 10.35 C ATOM 1030 O ILE B 23 22.654 37.554 32.713 1.00 10.59 O ATOM 1031 CB ILE B 23 20.152 38.192 34.228 1.00 14.81 C ATOM 1032 CG1 ILE B 23 19.431 38.167 35.616 1.00 18.20 C ATOM 1033 CG2 ILE B 23 19.145 38.512 33.081 1.00 15.27 C ATOM 1034 CD1 ILE B 23 19.138 39.649 36.001 1.00 20.91 C ATOM 1035 N LEU B 24 21.115 36.179 31.717 1.00 9.11 N ATOM 1036 CA LEU B 24 21.806 36.146 30.397 1.00 8.10 C ATOM 1037 C LEU B 24 20.983 37.061 29.486 1.00 10.08 C ATOM 1038 O LEU B 24 19.775 36.732 29.370 1.00 10.45 O ATOM 1039 CB LEU B 24 21.868 34.701 29.931 1.00 10.04 C ATOM 1040 CG LEU B 24 22.474 34.535 28.520 1.00 11.55 C ATOM 1041 CD1 LEU B 24 23.986 34.780 28.622 1.00 13.90 C ATOM 1042 CD2 LEU B 24 22.140 33.094 28.102 1.00 12.35 C ATOM 1043 N VAL B 25 21.557 38.100 28.931 1.00 8.99 N ATOM 1044 CA VAL B 25 20.807 39.066 28.102 1.00 8.92 C ATOM 1045 C VAL B 25 21.278 38.951 26.652 1.00 10.20 C ATOM 1046 O VAL B 25 22.478 39.078 26.394 1.00 11.05 O ATOM 1047 CB VAL B 25 21.018 40.509 28.593 1.00 9.27 C ATOM 1048 CG1 VAL B 25 20.251 41.526 27.736 1.00 10.50 C ATOM 1049 CG2 VAL B 25 20.639 40.664 30.076 1.00 10.68 C ATOM 1050 N ASP B 26 20.299 38.712 25.786 1.00 9.98 N ATOM 1051 CA ASP B 26 20.583 38.656 24.317 1.00 9.27 C ATOM 1052 C ASP B 26 20.221 40.029 23.687 1.00 10.64 C ATOM 1053 O ASP B 26 19.047 40.444 23.769 1.00 11.97 O ATOM 1054 CB ASP B 26 19.760 37.509 23.763 1.00 10.63 C ATOM 1055 CG ASP B 26 19.680 37.399 22.260 1.00 12.39 C ATOM 1056 OD1 ASP B 26 18.629 36.880 21.781 1.00 14.48 O ATOM 1057 OD2 ASP B 26 20.626 37.761 21.537 1.00 15.07 O ATOM 1058 N PHE B 27 21.251 40.662 23.125 1.00 9.89 N ATOM 1059 CA PHE B 27 21.005 41.909 22.319 1.00 10.90 C ATOM 1060 C PHE B 27 20.802 41.462 20.873 1.00 11.23 C ATOM 1061 O PHE B 27 21.679 40.772 20.329 1.00 12.58 O ATOM 1062 CB PHE B 27 22.216 42.822 22.470 1.00 11.18 C ATOM 1063 CG PHE B 27 22.334 43.456 23.808 1.00 12.81 C ATOM 1064 CD1 PHE B 27 21.958 44.799 23.997 1.00 14.43 C ATOM 1065 CD2 PHE B 27 22.773 42.734 24.913 1.00 14.10 C ATOM 1066 CE1 PHE B 27 22.069 45.416 25.234 1.00 14.57 C ATOM 1067 CE2 PHE B 27 22.870 43.322 26.185 1.00 14.69 C ATOM 1068 CZ PHE B 27 22.522 44.672 26.334 1.00 14.42 C ATOM 1069 N TRP B 28 19.649 41.814 20.280 1.00 12.40 N ATOM 1070 CA TRP B 28 19.285 41.313 18.950 1.00 12.31 C ATOM 1071 C TRP B 28 18.428 42.368 18.215 1.00 12.07 C ATOM 1072 O TRP B 28 18.046 43.385 18.783 1.00 13.39 O ATOM 1073 CB TRP B 28 18.488 39.995 19.101 1.00 13.10 C ATOM 1074 CG TRP B 28 17.112 40.231 19.662 1.00 13.68 C ATOM 1075 CD1 TRP B 28 16.719 40.658 20.888 1.00 14.49 C ATOM 1076 CD2 TRP B 28 15.872 40.156 18.909 1.00 15.17 C ATOM 1077 NE1 TRP B 28 15.353 40.817 20.984 1.00 15.26 N ATOM 1078 CE2 TRP B 28 14.841 40.523 19.752 1.00 14.78 C ATOM 1079 CE3 TRP B 28 15.616 39.827 17.569 1.00 16.80 C ATOM 1080 CZ2 TRP B 28 13.501 40.577 19.351 1.00 16.41 C ATOM 1081 CZ3 TRP B 28 14.295 39.862 17.157 1.00 18.01 C ATOM 1082 CH2 TRP B 28 13.245 40.219 18.025 1.00 17.26 C ATOM 1083 N ALA B 29 18.226 41.996 16.970 1.00 13.18 N ATOM 1084 CA ALA B 29 17.313 42.786 16.087 1.00 15.93 C ATOM 1085 C ALA B 29 16.715 41.819 15.067 1.00 16.58 C ATOM 1086 O ALA B 29 17.303 40.764 14.786 1.00 16.49 O ATOM 1087 CB ALA B 29 18.070 43.924 15.428 1.00 14.90 C ATOM 1088 N GLU B 30 15.576 42.223 14.494 1.00 20.22 N ATOM 1089 CA GLU B 30 14.864 41.297 13.586 1.00 22.57 C ATOM 1090 C GLU B 30 15.566 41.105 12.270 1.00 21.64 C ATOM 1091 O GLU B 30 15.416 40.047 11.616 1.00 21.37 O ATOM 1092 CB GLU B 30 13.388 41.731 13.413 1.00 27.83 C ATOM 1093 CG GLU B 30 12.475 41.166 14.499 1.00 34.91 C ATOM 1094 CD GLU B 30 11.126 41.683 14.846 1.00 39.12 C ATOM 1095 OE1 GLU B 30 10.663 42.791 14.528 1.00 41.76 O ATOM 1096 OE2 GLU B 30 10.448 40.860 15.556 1.00 40.13 O ATOM 1097 N TRP B 31 16.390 42.081 11.922 1.00 20.25 N ATOM 1098 CA TRP B 31 17.109 41.963 10.629 1.00 21.17 C ATOM 1099 C TRP B 31 18.357 41.097 10.711 1.00 20.43 C ATOM 1100 O TRP B 31 19.042 40.835 9.720 1.00 21.85 O ATOM 1101 CB TRP B 31 17.446 43.396 10.222 1.00 20.96 C ATOM 1102 CG TRP B 31 18.060 44.280 11.245 1.00 20.73 C ATOM 1103 CD1 TRP B 31 17.421 45.185 12.044 1.00 20.45 C ATOM 1104 CD2 TRP B 31 19.443 44.374 11.587 1.00 21.47 C ATOM 1105 NE1 TRP B 31 18.335 45.849 12.841 1.00 21.22 N ATOM 1106 CE2 TRP B 31 19.577 45.366 12.575 1.00 21.55 C ATOM 1107 CE3 TRP B 31 20.586 43.701 11.140 1.00 22.15 C ATOM 1108 CZ2 TRP B 31 20.792 45.717 13.164 1.00 21.26 C ATOM 1109 CZ3 TRP B 31 21.800 44.070 11.727 1.00 21.99 C ATOM 1110 CH2 TRP B 31 21.904 45.064 12.690 1.00 21.21 C ATOM 1111 N CYS B 32 18.705 40.603 11.897 1.00 18.22 N ATOM 1112 CA CYS B 32 19.956 39.881 12.161 1.00 16.70 C ATOM 1113 C CYS B 32 19.742 38.381 12.015 1.00 16.37 C ATOM 1114 O CYS B 32 19.042 37.756 12.830 1.00 16.23 O ATOM 1115 CB CYS B 32 20.376 40.283 13.580 1.00 16.47 C ATOM 1116 SG CYS B 32 21.690 39.258 14.277 1.00 15.96 S ATOM 1117 N GLY B 33 20.316 37.821 10.952 1.00 16.20 N ATOM 1118 CA GLY B 33 20.168 36.408 10.671 1.00 15.83 C ATOM 1119 C GLY B 33 20.612 35.502 11.813 1.00 16.74 C ATOM 1120 O GLY B 33 19.833 34.648 12.289 1.00 17.19 O ATOM 1121 N PRO B 34 21.854 35.630 12.213 1.00 15.83 N ATOM 1122 CA PRO B 34 22.392 34.814 13.325 1.00 16.19 C ATOM 1123 C PRO B 34 21.573 35.014 14.601 1.00 15.21 C ATOM 1124 O PRO B 34 21.503 34.056 15.406 1.00 15.72 O ATOM 1125 CB PRO B 34 23.848 35.237 13.440 1.00 16.11 C ATOM 1126 CG PRO B 34 24.173 35.857 12.095 1.00 16.18 C ATOM 1127 CD PRO B 34 22.894 36.540 11.665 1.00 16.46 C ATOM 1128 N CYS B 35 20.961 36.179 14.773 1.00 14.11 N ATOM 1129 CA CYS B 35 20.119 36.409 15.973 1.00 15.07 C ATOM 1130 C CYS B 35 18.921 35.468 15.978 1.00 17.96 C ATOM 1131 O CYS B 35 18.576 34.877 17.011 1.00 17.56 O ATOM 1132 CB CYS B 35 19.606 37.839 16.048 1.00 15.47 C ATOM 1133 SG CYS B 35 20.968 38.954 16.173 1.00 15.77 S ATOM 1134 N LYS B 36 18.302 35.338 14.804 1.00 17.56 N ATOM 1135 CA LYS B 36 17.182 34.396 14.660 1.00 20.79 C ATOM 1136 C LYS B 36 17.572 32.963 14.866 1.00 20.42 C ATOM 1137 O LYS B 36 16.756 32.179 15.418 1.00 20.93 O ATOM 1138 CB LYS B 36 16.546 34.577 13.246 1.00 23.86 C ATOM 1139 CG LYS B 36 15.959 36.005 13.224 1.00 28.07 C ATOM 1140 CD LYS B 36 14.806 36.135 12.223 1.00 32.27 C ATOM 1141 CE LYS B 36 15.197 37.006 11.055 1.00 35.17 C ATOM 1142 NZ LYS B 36 14.011 37.678 10.441 1.00 37.64 N ATOM 1143 N MET B 37 18.742 32.551 14.449 1.00 21.73 N ATOM 1144 CA MET B 37 19.253 31.197 14.593 1.00 24.57 C ATOM 1145 C MET B 37 19.372 30.822 16.066 1.00 22.92 C ATOM 1146 O MET B 37 19.152 29.643 16.410 1.00 23.67 O ATOM 1147 CB MET B 37 20.601 31.008 13.880 1.00 28.25 C ATOM 1148 CG MET B 37 20.421 31.168 12.383 1.00 34.60 C ATOM 1149 SD MET B 37 22.066 30.951 11.561 1.00 41.63 S ATOM 1150 CE MET B 37 21.967 32.278 10.324 1.00 40.29 C ATOM 1151 N ILE B 38 19.742 31.786 16.922 1.00 19.90 N ATOM 1152 CA ILE B 38 19.897 31.406 18.329 1.00 18.94 C ATOM 1153 C ILE B 38 18.627 31.492 19.144 1.00 17.92 C ATOM 1154 O ILE B 38 18.627 30.947 20.276 1.00 16.77 O ATOM 1155 CB ILE B 38 21.108 32.140 19.030 1.00 18.68 C ATOM 1156 CG1 ILE B 38 20.827 33.631 19.187 1.00 18.42 C ATOM 1157 CG2 ILE B 38 22.439 31.835 18.290 1.00 19.54 C ATOM 1158 CD1 ILE B 38 21.845 34.380 20.109 1.00 20.27 C ATOM 1159 N ALA B 39 17.564 32.065 18.639 1.00 17.67 N ATOM 1160 CA ALA B 39 16.349 32.190 19.469 1.00 18.49 C ATOM 1161 C ALA B 39 15.820 30.885 20.016 1.00 19.29 C ATOM 1162 O ALA B 39 15.485 30.849 21.235 1.00 18.27 O ATOM 1163 CB ALA B 39 15.295 32.990 18.699 1.00 19.13 C ATOM 1164 N PRO B 40 15.733 29.814 19.263 1.00 19.99 N ATOM 1165 CA PRO B 40 15.234 28.546 19.797 1.00 20.07 C ATOM 1166 C PRO B 40 16.176 27.976 20.847 1.00 20.07 C ATOM 1167 O PRO B 40 15.706 27.252 21.762 1.00 20.18 O ATOM 1168 CB PRO B 40 15.125 27.613 18.604 1.00 20.85 C ATOM 1169 CG PRO B 40 15.981 28.255 17.538 1.00 22.17 C ATOM 1170 CD PRO B 40 15.909 29.760 17.793 1.00 21.60 C ATOM 1171 N ILE B 41 17.472 28.227 20.671 1.00 18.08 N ATOM 1172 CA ILE B 41 18.433 27.721 21.655 1.00 18.06 C ATOM 1173 C ILE B 41 18.186 28.388 22.995 1.00 16.79 C ATOM 1174 O ILE B 41 18.305 27.707 24.041 1.00 16.37 O ATOM 1175 CB ILE B 41 19.906 27.980 21.198 1.00 19.20 C ATOM 1176 CG1 ILE B 41 20.221 27.177 19.916 1.00 20.84 C ATOM 1177 CG2 ILE B 41 20.915 27.657 22.321 1.00 20.66 C ATOM 1178 CD1 ILE B 41 21.525 27.765 19.256 1.00 21.79 C ATOM 1179 N LEU B 42 17.888 29.691 22.964 1.00 15.57 N ATOM 1180 CA LEU B 42 17.653 30.390 24.240 1.00 15.77 C ATOM 1181 C LEU B 42 16.382 29.891 24.923 1.00 16.18 C ATOM 1182 O LEU B 42 16.348 29.869 26.160 1.00 16.61 O ATOM 1183 CB LEU B 42 17.635 31.915 24.099 1.00 15.24 C ATOM 1184 CG LEU B 42 18.897 32.537 23.525 1.00 16.99 C ATOM 1185 CD1 LEU B 42 18.634 33.997 23.186 1.00 18.42 C ATOM 1186 CD2 LEU B 42 20.007 32.350 24.543 1.00 16.52 C ATOM 1187 N ASP B 43 15.392 29.531 24.132 1.00 17.23 N ATOM 1188 CA ASP B 43 14.167 28.938 24.734 1.00 19.07 C ATOM 1189 C ASP B 43 14.521 27.647 25.477 1.00 18.97 C ATOM 1190 O ASP B 43 13.999 27.430 26.584 1.00 19.36 O ATOM 1191 CB ASP B 43 13.106 28.656 23.657 1.00 20.14 C ATOM 1192 CG ASP B 43 12.366 29.919 23.272 1.00 22.35 C ATOM 1193 OD1 ASP B 43 11.882 29.893 22.123 1.00 24.80 O ATOM 1194 OD2 ASP B 43 12.229 30.858 24.031 1.00 22.30 O ATOM 1195 N GLU B 44 15.328 26.825 24.873 1.00 18.64 N ATOM 1196 CA GLU B 44 15.720 25.557 25.504 1.00 20.55 C ATOM 1197 C GLU B 44 16.495 25.763 26.788 1.00 19.21 C ATOM 1198 O GLU B 44 16.251 25.056 27.779 1.00 20.02 O ATOM 1199 CB GLU B 44 16.552 24.687 24.574 1.00 23.07 C ATOM 1200 CG GLU B 44 15.741 24.259 23.331 1.00 28.27 C ATOM 1201 CD GLU B 44 16.497 23.306 22.435 1.00 32.79 C ATOM 1202 OE1 GLU B 44 17.329 22.501 22.847 1.00 35.03 O ATOM 1203 OE2 GLU B 44 16.186 23.463 21.212 1.00 36.03 O ATOM 1204 N ILE B 45 17.430 26.703 26.766 1.00 17.29 N ATOM 1205 CA ILE B 45 18.270 27.035 27.945 1.00 16.65 C ATOM 1206 C ILE B 45 17.354 27.584 29.027 1.00 15.29 C ATOM 1207 O ILE B 45 17.510 27.274 30.227 1.00 15.61 O ATOM 1208 CB ILE B 45 19.395 28.059 27.535 1.00 17.35 C ATOM 1209 CG1 ILE B 45 20.451 27.406 26.632 1.00 18.50 C ATOM 1210 CG2 ILE B 45 20.045 28.814 28.730 1.00 18.81 C ATOM 1211 CD1 ILE B 45 21.308 26.278 27.182 1.00 20.61 C ATOM 1212 N ALA B 46 16.381 28.396 28.656 1.00 15.53 N ATOM 1213 CA ALA B 46 15.480 28.973 29.661 1.00 16.69 C ATOM 1214 C ALA B 46 14.737 27.829 30.379 1.00 19.41 C ATOM 1215 O ALA B 46 14.480 27.949 31.603 1.00 19.23 O ATOM 1216 CB ALA B 46 14.522 29.968 29.066 1.00 17.45 C ATOM 1217 N ASP B 47 14.381 26.799 29.617 1.00 19.93 N ATOM 1218 CA ASP B 47 13.686 25.633 30.209 1.00 21.67 C ATOM 1219 C ASP B 47 14.609 24.801 31.106 1.00 21.58 C ATOM 1220 O ASP B 47 14.256 24.509 32.282 1.00 21.63 O ATOM 1221 CB ASP B 47 13.031 24.777 29.105 1.00 23.89 C ATOM 1222 CG AASP B 47 11.569 25.189 28.956 0.50 24.82 C ATOM 1223 CG BASP B 47 12.373 23.524 29.694 0.50 25.47 C ATOM 1224 OD1AASP B 47 10.823 25.162 29.957 0.50 26.02 O ATOM 1225 OD1BASP B 47 12.726 22.388 29.322 0.50 26.53 O ATOM 1226 OD2AASP B 47 11.208 25.524 27.809 0.50 25.41 O ATOM 1227 OD2BASP B 47 11.504 23.680 30.585 0.50 25.78 O ATOM 1228 N GLU B 48 15.746 24.471 30.570 1.00 20.93 N ATOM 1229 CA GLU B 48 16.705 23.622 31.263 1.00 23.42 C ATOM 1230 C GLU B 48 17.230 24.270 32.546 1.00 24.12 C ATOM 1231 O GLU B 48 17.552 23.504 33.491 1.00 24.75 O ATOM 1232 CB GLU B 48 17.915 23.254 30.425 1.00 26.09 C ATOM 1233 CG GLU B 48 17.608 22.304 29.271 1.00 30.21 C ATOM 1234 CD GLU B 48 18.812 22.000 28.409 1.00 33.03 C ATOM 1235 OE1 GLU B 48 18.403 21.660 27.283 1.00 34.87 O ATOM 1236 OE2 GLU B 48 19.966 22.067 28.804 1.00 34.27 O ATOM 1237 N TYR B 49 17.302 25.583 32.592 1.00 22.79 N ATOM 1238 CA TYR B 49 17.894 26.268 33.751 1.00 23.14 C ATOM 1239 C TYR B 49 16.856 27.021 34.573 1.00 22.40 C ATOM 1240 O TYR B 49 17.292 27.856 35.376 1.00 20.45 O ATOM 1241 CB TYR B 49 19.031 27.179 33.295 1.00 25.21 C ATOM 1242 CG TYR B 49 20.250 26.506 32.747 1.00 28.44 C ATOM 1243 CD1 TYR B 49 20.300 25.901 31.500 1.00 30.16 C ATOM 1244 CD2 TYR B 49 21.446 26.532 33.487 1.00 30.77 C ATOM 1245 CE1 TYR B 49 21.448 25.298 30.980 1.00 32.02 C ATOM 1246 CE2 TYR B 49 22.628 25.950 33.007 1.00 31.75 C ATOM 1247 CZ TYR B 49 22.604 25.338 31.763 1.00 32.53 C ATOM 1248 OH TYR B 49 23.770 24.782 31.313 1.00 35.26 O ATOM 1249 N GLN B 50 15.557 26.686 34.466 1.00 21.77 N ATOM 1250 CA GLN B 50 14.598 27.537 35.223 1.00 22.91 C ATOM 1251 C GLN B 50 14.913 27.410 36.725 1.00 21.71 C ATOM 1252 O GLN B 50 15.208 26.293 37.146 1.00 22.27 O ATOM 1253 CB GLN B 50 13.119 27.320 35.004 1.00 26.17 C ATOM 1254 CG GLN B 50 12.596 25.937 35.202 1.00 30.19 C ATOM 1255 CD GLN B 50 11.203 25.825 34.552 1.00 32.23 C ATOM 1256 OE1 GLN B 50 11.055 24.902 33.726 1.00 35.16 O ATOM 1257 NE2 GLN B 50 10.319 26.761 34.872 1.00 31.55 N ATOM 1258 N GLY B 51 14.851 28.557 37.344 1.00 20.23 N ATOM 1259 CA GLY B 51 15.125 28.629 38.785 1.00 20.71 C ATOM 1260 C GLY B 51 16.595 28.890 39.044 1.00 20.66 C ATOM 1261 O GLY B 51 16.956 29.298 40.182 1.00 21.19 O ATOM 1262 N LYS B 52 17.463 28.717 38.043 1.00 19.51 N ATOM 1263 CA LYS B 52 18.881 28.971 38.273 1.00 19.82 C ATOM 1264 C LYS B 52 19.412 30.131 37.444 1.00 18.48 C ATOM 1265 O LYS B 52 20.369 30.817 37.835 1.00 19.41 O ATOM 1266 CB LYS B 52 19.681 27.724 37.881 1.00 23.85 C ATOM 1267 CG LYS B 52 19.390 26.588 38.890 1.00 29.59 C ATOM 1268 CD LYS B 52 20.017 25.292 38.366 1.00 34.52 C ATOM 1269 CE LYS B 52 19.719 24.137 39.345 1.00 37.67 C ATOM 1270 NZ LYS B 52 20.065 24.608 40.748 1.00 40.15 N ATOM 1271 N LEU B 53 18.824 30.278 36.258 1.00 16.06 N ATOM 1272 CA LEU B 53 19.320 31.343 35.326 1.00 15.75 C ATOM 1273 C LEU B 53 18.089 32.036 34.690 1.00 14.98 C ATOM 1274 O LEU B 53 17.158 31.242 34.404 1.00 16.71 O ATOM 1275 CB LEU B 53 20.170 30.647 34.244 1.00 15.01 C ATOM 1276 CG LEU B 53 20.581 31.605 33.101 1.00 16.11 C ATOM 1277 CD1 LEU B 53 21.618 32.571 33.570 1.00 16.37 C ATOM 1278 CD2 LEU B 53 21.070 30.737 31.952 1.00 17.00 C ATOM 1279 N THR B 54 18.119 33.343 34.531 1.00 13.61 N ATOM 1280 CA THR B 54 16.990 34.018 33.821 1.00 14.29 C ATOM 1281 C THR B 54 17.535 34.418 32.438 1.00 13.12 C ATOM 1282 O THR B 54 18.692 34.883 32.462 1.00 12.69 O ATOM 1283 CB THR B 54 16.510 35.280 34.632 1.00 17.07 C ATOM 1284 OG1 THR B 54 16.045 34.771 35.916 1.00 19.08 O ATOM 1285 CG2 THR B 54 15.495 36.163 33.899 1.00 18.26 C ATOM 1286 N VAL B 55 16.746 34.215 31.414 1.00 12.19 N ATOM 1287 CA VAL B 55 17.144 34.606 30.037 1.00 11.91 C ATOM 1288 C VAL B 55 16.289 35.822 29.669 1.00 13.88 C ATOM 1289 O VAL B 55 15.069 35.841 29.943 1.00 12.80 O ATOM 1290 CB VAL B 55 16.989 33.432 29.059 1.00 13.65 C ATOM 1291 CG1 VAL B 55 17.405 33.811 27.643 1.00 13.58 C ATOM 1292 CG2 VAL B 55 17.740 32.179 29.494 1.00 14.22 C ATOM 1293 N ALA B 56 16.956 36.839 29.121 1.00 11.50 N ATOM 1294 CA ALA B 56 16.245 38.106 28.783 1.00 10.67 C ATOM 1295 C ALA B 56 16.736 38.546 27.389 1.00 12.04 C ATOM 1296 O ALA B 56 17.818 38.144 26.920 1.00 12.38 O ATOM 1297 CB ALA B 56 16.565 39.097 29.853 1.00 10.32 C ATOM 1298 N LYS B 57 15.872 39.367 26.794 1.00 11.76 N ATOM 1299 CA LYS B 57 16.210 39.853 25.430 1.00 12.90 C ATOM 1300 C LYS B 57 16.015 41.366 25.387 1.00 13.02 C ATOM 1301 O LYS B 57 15.099 41.898 26.040 1.00 13.80 O ATOM 1302 CB LYS B 57 15.305 39.260 24.350 1.00 14.00 C ATOM 1303 CG LYS B 57 15.596 37.827 23.988 1.00 15.59 C ATOM 1304 CD LYS B 57 14.511 37.291 23.028 1.00 18.08 C ATOM 1305 CE LYS B 57 14.922 35.943 22.532 1.00 20.33 C ATOM 1306 NZ LYS B 57 13.968 35.436 21.511 1.00 22.73 N ATOM 1307 N LEU B 58 16.854 41.999 24.623 1.00 12.44 N ATOM 1308 CA LEU B 58 16.703 43.450 24.404 1.00 13.94 C ATOM 1309 C LEU B 58 16.832 43.673 22.881 1.00 13.70 C ATOM 1310 O LEU B 58 17.874 43.365 22.309 1.00 13.20 O ATOM 1311 CB LEU B 58 17.728 44.225 25.230 1.00 13.87 C ATOM 1312 CG LEU B 58 17.526 45.760 25.021 1.00 15.37 C ATOM 1313 CD1ALEU B 58 17.747 46.481 26.338 0.50 14.85 C ATOM 1314 CD1BLEU B 58 16.520 46.283 26.036 0.50 14.94 C ATOM 1315 CD2ALEU B 58 18.459 46.254 23.932 0.50 13.51 C ATOM 1316 CD2BLEU B 58 18.834 46.488 25.178 0.50 16.87 C ATOM 1317 N ASN B 59 15.779 44.258 22.319 1.00 13.80 N ATOM 1318 CA ASN B 59 15.766 44.545 20.861 1.00 14.82 C ATOM 1319 C ASN B 59 16.443 45.904 20.669 1.00 15.62 C ATOM 1320 O ASN B 59 15.895 46.903 21.212 1.00 16.34 O ATOM 1321 CB ASN B 59 14.310 44.523 20.370 1.00 16.20 C ATOM 1322 CG ASN B 59 14.298 44.775 18.858 1.00 18.25 C ATOM 1323 OD1 ASN B 59 14.590 45.915 18.479 1.00 18.69 O ATOM 1324 ND2 ASN B 59 14.017 43.813 18.007 1.00 20.32 N ATOM 1325 N ILE B 60 17.540 45.988 19.953 1.00 14.17 N ATOM 1326 CA ILE B 60 18.265 47.255 19.874 1.00 15.15 C ATOM 1327 C ILE B 60 17.610 48.280 18.929 1.00 16.65 C ATOM 1328 O ILE B 60 17.991 49.472 19.037 1.00 17.67 O ATOM 1329 CB ILE B 60 19.758 47.021 19.467 1.00 16.15 C ATOM 1330 CG1 ILE B 60 19.816 46.458 18.031 1.00 16.72 C ATOM 1331 CG2 ILE B 60 20.500 46.118 20.506 1.00 16.29 C ATOM 1332 CD1 ILE B 60 21.254 46.555 17.440 1.00 19.88 C ATOM 1333 N ASP B 61 16.697 47.856 18.107 1.00 16.36 N ATOM 1334 CA ASP B 61 15.943 48.797 17.216 1.00 18.57 C ATOM 1335 C ASP B 61 14.943 49.565 18.078 1.00 20.69 C ATOM 1336 O ASP B 61 14.752 50.778 17.900 1.00 21.65 O ATOM 1337 CB ASP B 61 15.265 48.088 16.067 1.00 18.05 C ATOM 1338 CG ASP B 61 16.175 47.577 14.986 1.00 18.43 C ATOM 1339 OD1 ASP B 61 17.308 48.028 14.800 1.00 21.15 O ATOM 1340 OD2 ASP B 61 15.795 46.651 14.252 1.00 20.69 O ATOM 1341 N GLN B 62 14.358 48.859 19.051 1.00 21.42 N ATOM 1342 CA GLN B 62 13.357 49.535 19.911 1.00 22.86 C ATOM 1343 C GLN B 62 13.989 50.196 21.108 1.00 22.24 C ATOM 1344 O GLN B 62 13.355 51.102 21.681 1.00 23.04 O ATOM 1345 CB GLN B 62 12.257 48.585 20.400 1.00 24.85 C ATOM 1346 CG GLN B 62 11.551 47.891 19.276 1.00 28.65 C ATOM 1347 CD GLN B 62 10.820 46.643 19.680 1.00 31.25 C ATOM 1348 OE1 GLN B 62 9.877 46.244 18.980 1.00 35.25 O ATOM 1349 NE2 GLN B 62 11.191 45.954 20.742 1.00 32.04 N ATOM 1350 N ASN B 63 15.148 49.769 21.530 1.00 20.39 N ATOM 1351 CA ASN B 63 15.789 50.308 22.737 1.00 20.82 C ATOM 1352 C ASN B 63 17.260 50.577 22.410 1.00 21.69 C ATOM 1353 O ASN B 63 18.148 49.757 22.707 1.00 21.02 O ATOM 1354 CB ASN B 63 15.688 49.275 23.874 1.00 20.83 C ATOM 1355 CG ASN B 63 14.258 49.112 24.353 1.00 21.45 C ATOM 1356 OD1 ASN B 63 13.837 49.993 25.108 1.00 23.24 O ATOM 1357 ND2 ASN B 63 13.603 48.080 23.903 1.00 21.70 N ATOM 1358 N PRO B 64 17.523 51.710 21.792 1.00 21.69 N ATOM 1359 CA PRO B 64 18.848 51.958 21.263 1.00 21.80 C ATOM 1360 C PRO B 64 19.811 52.558 22.248 1.00 21.91 C ATOM 1361 O PRO B 64 20.971 52.755 21.857 1.00 22.11 O ATOM 1362 CB PRO B 64 18.608 52.888 20.064 1.00 23.39 C ATOM 1363 CG PRO B 64 17.363 53.658 20.457 1.00 23.46 C ATOM 1364 CD PRO B 64 16.492 52.655 21.244 1.00 23.53 C ATOM 1365 N GLY B 65 19.399 52.854 23.451 1.00 20.70 N ATOM 1366 CA GLY B 65 20.245 53.466 24.453 1.00 21.53 C ATOM 1367 C GLY B 65 21.135 52.499 25.222 1.00 21.90 C ATOM 1368 O GLY B 65 22.194 52.933 25.709 1.00 22.36 O ATOM 1369 N THR B 66 20.778 51.229 25.289 1.00 19.09 N ATOM 1370 CA THR B 66 21.577 50.369 26.177 1.00 20.24 C ATOM 1371 C THR B 66 22.855 49.825 25.564 1.00 20.25 C ATOM 1372 O THR B 66 23.874 49.811 26.305 1.00 20.76 O ATOM 1373 CB THR B 66 20.701 49.201 26.785 1.00 21.21 C ATOM 1374 OG1 THR B 66 19.678 49.835 27.606 1.00 21.42 O ATOM 1375 CG2 THR B 66 21.508 48.208 27.640 1.00 20.04 C ATOM 1376 N ALA B 67 22.860 49.384 24.330 1.00 20.21 N ATOM 1377 CA ALA B 67 24.038 48.749 23.711 1.00 21.46 C ATOM 1378 C ALA B 67 25.299 49.604 23.797 1.00 23.27 C ATOM 1379 O ALA B 67 26.355 49.090 24.177 1.00 22.52 O ATOM 1380 CB ALA B 67 23.785 48.321 22.270 1.00 21.41 C ATOM 1381 N PRO B 68 25.213 50.891 23.474 1.00 25.12 N ATOM 1382 CA PRO B 68 26.337 51.820 23.564 1.00 25.49 C ATOM 1383 C PRO B 68 26.955 51.914 24.946 1.00 26.04 C ATOM 1384 O PRO B 68 28.160 52.172 25.026 1.00 26.54 O ATOM 1385 CB PRO B 68 25.750 53.170 23.127 1.00 26.21 C ATOM 1386 CG PRO B 68 24.608 52.755 22.216 1.00 26.47 C ATOM 1387 CD PRO B 68 24.011 51.529 22.875 1.00 25.82 C ATOM 1388 N LYS B 69 26.218 51.715 26.021 1.00 26.02 N ATOM 1389 CA LYS B 69 26.712 51.750 27.394 1.00 26.82 C ATOM 1390 C LYS B 69 27.669 50.588 27.648 1.00 26.08 C ATOM 1391 O LYS B 69 28.502 50.721 28.567 1.00 26.20 O ATOM 1392 CB LYS B 69 25.649 51.606 28.489 1.00 28.84 C ATOM 1393 CG LYS B 69 24.537 52.658 28.462 1.00 31.25 C ATOM 1394 CD LYS B 69 23.538 52.275 29.547 1.00 33.59 C ATOM 1395 CE LYS B 69 22.433 53.290 29.787 1.00 35.57 C ATOM 1396 NZ LYS B 69 21.598 52.744 30.917 1.00 36.47 N ATOM 1397 N TYR B 70 27.511 49.525 26.855 1.00 23.96 N ATOM 1398 CA TYR B 70 28.385 48.369 27.068 1.00 23.98 C ATOM 1399 C TYR B 70 29.428 48.191 25.992 1.00 23.64 C ATOM 1400 O TYR B 70 30.138 47.172 25.984 1.00 24.27 O ATOM 1401 CB TYR B 70 27.545 47.058 27.206 1.00 23.71 C ATOM 1402 CG TYR B 70 26.713 47.109 28.457 1.00 24.15 C ATOM 1403 CD1 TYR B 70 25.358 47.437 28.480 1.00 24.56 C ATOM 1404 CD2 TYR B 70 27.342 46.900 29.702 1.00 24.08 C ATOM 1405 CE1 TYR B 70 24.644 47.501 29.656 1.00 24.92 C ATOM 1406 CE2 TYR B 70 26.642 46.964 30.878 1.00 23.93 C ATOM 1407 CZ TYR B 70 25.298 47.270 30.866 1.00 24.58 C ATOM 1408 OH TYR B 70 24.670 47.342 32.084 1.00 25.82 O ATOM 1409 N GLY B 71 29.487 49.138 25.081 1.00 23.85 N ATOM 1410 CA GLY B 71 30.431 49.161 23.958 1.00 23.44 C ATOM 1411 C GLY B 71 30.087 48.035 22.991 1.00 23.26 C ATOM 1412 O GLY B 71 30.984 47.478 22.340 1.00 23.76 O ATOM 1413 N ILE B 72 28.801 47.703 22.873 1.00 22.39 N ATOM 1414 CA ILE B 72 28.414 46.621 21.949 1.00 22.89 C ATOM 1415 C ILE B 72 28.516 47.115 20.513 1.00 24.20 C ATOM 1416 O ILE B 72 27.920 48.157 20.275 1.00 25.56 O ATOM 1417 CB ILE B 72 26.968 46.109 22.315 1.00 21.72 C ATOM 1418 CG1 ILE B 72 27.085 45.388 23.696 1.00 22.28 C ATOM 1419 CG2 ILE B 72 26.377 45.187 21.228 1.00 21.27 C ATOM 1420 CD1 ILE B 72 25.777 45.214 24.505 1.00 23.02 C ATOM 1421 N ARG B 73 29.146 46.379 19.651 1.00 25.76 N ATOM 1422 CA ARG B 73 29.320 46.807 18.251 1.00 29.99 C ATOM 1423 C ARG B 73 28.785 45.814 17.244 1.00 29.33 C ATOM 1424 O ARG B 73 28.894 46.095 16.018 1.00 31.04 O ATOM 1425 CB ARG B 73 30.828 46.997 17.957 1.00 34.68 C ATOM 1426 CG ARG B 73 31.614 47.800 18.988 1.00 39.54 C ATOM 1427 CD ARG B 73 33.094 47.738 18.683 1.00 44.37 C ATOM 1428 NE ARG B 73 33.343 48.509 17.438 1.00 48.48 N ATOM 1429 CZ ARG B 73 33.810 49.775 17.464 1.00 50.61 C ATOM 1430 NH1 ARG B 73 33.968 50.484 16.337 1.00 51.21 N ATOM 1431 NH2 ARG B 73 34.163 50.319 18.652 1.00 51.80 N ATOM 1432 N GLY B 74 28.288 44.666 17.678 1.00 26.09 N ATOM 1433 CA GLY B 74 27.794 43.618 16.740 1.00 22.47 C ATOM 1434 C GLY B 74 26.712 42.803 17.478 1.00 19.46 C ATOM 1435 O GLY B 74 26.707 42.863 18.715 1.00 18.11 O ATOM 1436 N ILE B 75 25.898 42.125 16.703 1.00 16.80 N ATOM 1437 CA ILE B 75 24.819 41.312 17.307 1.00 14.22 C ATOM 1438 C ILE B 75 24.791 39.976 16.572 1.00 14.02 C ATOM 1439 O ILE B 75 25.331 39.894 15.439 1.00 16.05 O ATOM 1440 CB ILE B 75 23.451 42.032 17.349 1.00 13.41 C ATOM 1441 CG1 ILE B 75 23.137 42.566 15.915 1.00 15.89 C ATOM 1442 CG2 ILE B 75 23.393 43.189 18.375 1.00 13.98 C ATOM 1443 CD1 ILE B 75 21.640 43.053 15.804 1.00 15.40 C ATOM 1444 N PRO B 76 24.341 38.934 17.240 1.00 12.72 N ATOM 1445 CA PRO B 76 23.922 38.971 18.636 1.00 11.90 C ATOM 1446 C PRO B 76 25.113 39.144 19.588 1.00 12.27 C ATOM 1447 O PRO B 76 26.186 38.661 19.233 1.00 12.68 O ATOM 1448 CB PRO B 76 23.279 37.607 18.864 1.00 12.30 C ATOM 1449 CG PRO B 76 23.927 36.700 17.843 1.00 12.49 C ATOM 1450 CD PRO B 76 24.355 37.582 16.675 1.00 12.67 C ATOM 1451 N THR B 77 24.855 39.779 20.743 1.00 10.83 N ATOM 1452 CA THR B 77 25.873 39.843 21.811 1.00 10.50 C ATOM 1453 C THR B 77 25.120 39.326 23.062 1.00 9.29 C ATOM 1454 O THR B 77 23.992 39.764 23.272 1.00 10.15 O ATOM 1455 CB THR B 77 26.510 41.232 22.106 1.00 11.68 C ATOM 1456 OG1 THR B 77 27.352 41.530 20.937 1.00 11.99 O ATOM 1457 CG2 THR B 77 27.418 41.216 23.373 1.00 10.95 C ATOM 1458 N LEU B 78 25.747 38.418 23.780 1.00 8.55 N ATOM 1459 CA LEU B 78 25.169 37.909 25.021 1.00 9.35 C ATOM 1460 C LEU B 78 25.971 38.495 26.177 1.00 8.97 C ATOM 1461 O LEU B 78 27.220 38.403 26.099 1.00 10.50 O ATOM 1462 CB LEU B 78 25.267 36.370 25.072 1.00 11.37 C ATOM 1463 CG LEU B 78 24.619 35.596 23.931 1.00 14.20 C ATOM 1464 CD1 LEU B 78 24.887 34.101 24.073 1.00 16.65 C ATOM 1465 CD2 LEU B 78 23.119 35.912 24.049 1.00 15.60 C ATOM 1466 N LEU B 79 25.269 39.087 27.141 1.00 9.04 N ATOM 1467 CA LEU B 79 25.964 39.551 28.383 1.00 9.53 C ATOM 1468 C LEU B 79 25.498 38.653 29.508 1.00 9.88 C ATOM 1469 O LEU B 79 24.252 38.402 29.605 1.00 10.71 O ATOM 1470 CB LEU B 79 25.540 41.018 28.614 1.00 12.97 C ATOM 1471 CG LEU B 79 26.494 42.124 28.228 1.00 16.03 C ATOM 1472 CD1 LEU B 79 27.022 42.043 26.820 1.00 16.16 C ATOM 1473 CD2 LEU B 79 25.805 43.466 28.517 1.00 16.93 C ATOM 1474 N LEU B 80 26.390 38.189 30.361 1.00 8.93 N ATOM 1475 CA LEU B 80 25.972 37.400 31.531 1.00 8.63 C ATOM 1476 C LEU B 80 26.189 38.325 32.761 1.00 10.03 C ATOM 1477 O LEU B 80 27.332 38.797 32.954 1.00 10.25 O ATOM 1478 CB LEU B 80 26.770 36.101 31.610 1.00 10.35 C ATOM 1479 CG LEU B 80 26.490 35.262 32.878 1.00 11.50 C ATOM 1480 CD1ALEU B 80 25.109 34.654 32.771 0.50 7.99 C ATOM 1481 CD1BLEU B 80 26.653 33.781 32.574 0.50 13.64 C ATOM 1482 CD2ALEU B 80 27.624 34.249 33.054 0.50 6.57 C ATOM 1483 CD2BLEU B 80 27.529 35.632 33.926 0.50 14.72 C ATOM 1484 N PHE B 81 25.110 38.605 33.443 1.00 9.86 N ATOM 1485 CA PHE B 81 25.184 39.436 34.676 1.00 10.36 C ATOM 1486 C PHE B 81 25.136 38.514 35.912 1.00 11.21 C ATOM 1487 O PHE B 81 24.440 37.501 35.875 1.00 12.08 O ATOM 1488 CB PHE B 81 24.008 40.420 34.788 1.00 11.09 C ATOM 1489 CG PHE B 81 24.055 41.528 33.766 1.00 11.92 C ATOM 1490 CD1 PHE B 81 24.576 42.761 34.132 1.00 12.24 C ATOM 1491 CD2 PHE B 81 23.578 41.273 32.463 1.00 12.14 C ATOM 1492 CE1 PHE B 81 24.678 43.806 33.224 1.00 12.34 C ATOM 1493 CE2 PHE B 81 23.652 42.342 31.539 1.00 13.01 C ATOM 1494 CZ PHE B 81 24.173 43.581 31.944 1.00 12.98 C ATOM 1495 N LYS B 82 25.909 38.911 36.910 1.00 11.58 N ATOM 1496 CA LYS B 82 25.906 38.257 38.218 1.00 12.81 C ATOM 1497 C LYS B 82 25.556 39.369 39.223 1.00 14.63 C ATOM 1498 O LYS B 82 26.373 40.257 39.369 1.00 14.99 O ATOM 1499 CB LYS B 82 27.222 37.641 38.610 1.00 12.86 C ATOM 1500 CG LYS B 82 27.574 36.336 37.908 1.00 12.89 C ATOM 1501 CD LYS B 82 28.979 35.887 38.390 1.00 14.24 C ATOM 1502 CE LYS B 82 29.375 34.606 37.686 1.00 14.65 C ATOM 1503 NZ LYS B 82 30.793 34.270 38.033 1.00 15.30 N ATOM 1504 N ASN B 83 24.370 39.237 39.797 1.00 16.60 N ATOM 1505 CA ASN B 83 23.922 40.224 40.794 1.00 20.93 C ATOM 1506 C ASN B 83 24.118 41.637 40.289 1.00 21.83 C ATOM 1507 O ASN B 83 24.732 42.494 40.944 1.00 24.20 O ATOM 1508 CB ASN B 83 24.654 39.892 42.109 1.00 23.72 C ATOM 1509 CG ASN B 83 24.073 40.646 43.311 1.00 27.18 C ATOM 1510 OD1 ASN B 83 24.817 41.276 44.090 1.00 29.89 O ATOM 1511 ND2 ASN B 83 22.761 40.570 43.394 1.00 27.36 N ATOM 1512 N GLY B 84 23.708 41.929 39.073 1.00 21.06 N ATOM 1513 CA GLY B 84 23.739 43.277 38.526 1.00 21.11 C ATOM 1514 C GLY B 84 25.003 43.715 37.810 1.00 21.67 C ATOM 1515 O GLY B 84 24.898 44.756 37.094 1.00 23.56 O ATOM 1516 N GLU B 85 26.104 42.998 37.902 1.00 19.40 N ATOM 1517 CA GLU B 85 27.345 43.444 37.204 1.00 19.73 C ATOM 1518 C GLU B 85 27.679 42.453 36.070 1.00 16.01 C ATOM 1519 O GLU B 85 27.400 41.280 36.221 1.00 12.58 O ATOM 1520 CB GLU B 85 28.548 43.378 38.080 1.00 24.68 C ATOM 1521 CG GLU B 85 28.766 44.119 39.409 1.00 32.09 C ATOM 1522 CD GLU B 85 30.026 43.557 40.059 1.00 35.14 C ATOM 1523 OE1 GLU B 85 30.002 42.779 41.004 1.00 38.21 O ATOM 1524 OE2 GLU B 85 31.067 43.898 39.428 1.00 37.66 O ATOM 1525 N VAL B 86 28.263 42.965 34.994 1.00 14.94 N ATOM 1526 CA VAL B 86 28.629 42.050 33.888 1.00 13.61 C ATOM 1527 C VAL B 86 29.709 41.115 34.343 1.00 14.16 C ATOM 1528 O VAL B 86 30.739 41.613 34.881 1.00 16.56 O ATOM 1529 CB VAL B 86 29.097 42.895 32.670 1.00 15.45 C ATOM 1530 CG1 VAL B 86 29.706 42.002 31.553 1.00 16.93 C ATOM 1531 CG2 VAL B 86 28.000 43.769 32.098 1.00 16.80 C ATOM 1532 N ALA B 87 29.572 39.823 34.121 1.00 11.00 N ATOM 1533 CA ALA B 87 30.558 38.837 34.470 1.00 11.55 C ATOM 1534 C ALA B 87 31.177 38.159 33.253 1.00 11.03 C ATOM 1535 O ALA B 87 32.253 37.574 33.394 1.00 11.03 O ATOM 1536 CB ALA B 87 29.952 37.768 35.390 1.00 13.50 C ATOM 1537 N ALA B 88 30.527 38.205 32.092 1.00 8.45 N ATOM 1538 CA ALA B 88 31.086 37.546 30.915 1.00 7.80 C ATOM 1539 C ALA B 88 30.307 38.051 29.696 1.00 7.67 C ATOM 1540 O ALA B 88 29.161 38.499 29.857 1.00 8.89 O ATOM 1541 CB ALA B 88 30.984 36.013 30.990 1.00 7.59 C ATOM 1542 N THR B 89 30.966 38.030 28.574 1.00 8.49 N ATOM 1543 CA THR B 89 30.248 38.414 27.319 1.00 9.41 C ATOM 1544 C THR B 89 30.682 37.453 26.221 1.00 9.32 C ATOM 1545 O THR B 89 31.742 36.835 26.251 1.00 7.78 O ATOM 1546 CB THR B 89 30.542 39.923 26.951 1.00 10.89 C ATOM 1547 OG1 THR B 89 31.901 39.966 26.488 1.00 12.88 O ATOM 1548 CG2 THR B 89 30.350 40.913 28.094 1.00 11.67 C ATOM 1549 N LYS B 90 29.830 37.433 25.177 1.00 9.37 N ATOM 1550 CA LYS B 90 30.131 36.589 23.992 1.00 9.46 C ATOM 1551 C LYS B 90 29.539 37.273 22.785 1.00 10.76 C ATOM 1552 O LYS B 90 28.310 37.532 22.788 1.00 11.02 O ATOM 1553 CB LYS B 90 29.501 35.236 24.218 1.00 10.64 C ATOM 1554 CG LYS B 90 30.140 34.129 23.353 1.00 14.15 C ATOM 1555 CD LYS B 90 29.596 34.159 21.929 1.00 14.89 C ATOM 1556 CE LYS B 90 30.285 33.040 21.113 1.00 15.37 C ATOM 1557 NZ LYS B 90 30.344 33.375 19.683 1.00 15.66 N ATOM 1558 N VAL B 91 30.354 37.590 21.807 1.00 9.94 N ATOM 1559 CA VAL B 91 29.803 38.241 20.602 1.00 11.17 C ATOM 1560 C VAL B 91 29.618 37.153 19.529 1.00 10.07 C ATOM 1561 O VAL B 91 30.585 36.382 19.295 1.00 11.22 O ATOM 1562 CB VAL B 91 30.775 39.346 20.143 1.00 13.03 C ATOM 1563 CG1 VAL B 91 30.264 39.991 18.825 1.00 14.29 C ATOM 1564 CG2 VAL B 91 31.023 40.371 21.236 1.00 13.64 C ATOM 1565 N GLY B 92 28.466 37.160 18.900 1.00 10.29 N ATOM 1566 CA GLY B 92 28.231 36.229 17.756 1.00 10.33 C ATOM 1567 C GLY B 92 27.432 34.997 18.153 1.00 12.66 C ATOM 1568 O GLY B 92 27.400 34.646 19.327 1.00 12.97 O ATOM 1569 N ALA B 93 26.816 34.382 17.139 1.00 12.35 N ATOM 1570 CA ALA B 93 26.036 33.144 17.367 1.00 13.48 C ATOM 1571 C ALA B 93 26.908 32.002 17.851 1.00 13.53 C ATOM 1572 O ALA B 93 28.142 31.991 17.696 1.00 13.54 O ATOM 1573 CB ALA B 93 25.385 32.764 16.019 1.00 15.85 C ATOM 1574 N LEU B 94 26.241 31.040 18.510 1.00 12.81 N ATOM 1575 CA LEU B 94 26.925 29.808 18.959 1.00 13.21 C ATOM 1576 C LEU B 94 25.906 28.666 19.005 1.00 14.26 C ATOM 1577 O LEU B 94 24.696 28.980 18.984 1.00 14.33 O ATOM 1578 CB LEU B 94 27.620 30.066 20.315 1.00 13.94 C ATOM 1579 CG LEU B 94 26.812 30.118 21.594 1.00 14.70 C ATOM 1580 CD1 LEU B 94 27.752 30.475 22.763 1.00 14.91 C ATOM 1581 CD2 LEU B 94 25.657 31.110 21.543 1.00 16.62 C ATOM 1582 N SER B 95 26.384 27.443 19.082 1.00 14.18 N ATOM 1583 CA SER B 95 25.514 26.270 19.189 1.00 14.94 C ATOM 1584 C SER B 95 25.000 26.080 20.623 1.00 15.79 C ATOM 1585 O SER B 95 25.474 26.667 21.587 1.00 14.43 O ATOM 1586 CB SER B 95 26.323 25.049 18.728 1.00 15.23 C ATOM 1587 OG SER B 95 27.252 24.722 19.755 1.00 16.34 O ATOM 1588 N LYS B 96 24.033 25.188 20.794 1.00 15.59 N ATOM 1589 CA LYS B 96 23.563 24.888 22.146 1.00 17.02 C ATOM 1590 C LYS B 96 24.700 24.351 23.010 1.00 15.21 C ATOM 1591 O LYS B 96 24.765 24.803 24.175 1.00 15.62 O ATOM 1592 CB LYS B 96 22.407 23.903 22.175 1.00 19.22 C ATOM 1593 CG LYS B 96 21.882 23.690 23.619 1.00 21.86 C ATOM 1594 CD LYS B 96 20.651 22.779 23.436 1.00 25.50 C ATOM 1595 CE LYS B 96 19.944 22.577 24.765 1.00 27.81 C ATOM 1596 NZ LYS B 96 19.453 21.155 24.737 1.00 30.75 N ATOM 1597 N GLY B 97 25.524 23.483 22.461 1.00 13.92 N ATOM 1598 CA GLY B 97 26.675 22.881 23.181 1.00 13.11 C ATOM 1599 C GLY B 97 27.662 23.957 23.593 1.00 13.07 C ATOM 1600 O GLY B 97 28.144 23.965 24.729 1.00 13.86 O ATOM 1601 N GLN B 98 27.942 24.883 22.715 1.00 12.47 N ATOM 1602 CA GLN B 98 28.858 25.982 23.051 1.00 11.96 C ATOM 1603 C GLN B 98 28.212 26.869 24.116 1.00 11.98 C ATOM 1604 O GLN B 98 28.979 27.376 24.955 1.00 11.85 O ATOM 1605 CB GLN B 98 29.234 26.812 21.830 1.00 13.22 C ATOM 1606 CG GLN B 98 30.195 26.049 20.905 1.00 14.42 C ATOM 1607 CD GLN B 98 30.405 26.800 19.599 1.00 15.12 C ATOM 1608 OE1 GLN B 98 29.337 27.170 18.934 1.00 14.08 O ATOM 1609 NE2 GLN B 98 31.567 27.092 19.206 1.00 17.95 N ATOM 1610 N LEU B 99 26.907 27.122 24.054 1.00 10.46 N ATOM 1611 CA LEU B 99 26.333 27.993 25.113 1.00 11.68 C ATOM 1612 C LEU B 99 26.411 27.284 26.458 1.00 11.81 C ATOM 1613 O LEU B 99 26.700 27.989 27.454 1.00 11.26 O ATOM 1614 CB LEU B 99 24.885 28.368 24.703 1.00 13.04 C ATOM 1615 CG LEU B 99 24.170 29.302 25.679 1.00 14.62 C ATOM 1616 CD1 LEU B 99 24.980 30.554 25.960 1.00 15.08 C ATOM 1617 CD2 LEU B 99 22.787 29.662 25.121 1.00 16.28 C ATOM 1618 N LYS B 100 26.116 25.986 26.486 1.00 12.46 N ATOM 1619 CA LYS B 100 26.312 25.258 27.775 1.00 14.80 C ATOM 1620 C LYS B 100 27.752 25.354 28.262 1.00 13.88 C ATOM 1621 O LYS B 100 27.936 25.522 29.498 1.00 14.98 O ATOM 1622 CB LYS B 100 25.807 23.805 27.740 1.00 17.98 C ATOM 1623 CG LYS B 100 24.328 23.876 27.331 1.00 22.43 C ATOM 1624 CD LYS B 100 23.309 22.952 27.854 1.00 26.13 C ATOM 1625 CE LYS B 100 23.701 21.502 27.950 1.00 29.23 C ATOM 1626 NZ LYS B 100 22.415 20.707 28.089 1.00 31.04 N ATOM 1627 N GLU B 101 28.762 25.253 27.396 1.00 13.77 N ATOM 1628 CA GLU B 101 30.169 25.408 27.800 1.00 14.07 C ATOM 1629 C GLU B 101 30.445 26.804 28.335 1.00 13.17 C ATOM 1630 O GLU B 101 31.132 26.937 29.363 1.00 13.40 O ATOM 1631 CB GLU B 101 31.110 25.227 26.594 1.00 16.68 C ATOM 1632 CG GLU B 101 31.233 23.743 26.168 1.00 19.04 C ATOM 1633 CD GLU B 101 32.163 23.666 24.968 1.00 20.67 C ATOM 1634 OE1 GLU B 101 32.049 24.300 23.940 1.00 21.77 O ATOM 1635 OE2 GLU B 101 33.159 22.998 25.258 1.00 23.29 O ATOM 1636 N PHE B 102 29.892 27.797 27.679 1.00 12.08 N ATOM 1637 CA PHE B 102 30.034 29.208 28.114 1.00 11.43 C ATOM 1638 C PHE B 102 29.443 29.351 29.521 1.00 12.01 C ATOM 1639 O PHE B 102 30.074 29.975 30.394 1.00 11.82 O ATOM 1640 CB PHE B 102 29.374 30.146 27.099 1.00 12.52 C ATOM 1641 CG PHE B 102 29.437 31.611 27.444 1.00 13.39 C ATOM 1642 CD1 PHE B 102 28.314 32.227 28.006 1.00 14.60 C ATOM 1643 CD2 PHE B 102 30.616 32.326 27.240 1.00 13.17 C ATOM 1644 CE1 PHE B 102 28.335 33.601 28.318 1.00 15.32 C ATOM 1645 CE2 PHE B 102 30.616 33.692 27.562 1.00 12.39 C ATOM 1646 CZ PHE B 102 29.492 34.312 28.079 1.00 12.95 C ATOM 1647 N LEU B 103 28.274 28.749 29.746 1.00 11.99 N ATOM 1648 CA LEU B 103 27.686 28.882 31.111 1.00 11.95 C ATOM 1649 C LEU B 103 28.495 28.116 32.145 1.00 11.33 C ATOM 1650 O LEU B 103 28.672 28.671 33.226 1.00 13.13 O ATOM 1651 CB LEU B 103 26.208 28.428 31.066 1.00 11.91 C ATOM 1652 CG LEU B 103 25.333 29.287 30.193 1.00 12.27 C ATOM 1653 CD1 LEU B 103 23.929 28.699 30.009 1.00 15.35 C ATOM 1654 CD2 LEU B 103 25.252 30.682 30.806 1.00 13.53 C ATOM 1655 N ASP B 104 28.936 26.927 31.836 1.00 12.67 N ATOM 1656 CA ASP B 104 29.717 26.116 32.783 1.00 15.82 C ATOM 1657 C ASP B 104 30.981 26.853 33.173 1.00 15.39 C ATOM 1658 O ASP B 104 31.459 26.778 34.346 1.00 15.00 O ATOM 1659 CB ASP B 104 30.007 24.727 32.178 1.00 19.47 C ATOM 1660 CG ASP B 104 30.581 23.875 33.307 1.00 23.99 C ATOM 1661 OD1 ASP B 104 29.830 23.513 34.245 1.00 26.85 O ATOM 1662 OD2 ASP B 104 31.819 23.635 33.336 1.00 25.69 O ATOM 1663 N ALA B 105 31.492 27.627 32.203 1.00 12.02 N ATOM 1664 CA ALA B 105 32.746 28.350 32.557 1.00 12.49 C ATOM 1665 C ALA B 105 32.553 29.477 33.558 1.00 12.99 C ATOM 1666 O ALA B 105 33.510 29.980 34.151 1.00 14.77 O ATOM 1667 CB ALA B 105 33.374 28.898 31.259 1.00 12.58 C ATOM 1668 N ASN B 106 31.313 29.927 33.725 1.00 10.58 N ATOM 1669 CA ASN B 106 31.005 31.138 34.466 1.00 11.76 C ATOM 1670 C ASN B 106 30.131 30.879 35.696 1.00 13.46 C ATOM 1671 O ASN B 106 30.153 31.789 36.523 1.00 14.23 O ATOM 1672 CB ASN B 106 30.268 32.099 33.510 1.00 11.88 C ATOM 1673 CG ASN B 106 31.226 32.806 32.564 1.00 12.35 C ATOM 1674 OD1 ASN B 106 32.002 33.657 32.973 1.00 13.38 O ATOM 1675 ND2 ASN B 106 31.216 32.466 31.270 1.00 12.95 N ATOM 1676 N LEU B 107 29.443 29.770 35.796 1.00 15.28 N ATOM 1677 CA LEU B 107 28.450 29.682 36.903 1.00 18.38 C ATOM 1678 C LEU B 107 28.687 28.441 37.757 1.00 21.98 C ATOM 1679 O LEU B 107 29.074 27.448 37.159 1.00 23.49 O ATOM 1680 CB LEU B 107 27.026 29.618 36.332 1.00 18.70 C ATOM 1681 CG LEU B 107 26.609 30.873 35.569 1.00 19.61 C ATOM 1682 CD1 LEU B 107 25.303 30.582 34.863 1.00 20.52 C ATOM 1683 CD2 LEU B 107 26.492 32.044 36.530 1.00 20.72 C ATOM 1684 N ALA B 108 28.470 28.652 39.045 1.00 25.81 N ATOM 1685 CA ALA B 108 28.548 27.541 40.012 1.00 29.38 C ATOM 1686 C ALA B 108 27.113 27.194 40.424 1.00 31.86 C ATOM 1687 O ALA B 108 26.183 27.969 40.106 1.00 32.16 O ATOM 1688 CB ALA B 108 29.368 27.921 41.227 1.00 30.02 C ATOM 1689 OXT ALA B 108 26.995 26.160 41.099 1.00 35.42 O TER 1690 ALA B 108 HETATM 1691 CU CU A 109 20.784 24.263 -3.038 1.00 19.01 CU HETATM 1692 C1 MPD A 601 22.066 43.909 7.477 0.75 29.38 C HETATM 1693 C2 MPD A 601 21.051 44.948 7.040 0.75 30.39 C HETATM 1694 O2 MPD A 601 21.454 45.555 5.787 0.75 19.79 O HETATM 1695 CM MPD A 601 19.729 44.241 6.724 0.75 23.44 C HETATM 1696 C3 MPD A 601 20.760 45.938 8.129 0.75 24.28 C HETATM 1697 C4 MPD A 601 21.848 46.902 8.496 0.75 31.16 C HETATM 1698 O4 MPD A 601 22.241 47.681 7.324 0.75 22.95 O HETATM 1699 C5 MPD A 601 21.296 47.867 9.549 0.75 25.64 C HETATM 1700 C1 MPD A 605 38.885 22.843 -15.734 0.55 58.02 C HETATM 1701 C2 MPD A 605 38.357 23.149 -14.327 0.55 57.51 C HETATM 1702 O2 MPD A 605 38.951 22.205 -13.404 0.55 60.33 O HETATM 1703 CM MPD A 605 38.841 24.546 -13.964 0.55 58.26 C HETATM 1704 C3 MPD A 605 36.853 23.060 -14.340 0.55 55.70 C HETATM 1705 C4 MPD A 605 36.188 22.809 -13.014 0.55 52.17 C HETATM 1706 O4 MPD A 605 36.082 24.048 -12.271 0.55 56.02 O HETATM 1707 C5 MPD A 605 34.765 22.285 -13.243 0.55 60.57 C HETATM 1708 C1 MPD A 606 46.534 38.537 -1.632 0.75 43.14 C HETATM 1709 C2 MPD A 606 45.507 39.104 -2.604 0.75 54.26 C HETATM 1710 O2 MPD A 606 44.567 39.924 -1.859 0.75 61.78 O HETATM 1711 CM MPD A 606 46.248 39.979 -3.614 0.75 50.04 C HETATM 1712 C3 MPD A 606 44.757 38.025 -3.364 0.75 39.98 C HETATM 1713 C4 MPD A 606 43.803 37.284 -2.448 0.75 51.13 C HETATM 1714 O4 MPD A 606 42.566 38.025 -2.315 0.75 49.20 O HETATM 1715 C5 MPD A 606 43.526 35.900 -2.974 0.75 38.60 C HETATM 1716 C1 MPD A 607 36.391 40.671 -10.529 0.55 59.17 C HETATM 1717 C2 MPD A 607 36.963 42.083 -10.334 0.55 52.06 C HETATM 1718 O2 MPD A 607 38.332 42.019 -10.812 0.55 56.27 O HETATM 1719 CM MPD A 607 36.174 43.007 -11.248 0.55 55.53 C HETATM 1720 C3 MPD A 607 36.878 42.435 -8.876 0.55 45.78 C HETATM 1721 C4 MPD A 607 37.139 43.865 -8.497 0.55 62.34 C HETATM 1722 O4 MPD A 607 36.527 44.172 -7.213 0.55 50.30 O HETATM 1723 C5 MPD A 607 38.626 44.172 -8.469 0.55 59.00 C HETATM 1724 CU CU B 109 8.410 30.145 25.459 1.00 27.45 CU HETATM 1725 C1 MPD B 602 17.306 39.938 7.332 0.65 42.44 C HETATM 1726 C2 MPD B 602 16.650 38.717 7.986 0.65 50.51 C HETATM 1727 O2 MPD B 602 15.836 39.197 9.110 0.65 48.14 O HETATM 1728 CM MPD B 602 15.659 38.121 6.995 0.65 56.00 C HETATM 1729 C3 MPD B 602 17.700 37.796 8.526 0.65 39.68 C HETATM 1730 C4 MPD B 602 18.104 36.594 7.718 0.65 45.04 C HETATM 1731 O4 MPD B 602 19.533 36.606 7.510 0.65 44.28 O HETATM 1732 C5 MPD B 602 17.679 35.298 8.388 0.65 43.42 C HETATM 1733 C1 MPD B 603 30.072 43.542 24.478 1.00 42.91 C HETATM 1734 C2 MPD B 603 31.603 43.598 24.490 1.00 51.69 C HETATM 1735 O2 MPD B 603 32.078 42.477 25.274 1.00 42.39 O HETATM 1736 CM MPD B 603 32.022 43.392 23.036 1.00 62.02 C HETATM 1737 C3 MPD B 603 32.051 44.923 25.038 1.00 45.21 C HETATM 1738 C4 MPD B 603 33.527 45.130 25.222 1.00 50.88 C HETATM 1739 O4 MPD B 603 33.795 46.571 25.183 1.00 61.26 O HETATM 1740 C5 MPD B 603 34.023 44.686 26.593 1.00 45.03 C HETATM 1741 C1 MPD B 604 25.097 47.924 14.515 0.55 55.95 C HETATM 1742 C2 MPD B 604 24.874 48.498 15.918 0.55 49.56 C HETATM 1743 O2 MPD B 604 26.010 49.334 16.246 0.55 59.92 O HETATM 1744 CM MPD B 604 23.617 49.354 15.870 0.55 52.36 C HETATM 1745 C3 MPD B 604 24.723 47.353 16.880 0.55 47.14 C HETATM 1746 C4 MPD B 604 25.018 47.660 18.319 0.55 50.81 C HETATM 1747 O4 MPD B 604 24.769 49.035 18.680 0.55 54.34 O HETATM 1748 C5 MPD B 604 24.176 46.744 19.200 0.55 54.26 C HETATM 1749 O HOH A 402 29.396 44.583 6.834 0.95 17.71 O HETATM 1750 O HOH A 403 30.033 30.918 -8.325 0.99 19.30 O HETATM 1751 O HOH A 404 26.404 26.318 3.759 0.93 16.54 O HETATM 1752 O HOH A 405 23.214 24.483 -2.005 0.99 19.24 O HETATM 1753 O HOH A 406 34.701 18.605 -10.205 0.80 24.92 O HETATM 1754 O HOH A 408 26.118 27.177 -5.744 1.00 23.72 O HETATM 1755 O HOH A 410 25.391 38.875 -3.080 1.00 16.95 O HETATM 1756 O HOH A 412 34.070 34.782 14.482 1.00 19.24 O HETATM 1757 O HOH A 413 27.065 23.698 4.464 1.00 22.97 O HETATM 1758 O HOH A 414 31.420 17.802 -9.789 1.00 35.41 O HETATM 1759 O HOH A 419 20.405 20.444 -1.363 0.87 14.35 O HETATM 1760 O HOH A 420 27.137 35.289 14.507 0.99 16.97 O HETATM 1761 O HOH A 421 22.211 38.936 9.064 0.83 22.15 O HETATM 1762 O HOH A 422 26.265 37.758 13.963 0.92 19.86 O HETATM 1763 O HOH A 425 30.314 27.607 9.940 0.83 24.68 O HETATM 1764 O HOH A 428 34.879 34.306 10.677 1.00 15.61 O HETATM 1765 O HOH A 429 50.990 40.405 -8.192 0.87 28.10 O HETATM 1766 O HOH A 431 31.217 30.708 18.815 1.00 23.99 O HETATM 1767 O HOH A 435 23.417 39.866 -11.209 0.95 58.28 O HETATM 1768 O HOH A 436 25.154 36.195 -4.365 0.83 16.51 O HETATM 1769 O HOH A 437 27.688 45.864 11.163 0.84 39.62 O HETATM 1770 O HOH A 438 41.585 37.690 -6.557 1.00 26.00 O HETATM 1771 O HOH A 439 33.905 25.070 11.188 0.93 28.66 O HETATM 1772 O HOH A 442 23.063 18.508 -3.461 0.99 34.96 O HETATM 1773 O HOH A 443 37.320 16.226 -8.844 0.53 20.96 O HETATM 1774 O HOH A 444 27.067 31.239 -8.518 1.00 30.97 O HETATM 1775 O HOH A 446 27.019 31.968 12.723 1.00 39.16 O HETATM 1776 O HOH A 447 34.344 32.015 12.274 1.00 20.18 O HETATM 1777 O HOH A 448 26.583 42.753 13.840 0.68 20.95 O HETATM 1778 O HOH A 449 23.792 21.934 -1.257 1.00 27.06 O HETATM 1779 O HOH A 450 28.265 48.699 3.462 0.76 32.65 O HETATM 1780 O HOH A 451 32.677 43.572 -3.878 1.00 20.44 O HETATM 1781 O HOH A 452 39.242 30.479 -13.452 0.92 22.25 O HETATM 1782 O HOH A 455 22.786 36.877 -6.246 0.89 49.28 O HETATM 1783 O HOH A 456 44.544 37.043 7.616 0.89 21.95 O HETATM 1784 O HOH A 457 23.096 40.753 -3.886 0.84 30.95 O HETATM 1785 O HOH A 462 26.956 34.176 11.585 0.65 56.67 O HETATM 1786 O HOH A 463 31.317 44.696 -11.258 1.00 54.48 O HETATM 1787 O HOH A 468 17.282 27.973 1.776 0.48 35.87 O HETATM 1788 O HOH A 470 26.774 43.547 9.407 1.00 19.87 O HETATM 1789 O HOH A 471 22.692 37.720 4.567 1.00 49.53 O HETATM 1790 O HOH A 472 25.997 39.690 -11.700 1.00 27.33 O HETATM 1791 O HOH A 473 22.444 17.403 3.042 1.00 29.98 O HETATM 1792 O HOH A 474 31.363 44.873 3.548 1.00 30.24 O HETATM 1793 O HOH A 476 24.063 28.777 -8.231 0.41 19.45 O HETATM 1794 O HOH A 477 33.111 15.725 4.613 0.59 55.53 O HETATM 1795 O HOH A 485 40.113 15.366 -2.934 0.82 36.14 O HETATM 1796 O HOH A 486 20.529 33.519 2.725 0.83 37.02 O HETATM 1797 O HOH A 487 38.147 30.341 -6.631 0.45 19.23 O HETATM 1798 O HOH A 489 34.219 30.778 15.387 1.00 35.60 O HETATM 1799 O HOH A 490 23.311 30.350 -4.870 0.89 43.21 O HETATM 1800 O HOH A 493 26.302 33.010 9.388 1.00 35.47 O HETATM 1801 O HOH A 494 33.856 44.861 -6.185 0.69 28.86 O HETATM 1802 O HOH A 496 26.832 23.970 7.918 0.96 33.88 O HETATM 1803 O HOH A 499 32.336 45.189 -8.847 0.64 31.28 O HETATM 1804 O HOH A 507 48.313 39.117 -7.404 0.91 36.09 O HETATM 1805 O HOH A 508 38.027 38.230 -13.035 0.65 25.27 O HETATM 1806 O HOH A 511 23.687 26.159 -7.975 0.79 43.05 O HETATM 1807 O HOH A 512 36.269 14.370 -7.049 0.81 44.67 O HETATM 1808 O HOH A 514 33.548 34.773 -18.224 0.89 45.79 O HETATM 1809 O HOH A 515 34.629 39.412 14.209 1.00 38.90 O HETATM 1810 O HOH A 516 28.235 48.776 -1.657 0.52 28.71 O HETATM 1811 O HOH A 517 31.197 47.729 2.436 1.00 51.00 O HETATM 1812 O HOH A 518 40.828 17.147 -9.551 1.00 46.48 O HETATM 1813 O HOH A 519 24.671 48.042 -8.260 1.00 60.99 O HETATM 1814 O HOH A 520 41.229 35.973 14.431 0.72 26.55 O HETATM 1815 O HOH A 521 40.083 34.555 -11.154 0.79 42.63 O HETATM 1816 O HOH A 524 30.993 15.284 -8.418 0.93 53.96 O HETATM 1817 O HOH A 525 47.422 15.529 -1.183 1.00 57.93 O HETATM 1818 O HOH A 527 31.932 19.490 -11.721 0.57 37.80 O HETATM 1819 O HOH A 530 15.324 23.895 -1.238 0.93 44.28 O HETATM 1820 O HOH A 534 37.079 40.916 11.859 0.53 29.08 O HETATM 1821 O HOH A 536 19.795 37.957 2.660 0.47 35.80 O HETATM 1822 O HOH A 539 27.226 30.760 9.922 0.85 46.28 O HETATM 1823 O HOH A 540 40.612 45.488 5.505 0.59 40.36 O HETATM 1824 O HOH B 401 30.339 33.478 16.727 1.00 17.61 O HETATM 1825 O HOH B 407 32.247 34.886 35.483 0.93 17.79 O HETATM 1826 O HOH B 409 20.165 50.675 17.627 0.67 24.40 O HETATM 1827 O HOH B 411 14.090 32.923 22.264 1.00 28.71 O HETATM 1828 O HOH B 415 29.670 43.595 20.432 1.00 24.28 O HETATM 1829 O HOH B 416 13.385 44.732 24.036 1.00 23.38 O HETATM 1830 O HOH B 417 32.639 36.673 17.385 1.00 23.61 O HETATM 1831 O HOH B 418 12.458 23.913 25.361 1.00 60.26 O HETATM 1832 O HOH B 423 8.144 26.529 27.446 1.00 25.34 O HETATM 1833 O HOH B 424 21.941 40.212 37.784 1.00 20.01 O HETATM 1834 O HOH B 426 24.147 26.938 36.069 0.89 54.36 O HETATM 1835 O HOH B 427 14.336 21.913 34.304 0.52 42.12 O HETATM 1836 O HOH B 430 23.698 27.164 38.624 0.60 49.93 O HETATM 1837 O HOH B 432 14.897 30.303 33.070 1.00 19.07 O HETATM 1838 O HOH B 433 13.251 41.824 22.915 0.91 18.74 O HETATM 1839 O HOH B 434 8.009 36.229 28.935 0.84 38.88 O HETATM 1840 O HOH B 440 18.122 34.742 37.746 0.73 24.99 O HETATM 1841 O HOH B 441 22.732 23.891 18.590 1.00 29.20 O HETATM 1842 O HOH B 445 31.725 41.195 37.394 0.45 18.55 O HETATM 1843 O HOH B 453 20.666 49.174 22.459 1.00 19.46 O HETATM 1844 O HOH B 454 10.761 47.139 23.353 1.00 50.09 O HETATM 1845 O HOH B 458 14.163 44.503 15.165 1.00 21.91 O HETATM 1846 O HOH B 459 21.688 50.552 20.015 0.91 30.60 O HETATM 1847 O HOH B 460 28.779 45.769 35.273 0.81 32.95 O HETATM 1848 O HOH B 461 9.933 29.502 36.191 0.78 51.80 O HETATM 1849 O HOH B 464 24.011 55.568 25.064 0.98 58.43 O HETATM 1850 O HOH B 465 14.563 31.294 36.210 1.00 33.02 O HETATM 1851 O HOH B 466 26.157 25.462 34.268 1.00 51.84 O HETATM 1852 O HOH B 467 28.464 40.269 41.187 1.00 36.34 O HETATM 1853 O HOH B 469 32.362 44.336 35.588 1.00 50.52 O HETATM 1854 O HOH B 475 32.777 32.205 38.249 1.00 24.27 O HETATM 1855 O HOH B 478 10.784 30.401 26.569 1.00 24.41 O HETATM 1856 O HOH B 479 14.240 32.771 31.963 1.00 18.27 O HETATM 1857 O HOH B 480 18.077 36.413 19.223 1.00 18.28 O HETATM 1858 O HOH B 481 14.999 36.724 18.976 0.93 24.75 O HETATM 1859 O HOH B 482 14.125 47.487 12.124 0.83 26.19 O HETATM 1860 O HOH B 483 20.384 33.084 39.541 0.83 29.84 O HETATM 1861 O HOH B 484 13.515 53.986 19.363 0.87 37.68 O HETATM 1862 O HOH B 488 19.681 51.587 29.578 1.00 31.84 O HETATM 1863 O HOH B 491 25.435 48.145 34.353 1.00 39.53 O HETATM 1864 O HOH B 492 16.293 52.706 16.743 0.96 31.60 O HETATM 1865 O HOH B 495 11.517 28.234 27.761 0.91 30.96 O HETATM 1866 O HOH B 497 12.213 46.373 30.839 0.49 33.68 O HETATM 1867 O HOH B 498 19.234 49.659 14.769 1.00 59.59 O HETATM 1868 O HOH B 500 5.160 29.087 31.065 0.76 44.39 O HETATM 1869 O HOH B 501 25.404 21.709 20.090 0.61 26.77 O HETATM 1870 O HOH B 502 11.137 24.946 22.821 0.81 48.72 O HETATM 1871 O HOH B 503 27.680 51.069 19.720 0.67 59.82 O HETATM 1872 O HOH B 504 23.342 51.470 32.735 1.00 52.80 O HETATM 1873 O HOH B 505 8.659 40.224 29.995 0.95 48.02 O HETATM 1874 O HOH B 506 30.411 25.431 36.620 1.00 51.19 O HETATM 1875 O HOH B 509 13.538 24.890 20.764 0.90 41.62 O HETATM 1876 O HOH B 510 26.264 25.199 31.597 1.00 43.81 O HETATM 1877 O HOH B 513 13.709 35.631 17.058 0.86 32.66 O HETATM 1878 O HOH B 522 24.194 19.021 29.933 0.60 45.73 O HETATM 1879 O HOH B 523 19.945 22.792 19.860 0.91 49.51 O HETATM 1880 O HOH B 526 18.801 53.874 31.989 0.60 37.91 O HETATM 1881 O HOH B 528 15.771 41.061 42.160 1.00 43.05 O HETATM 1882 O HOH B 529 29.038 22.833 19.098 0.58 27.76 O HETATM 1883 O HOH B 531 18.858 38.057 46.752 0.71 39.43 O HETATM 1884 O HOH B 532 11.134 36.262 22.719 0.67 36.86 O HETATM 1885 O HOH B 533 17.378 37.038 38.611 0.82 43.41 O HETATM 1886 O HOH B 535 12.748 47.737 32.940 0.85 56.90 O HETATM 1887 O HOH B 537 26.985 50.290 33.430 1.00 60.67 O HETATM 1888 O HOH B 538 12.233 30.720 19.502 0.42 26.30 O CONECT 1 1691 CONECT 7 1691 CONECT 13 1691 CONECT 272 289 CONECT 289 272 CONECT 851 1724 CONECT 857 1724 CONECT 863 1724 CONECT 1116 1133 CONECT 1133 1116 CONECT 1691 1 7 13 1752 CONECT 1692 1693 CONECT 1693 1692 1694 1695 1696 CONECT 1694 1693 CONECT 1695 1693 CONECT 1696 1693 1697 CONECT 1697 1696 1698 1699 CONECT 1698 1697 CONECT 1699 1697 CONECT 1700 1701 CONECT 1701 1700 1702 1703 1704 CONECT 1702 1701 CONECT 1703 1701 CONECT 1704 1701 1705 CONECT 1705 1704 1706 1707 CONECT 1706 1705 CONECT 1707 1705 CONECT 1708 1709 CONECT 1709 1708 1710 1711 1712 CONECT 1710 1709 CONECT 1711 1709 CONECT 1712 1709 1713 CONECT 1713 1712 1714 1715 CONECT 1714 1713 CONECT 1715 1713 CONECT 1716 1717 CONECT 1717 1716 1718 1719 1720 CONECT 1718 1717 CONECT 1719 1717 CONECT 1720 1717 1721 CONECT 1721 1720 1722 1723 CONECT 1722 1721 CONECT 1723 1721 CONECT 1724 851 857 863 1855 CONECT 1725 1726 CONECT 1726 1725 1727 1728 1729 CONECT 1727 1726 CONECT 1728 1726 CONECT 1729 1726 1730 CONECT 1730 1729 1731 1732 CONECT 1731 1730 CONECT 1732 1730 CONECT 1733 1734 CONECT 1734 1733 1735 1736 1737 CONECT 1735 1734 CONECT 1736 1734 CONECT 1737 1734 1738 CONECT 1738 1737 1739 1740 CONECT 1739 1738 CONECT 1740 1738 CONECT 1741 1742 CONECT 1742 1741 1743 1744 1745 CONECT 1743 1742 CONECT 1744 1742 CONECT 1745 1742 1746 CONECT 1746 1745 1747 1748 CONECT 1747 1746 CONECT 1748 1746 CONECT 1752 1691 CONECT 1855 1724 MASTER 353 3 9 10 10 10 14 6 1842 2 70 18 END