Browse entries in the PDBbind-CN Database
HEADER TRANSPORT PROTEIN 07-MAR-09 3GJ6 TITLE CRYSTAL STRUCTURE OF HUMAN RANGDP-NUP153ZNF1 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GTPASE RAN, RAS-RELATED NUCLEAR PROTEIN, RAS-LIKE COMPND 5 PROTEIN TC4, ANDROGEN RECEPTOR-ASSOCIATED PROTEIN 24; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NUCLEAR PORE COMPLEX PROTEIN NUP153; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: NUP153 - ZINC FINGER MODULE 1: UNP RESIDUES 658- COMPND 12 686; COMPND 13 SYNONYM: NUCLEOPORIN NUP153, 153 KDA NUCLEOPORIN; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: RAN, ARA24, OK/SW-CL.81; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 13 ORGANISM_COMMON: RAT; SOURCE 14 ORGANISM_TAXID: 10116; SOURCE 15 GENE: NUP153; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 18 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1 KEYWDS G PROTEIN, GDP, RAN, NUCLEAR PORE, NUP153, ZINC FINGER, KEYWDS 2 ACETYLATION, CYTOPLASM, GTP-BINDING, HOST-VIRUS KEYWDS 3 INTERACTION, ISOPEPTIDE BOND, NUCLEOTIDE-BINDING, NUCLEUS, KEYWDS 4 PHOSPHOPROTEIN, POLYMORPHISM, PROTEIN TRANSPORT, TRANSPORT, KEYWDS 5 UBL CONJUGATION, DNA-BINDING, METAL-BINDING, MRNA KEYWDS 6 TRANSPORT, NUCLEAR PORE COMPLEX, TRANSLOCATION, ZINC, ZINC- KEYWDS 7 FINGER, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.R.PARTRIDGE,T.U.SCHWARTZ REVDAT 1 04-AUG-09 3GJ6 0 JRNL AUTH J.R.PARTRIDGE,T.U.SCHWARTZ JRNL TITL CRYSTALLOGRAPHIC AND BIOCHEMICAL ANALYSIS OF THE JRNL TITL 2 RAN-BINDING ZINC FINGER DOMAIN. JRNL REF J.MOL.BIOL. V. 391 375 2009 JRNL REFN ISSN 0022-2836 JRNL PMID 19505478 JRNL DOI 10.1016/J.JMB.2009.06.011 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.12 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 7461 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.214 REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.279 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 12.570 REMARK 3 FREE R VALUE TEST SET COUNT : 938 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 36.1194 - 5.1625 0.99 1029 138 0.1976 0.2713 REMARK 3 2 5.1625 - 4.0994 1.00 956 149 0.1607 0.2110 REMARK 3 3 4.0994 - 3.5818 0.98 922 138 0.1940 0.2592 REMARK 3 4 3.5818 - 3.2545 0.99 940 134 0.1979 0.3270 REMARK 3 5 3.2545 - 3.0214 1.00 916 147 0.2101 0.2695 REMARK 3 6 3.0214 - 2.8433 0.97 933 115 0.2370 0.3566 REMARK 3 7 2.8433 - 2.7000 0.90 827 117 0.2823 0.3766 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.25 REMARK 3 B_SOL : 48.93 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.810 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.100 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 47.33 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 1892 REMARK 3 ANGLE : 1.138 2570 REMARK 3 CHIRALITY : 0.074 286 REMARK 3 PLANARITY : 0.004 323 REMARK 3 DIHEDRAL : 16.536 690 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -4.4270 26.9383 13.7668 REMARK 3 T TENSOR REMARK 3 T11: 0.1650 T22: 0.1924 REMARK 3 T33: 0.2547 T12: -0.0331 REMARK 3 T13: -0.0471 T23: -0.0811 REMARK 3 L TENSOR REMARK 3 L11: 2.9077 L22: 2.1367 REMARK 3 L33: 1.3794 L12: 0.1912 REMARK 3 L13: 0.0684 L23: -0.3487 REMARK 3 S TENSOR REMARK 3 S11: -0.0926 S12: 0.1424 S13: -0.4817 REMARK 3 S21: -0.1938 S22: 0.1788 S23: 0.0750 REMARK 3 S31: 0.0684 S32: -0.0137 S33: -0.0688 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3GJ6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-09. REMARK 100 THE RCSB ID CODE IS RCSB051926. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-AUG-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7528 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07000 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.70000 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.620 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3GJ3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 18-20% PEG REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 30.06600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.15250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.06600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.15250 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 234 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -4 REMARK 465 PRO A -3 REMARK 465 HIS A -2 REMARK 465 MET A -1 REMARK 465 ALA A 0 REMARK 465 SER A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 GLN A 4 REMARK 465 GLY A 5 REMARK 465 LEU A 209 REMARK 465 PRO A 210 REMARK 465 ASP A 211 REMARK 465 GLU A 212 REMARK 465 ASP A 213 REMARK 465 ASP A 214 REMARK 465 ASP A 215 REMARK 465 LEU A 216 REMARK 465 GLY B 653 REMARK 465 PRO B 654 REMARK 465 LEU B 655 REMARK 465 GLY B 656 REMARK 465 SER B 657 REMARK 465 ALA B 658 REMARK 465 GLY B 659 REMARK 465 SER B 660 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 LEU A 43 -5.82 -140.27 REMARK 500 ALA A 67 34.76 -92.90 REMARK 500 GLN A 82 12.04 48.81 REMARK 500 CYS A 85 168.12 178.02 REMARK 500 LEU A 108 -65.19 -90.30 REMARK 500 ASN A 114 75.20 44.81 REMARK 500 VAL A 137 -20.20 -142.92 REMARK 500 LYS A 142 -131.73 69.59 REMARK 500 ASN A 143 54.73 -141.74 REMARK 500 VAL A 203 12.85 -64.25 REMARK 500 THR A 207 -66.16 -123.13 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 MG A 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 24 OG1 REMARK 620 2 HOH A 217 O 109.4 REMARK 620 3 HOH A 220 O 99.3 126.5 REMARK 620 4 HOH A 218 O 161.4 74.2 65.9 REMARK 620 5 HOH A 219 O 108.2 112.2 99.5 86.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 300 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 664 SG REMARK 620 2 CYS B 667 SG 118.2 REMARK 620 3 CYS B 678 SG 100.0 107.1 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 302 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3CH5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE RANGDP-NUP153ZNF2 COMPLEX REMARK 900 RELATED ID: 2GQE RELATED DB: PDB REMARK 900 MOLECULAR CHARACTERIZATION OF THE RAN BINDING ZINC FINGER REMARK 900 DOMAIN REMARK 900 RELATED ID: 1BYU RELATED DB: PDB REMARK 900 CANINE GDP-RAN REMARK 900 RELATED ID: 3GJ0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN REMARK 900 RELATED ID: 3GJ3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN IN COMPLEX WITH REMARK 900 NUP153 - ZINC FINGER MODULE 2 REMARK 900 RELATED ID: 3GJ4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN IN COMPLEX WITH REMARK 900 NUP153 - ZINC FINGER MODULE 3 REMARK 900 RELATED ID: 3GJ5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 4 REMARK 900 RELATED ID: 3GJ7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 12 REMARK 900 RELATED ID: 3GJ8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 34 DBREF 3GJ6 A 2 216 UNP P62826 RAN_HUMAN 2 216 DBREF 3GJ6 B 658 686 UNP P49791 NU153_RAT 658 686 SEQADV 3GJ6 GLY A -4 UNP P62826 EXPRESSION TAG SEQADV 3GJ6 PRO A -3 UNP P62826 EXPRESSION TAG SEQADV 3GJ6 HIS A -2 UNP P62826 EXPRESSION TAG SEQADV 3GJ6 MET A -1 UNP P62826 EXPRESSION TAG SEQADV 3GJ6 ALA A 0 UNP P62826 EXPRESSION TAG SEQADV 3GJ6 SER A 1 UNP P62826 EXPRESSION TAG SEQADV 3GJ6 SER A 35 UNP P62826 PHE 35 ENGINEERED SEQADV 3GJ6 GLY B 653 UNP P49791 EXPRESSION TAG SEQADV 3GJ6 PRO B 654 UNP P49791 EXPRESSION TAG SEQADV 3GJ6 LEU B 655 UNP P49791 EXPRESSION TAG SEQADV 3GJ6 GLY B 656 UNP P49791 EXPRESSION TAG SEQADV 3GJ6 SER B 657 UNP P49791 EXPRESSION TAG SEQRES 1 A 221 GLY PRO HIS MET ALA SER ALA ALA GLN GLY GLU PRO GLN SEQRES 2 A 221 VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY THR SEQRES 3 A 221 GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY GLU SEQRES 4 A 221 SER GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU VAL SEQRES 5 A 221 HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE LYS SEQRES 6 A 221 PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE GLY SEQRES 7 A 221 GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS ALA SEQRES 8 A 221 ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR LYS SEQRES 9 A 221 ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL CYS SEQRES 10 A 221 GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL ASP SEQRES 11 A 221 ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL PHE SEQRES 12 A 221 HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER ALA SEQRES 13 A 221 LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP LEU SEQRES 14 A 221 ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE VAL SEQRES 15 A 221 ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET ASP SEQRES 16 A 221 PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU VAL SEQRES 17 A 221 ALA GLN THR THR ALA LEU PRO ASP GLU ASP ASP ASP LEU SEQRES 1 B 34 GLY PRO LEU GLY SER ALA GLY SER SER TRP GLN CYS ASP SEQRES 2 B 34 THR CYS LEU LEU GLN ASN LYS VAL THR ASP ASN LYS CYS SEQRES 3 B 34 ILE ALA CYS GLN ALA ALA LYS LEU HET MG A 301 1 HET GDP A 302 28 HET ZN B 300 1 HETNAM MG MAGNESIUM ION HETNAM GDP GUANOSINE-5'-DIPHOSPHATE HETNAM ZN ZINC ION FORMUL 3 MG MG 2+ FORMUL 4 GDP C10 H15 N5 O11 P2 FORMUL 5 ZN ZN 2+ FORMUL 6 HOH *34(H2 O) HELIX 1 1 GLY A 22 LYS A 28 1 7 HELIX 2 2 HIS A 30 LYS A 37 1 8 HELIX 3 3 GLY A 68 GLY A 73 5 6 HELIX 4 4 ARG A 76 ILE A 81 1 6 HELIX 5 5 SER A 94 ASN A 100 1 7 HELIX 6 6 ASN A 100 ARG A 110 1 11 HELIX 7 7 LYS A 132 ILE A 136 5 5 HELIX 8 8 VAL A 137 LYS A 141 5 5 HELIX 9 9 SER A 150 ASN A 154 5 5 HELIX 10 10 GLU A 158 GLY A 170 1 13 HELIX 11 11 ASP A 190 THR A 206 1 17 SHEET 1 A 7 LYS A 38 VAL A 40 0 SHEET 2 A 7 VAL A 45 THR A 54 -1 O VAL A 47 N LYS A 38 SHEET 3 A 7 GLY A 57 THR A 66 -1 O GLY A 57 N THR A 54 SHEET 4 A 7 GLN A 10 GLY A 17 1 N PHE A 11 O ASN A 62 SHEET 5 A 7 CYS A 85 ASP A 91 1 O MET A 89 N VAL A 16 SHEET 6 A 7 ILE A 117 ASN A 122 1 O CYS A 120 N ILE A 88 SHEET 7 A 7 LEU A 144 ASP A 148 1 O GLN A 145 N LEU A 119 SHEET 1 B 3 LYS A 38 VAL A 40 0 SHEET 2 B 3 VAL A 45 THR A 54 -1 O VAL A 47 N LYS A 38 SHEET 3 B 3 PHE A 176 ALA A 178 -1 O VAL A 177 N HIS A 53 LINK OG1 THR A 24 MG MG A 301 1555 1555 2.28 LINK SG CYS B 664 ZN ZN B 300 1555 1555 2.81 LINK SG CYS B 667 ZN ZN B 300 1555 1555 2.58 LINK SG CYS B 678 ZN ZN B 300 1555 1555 2.62 LINK MG MG A 301 O HOH A 217 1555 1555 2.45 LINK MG MG A 301 O HOH A 220 1555 1555 2.35 LINK MG MG A 301 O HOH A 218 1555 1555 2.48 LINK MG MG A 301 O HOH A 219 1555 1555 2.42 SITE 1 AC1 7 THR A 24 THR A 66 HOH A 217 HOH A 218 SITE 2 AC1 7 HOH A 219 HOH A 220 GDP A 302 SITE 1 AC2 19 GLY A 20 THR A 21 GLY A 22 LYS A 23 SITE 2 AC2 19 THR A 24 THR A 25 ASN A 122 LYS A 123 SITE 3 AC2 19 ASP A 125 ILE A 126 SER A 150 ALA A 151 SITE 4 AC2 19 LYS A 152 HOH A 217 HOH A 218 HOH A 220 SITE 5 AC2 19 HOH A 226 MG A 301 LYS B 672 SITE 1 AC3 4 CYS B 664 CYS B 667 CYS B 678 CYS B 681 CRYST1 60.132 80.305 54.634 90.00 90.00 90.00 P 21 21 2 4 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 0.016630 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012453 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018304 0.00000 ATOM 1 N GLU A 6 -12.958 42.655 7.935 1.00128.75 N ANISOU 1 N GLU A 6 16527 16346 16047 1538 1063 -1714 N ATOM 2 CA GLU A 6 -13.469 41.764 6.897 1.00131.47 C ANISOU 2 CA GLU A 6 16721 16698 16534 1494 1003 -1454 C ATOM 3 C GLU A 6 -12.584 40.533 6.678 1.00137.42 C ANISOU 3 C GLU A 6 17485 17576 17151 1340 879 -1323 C ATOM 4 O GLU A 6 -11.360 40.650 6.546 1.00133.58 O ANISOU 4 O GLU A 6 17111 17057 16585 1234 750 -1392 O ATOM 5 CB GLU A 6 -13.670 42.524 5.585 1.00126.78 C ANISOU 5 CB GLU A 6 16087 15871 16214 1495 899 -1398 C ATOM 6 CG GLU A 6 -14.855 43.476 5.609 1.00124.81 C ANISOU 6 CG GLU A 6 15758 15498 16167 1664 1024 -1445 C ATOM 7 CD GLU A 6 -15.190 44.025 4.236 1.00116.48 C ANISOU 7 CD GLU A 6 14632 14239 15386 1664 908 -1320 C ATOM 8 OE1 GLU A 6 -14.373 44.798 3.690 1.00115.71 O ANISOU 8 OE1 GLU A 6 14641 13974 15349 1602 788 -1381 O ATOM 9 OE2 GLU A 6 -16.272 43.686 3.708 1.00107.89 O ANISOU 9 OE2 GLU A 6 13377 13164 14453 1722 932 -1152 O ATOM 10 N PRO A 7 -13.215 39.344 6.643 1.00143.09 N ANISOU 10 N PRO A 7 18076 18430 17863 1330 922 -1133 N ATOM 11 CA PRO A 7 -12.584 38.022 6.510 1.00140.33 C ANISOU 11 CA PRO A 7 17710 18198 17412 1206 832 -990 C ATOM 12 C PRO A 7 -12.267 37.665 5.056 1.00130.70 C ANISOU 12 C PRO A 7 16445 16862 16352 1102 667 -866 C ATOM 13 O PRO A 7 -13.027 38.020 4.155 1.00131.14 O ANISOU 13 O PRO A 7 16416 16806 16605 1135 650 -801 O ATOM 14 CB PRO A 7 -13.654 37.063 7.060 1.00142.36 C ANISOU 14 CB PRO A 7 17830 18611 17648 1258 972 -841 C ATOM 15 CG PRO A 7 -14.784 37.949 7.588 1.00144.89 C ANISOU 15 CG PRO A 7 18102 18919 18032 1416 1151 -929 C ATOM 16 CD PRO A 7 -14.669 39.226 6.833 1.00143.88 C ANISOU 16 CD PRO A 7 18024 18574 18070 1450 1079 -1049 C ATOM 17 N GLN A 8 -11.165 36.955 4.832 1.00118.62 N ANISOU 17 N GLN A 8 14967 15369 14734 981 549 -833 N ATOM 18 CA GLN A 8 -10.719 36.664 3.472 1.00103.13 C ANISOU 18 CA GLN A 8 12983 13308 12893 879 402 -748 C ATOM 19 C GLN A 8 -11.126 35.272 2.988 1.00 91.09 C ANISOU 19 C GLN A 8 11340 11851 11420 824 377 -566 C ATOM 20 O GLN A 8 -11.326 34.366 3.797 1.00 94.84 O ANISOU 20 O GLN A 8 11773 12455 11807 831 447 -498 O ATOM 21 CB GLN A 8 -9.205 36.831 3.365 1.00 97.40 C ANISOU 21 CB GLN A 8 12377 12556 12074 779 286 -837 C ATOM 22 CG GLN A 8 -8.691 36.646 1.956 1.00 99.44 C ANISOU 22 CG GLN A 8 12621 12720 12442 679 155 -767 C ATOM 23 CD GLN A 8 -7.190 36.796 1.851 1.00103.38 C ANISOU 23 CD GLN A 8 13216 13200 12863 581 56 -847 C ATOM 24 OE1 GLN A 8 -6.664 37.104 0.781 1.00100.84 O ANISOU 24 OE1 GLN A 8 12910 12782 12620 509 -31 -836 O ATOM 25 NE2 GLN A 8 -6.489 36.577 2.962 1.00104.73 N ANISOU 25 NE2 GLN A 8 13444 13474 12876 574 69 -920 N ATOM 26 N VAL A 9 -11.244 35.113 1.667 1.00 74.51 N ANISOU 26 N VAL A 9 9189 9661 9462 764 276 -488 N ATOM 27 CA VAL A 9 -11.557 33.815 1.057 1.00 65.09 C ANISOU 27 CA VAL A 9 7893 8506 8333 695 230 -343 C ATOM 28 C VAL A 9 -10.309 33.024 0.650 1.00 63.59 C ANISOU 28 C VAL A 9 7757 8324 8079 580 125 -342 C ATOM 29 O VAL A 9 -9.615 33.369 -0.315 1.00 65.69 O ANISOU 29 O VAL A 9 8076 8512 8372 515 26 -379 O ATOM 30 CB VAL A 9 -12.500 33.958 -0.170 1.00 58.23 C ANISOU 30 CB VAL A 9 6926 7556 7644 692 173 -258 C ATOM 31 CG1 VAL A 9 -12.403 32.729 -1.085 1.00 55.69 C ANISOU 31 CG1 VAL A 9 6543 7244 7372 582 75 -161 C ATOM 32 CG2 VAL A 9 -13.936 34.163 0.285 1.00 50.53 C ANISOU 32 CG2 VAL A 9 5828 6606 6765 800 286 -200 C ATOM 33 N GLN A 10 -10.029 31.956 1.387 1.00 60.64 N ANISOU 33 N GLN A 10 7364 8047 7628 558 154 -288 N ATOM 34 CA GLN A 10 -8.853 31.138 1.098 1.00 54.85 C ANISOU 34 CA GLN A 10 6666 7318 6855 465 66 -283 C ATOM 35 C GLN A 10 -9.109 29.643 1.252 1.00 55.68 C ANISOU 35 C GLN A 10 6681 7473 7002 430 74 -152 C ATOM 36 O GLN A 10 -9.880 29.218 2.115 1.00 60.80 O ANISOU 36 O GLN A 10 7267 8197 7637 479 168 -67 O ATOM 37 CB GLN A 10 -7.674 31.567 1.975 1.00 52.32 C ANISOU 37 CB GLN A 10 6456 7046 6379 466 58 -384 C ATOM 38 CG GLN A 10 -7.978 31.598 3.454 1.00 56.22 C ANISOU 38 CG GLN A 10 6964 7659 6737 540 162 -386 C ATOM 39 CD GLN A 10 -6.895 32.302 4.240 1.00 61.60 C ANISOU 39 CD GLN A 10 7765 8382 7259 539 135 -519 C ATOM 40 OE1 GLN A 10 -7.167 33.208 5.042 1.00 55.83 O ANISOU 40 OE1 GLN A 10 7093 7684 6436 608 206 -621 O ATOM 41 NE2 GLN A 10 -5.649 31.903 4.001 1.00 64.05 N ANISOU 41 NE2 GLN A 10 8106 8687 7544 461 32 -530 N ATOM 42 N PHE A 11 -8.453 28.846 0.410 1.00 55.44 N ANISOU 42 N PHE A 11 6641 7394 7030 346 -16 -135 N ATOM 43 CA PHE A 11 -8.568 27.388 0.488 1.00 59.74 C ANISOU 43 CA PHE A 11 7105 7951 7643 305 -20 -22 C ATOM 44 C PHE A 11 -7.209 26.757 0.642 1.00 53.54 C ANISOU 44 C PHE A 11 6365 7169 6808 261 -76 -41 C ATOM 45 O PHE A 11 -6.242 27.236 0.047 1.00 53.38 O ANISOU 45 O PHE A 11 6411 7111 6759 226 -141 -141 O ATOM 46 CB PHE A 11 -9.194 26.821 -0.785 1.00 58.40 C ANISOU 46 CB PHE A 11 6859 7701 7631 245 -80 12 C ATOM 47 CG PHE A 11 -10.422 27.547 -1.235 1.00 55.31 C ANISOU 47 CG PHE A 11 6415 7292 7309 278 -62 25 C ATOM 48 CD1 PHE A 11 -11.650 27.269 -0.672 1.00 60.83 C ANISOU 48 CD1 PHE A 11 7006 8031 8076 322 18 129 C ATOM 49 CD2 PHE A 11 -10.344 28.498 -2.232 1.00 45.93 C ANISOU 49 CD2 PHE A 11 5274 6050 6129 266 -127 -50 C ATOM 50 CE1 PHE A 11 -12.784 27.928 -1.098 1.00 67.14 C ANISOU 50 CE1 PHE A 11 7736 8814 8962 360 30 148 C ATOM 51 CE2 PHE A 11 -11.469 29.159 -2.655 1.00 57.80 C ANISOU 51 CE2 PHE A 11 6718 7533 7711 304 -123 -21 C ATOM 52 CZ PHE A 11 -12.693 28.873 -2.090 1.00 66.51 C ANISOU 52 CZ PHE A 11 7703 8673 8893 354 -47 75 C ATOM 53 N LYS A 12 -7.122 25.673 1.409 1.00 52.91 N ANISOU 53 N LYS A 12 6240 7132 6732 262 -52 68 N ATOM 54 CA LYS A 12 -5.890 24.878 1.408 1.00 47.85 C ANISOU 54 CA LYS A 12 5613 6473 6096 222 -117 72 C ATOM 55 C LYS A 12 -5.870 23.984 0.170 1.00 49.35 C ANISOU 55 C LYS A 12 5748 6548 6454 154 -175 69 C ATOM 56 O LYS A 12 -6.798 23.206 -0.055 1.00 54.40 O ANISOU 56 O LYS A 12 6306 7147 7218 135 -158 154 O ATOM 57 CB LYS A 12 -5.762 24.031 2.674 1.00 43.65 C ANISOU 57 CB LYS A 12 5051 6019 5514 250 -80 208 C ATOM 58 CG LYS A 12 -4.729 22.924 2.552 1.00 41.64 C ANISOU 58 CG LYS A 12 4771 5714 5337 214 -149 254 C ATOM 59 CD LYS A 12 -4.547 22.204 3.869 1.00 45.63 C ANISOU 59 CD LYS A 12 5254 6307 5776 246 -124 410 C ATOM 60 CE LYS A 12 -3.463 21.161 3.770 1.00 46.84 C ANISOU 60 CE LYS A 12 5373 6396 6026 224 -200 461 C ATOM 61 NZ LYS A 12 -3.122 20.668 5.125 1.00 56.32 N ANISOU 61 NZ LYS A 12 6568 7706 7127 260 -197 619 N ATOM 62 N LEU A 13 -4.836 24.118 -0.647 1.00 42.99 N ANISOU 62 N LEU A 13 4986 5695 5654 114 -240 -36 N ATOM 63 CA LEU A 13 -4.707 23.289 -1.832 1.00 42.01 C ANISOU 63 CA LEU A 13 4824 5473 5665 52 -288 -69 C ATOM 64 C LEU A 13 -3.451 22.423 -1.701 1.00 48.76 C ANISOU 64 C LEU A 13 5669 6298 6561 42 -318 -72 C ATOM 65 O LEU A 13 -2.342 22.952 -1.653 1.00 57.11 O ANISOU 65 O LEU A 13 6774 7385 7540 45 -342 -144 O ATOM 66 CB LEU A 13 -4.628 24.167 -3.082 1.00 37.34 C ANISOU 66 CB LEU A 13 4283 4855 5050 13 -325 -190 C ATOM 67 CG LEU A 13 -4.566 23.472 -4.453 1.00 44.15 C ANISOU 67 CG LEU A 13 5125 5640 6011 -57 -372 -253 C ATOM 68 CD1 LEU A 13 -4.763 24.472 -5.576 1.00 50.73 C ANISOU 68 CD1 LEU A 13 6009 6478 6788 -91 -404 -334 C ATOM 69 CD2 LEU A 13 -3.284 22.693 -4.683 1.00 33.50 C ANISOU 69 CD2 LEU A 13 3774 4251 4702 -77 -388 -308 C ATOM 70 N VAL A 14 -3.601 21.104 -1.630 1.00 50.45 N ANISOU 70 N VAL A 14 5811 6444 6914 30 -321 9 N ATOM 71 CA VAL A 14 -2.418 20.237 -1.544 1.00 49.62 C ANISOU 71 CA VAL A 14 5682 6290 6881 33 -350 12 C ATOM 72 C VAL A 14 -1.930 19.817 -2.926 1.00 39.86 C ANISOU 72 C VAL A 14 4442 4955 5749 -17 -379 -122 C ATOM 73 O VAL A 14 -2.721 19.478 -3.795 1.00 45.84 O ANISOU 73 O VAL A 14 5181 5647 6588 -63 -386 -162 O ATOM 74 CB VAL A 14 -2.650 18.990 -0.671 1.00 46.45 C ANISOU 74 CB VAL A 14 5205 5849 6594 54 -338 180 C ATOM 75 CG1 VAL A 14 -2.704 19.375 0.802 1.00 44.42 C ANISOU 75 CG1 VAL A 14 4965 5723 6190 109 -309 308 C ATOM 76 CG2 VAL A 14 -3.905 18.238 -1.108 1.00 43.12 C ANISOU 76 CG2 VAL A 14 4720 5339 6323 13 -321 232 C ATOM 77 N LEU A 15 -0.624 19.861 -3.133 1.00 36.29 N ANISOU 77 N LEU A 15 4001 4501 5285 -11 -397 -198 N ATOM 78 CA LEU A 15 -0.071 19.583 -4.447 1.00 50.94 C ANISOU 78 CA LEU A 15 5859 6288 7209 -53 -403 -342 C ATOM 79 C LEU A 15 0.735 18.285 -4.391 1.00 54.24 C ANISOU 79 C LEU A 15 6206 6606 7798 -30 -406 -332 C ATOM 80 O LEU A 15 1.844 18.265 -3.864 1.00 55.72 O ANISOU 80 O LEU A 15 6369 6818 7983 9 -415 -311 O ATOM 81 CB LEU A 15 0.817 20.746 -4.914 1.00 49.59 C ANISOU 81 CB LEU A 15 5747 6191 6905 -68 -403 -450 C ATOM 82 CG LEU A 15 0.904 20.985 -6.427 1.00 47.80 C ANISOU 82 CG LEU A 15 5555 5945 6663 -128 -395 -594 C ATOM 83 CD1 LEU A 15 1.851 22.119 -6.764 1.00 41.46 C ANISOU 83 CD1 LEU A 15 4799 5214 5741 -147 -386 -666 C ATOM 84 CD2 LEU A 15 1.308 19.731 -7.165 1.00 57.37 C ANISOU 84 CD2 LEU A 15 6718 7058 8022 -140 -382 -672 C ATOM 85 N VAL A 16 0.168 17.208 -4.933 1.00 46.61 N ANISOU 85 N VAL A 16 5199 5517 6993 -56 -406 -347 N ATOM 86 CA VAL A 16 0.784 15.896 -4.849 1.00 47.49 C ANISOU 86 CA VAL A 16 5237 5499 7306 -27 -406 -330 C ATOM 87 C VAL A 16 1.071 15.322 -6.223 1.00 55.76 C ANISOU 87 C VAL A 16 6285 6445 8457 -65 -392 -519 C ATOM 88 O VAL A 16 0.513 15.772 -7.227 1.00 54.47 O ANISOU 88 O VAL A 16 6176 6309 8212 -126 -392 -638 O ATOM 89 CB VAL A 16 -0.092 14.896 -4.067 1.00 45.26 C ANISOU 89 CB VAL A 16 4895 5129 7173 -20 -414 -160 C ATOM 90 CG1 VAL A 16 -0.310 15.372 -2.643 1.00 50.21 C ANISOU 90 CG1 VAL A 16 5522 5874 7681 23 -414 31 C ATOM 91 CG2 VAL A 16 -1.413 14.671 -4.772 1.00 46.70 C ANISOU 91 CG2 VAL A 16 5081 5254 7409 -90 -419 -200 C ATOM 92 N GLY A 17 1.954 14.322 -6.243 1.00 55.59 N ANISOU 92 N GLY A 17 6200 6308 8613 -23 -379 -545 N ATOM 93 CA GLY A 17 2.344 13.618 -7.450 1.00 41.95 C ANISOU 93 CA GLY A 17 4465 4470 7005 -43 -350 -739 C ATOM 94 C GLY A 17 3.780 13.164 -7.297 1.00 60.45 C ANISOU 94 C GLY A 17 6740 6766 9462 32 -320 -766 C ATOM 95 O GLY A 17 4.475 13.603 -6.379 1.00 63.64 O ANISOU 95 O GLY A 17 7115 7253 9813 83 -336 -646 O ATOM 96 N ASP A 18 4.230 12.285 -8.190 1.00 65.63 N ANISOU 96 N ASP A 18 7368 7291 10279 39 -279 -931 N ATOM 97 CA ASP A 18 5.593 11.766 -8.154 1.00 55.51 C ANISOU 97 CA ASP A 18 6002 5947 9143 121 -238 -972 C ATOM 98 C ASP A 18 6.632 12.880 -8.054 1.00 60.97 C ANISOU 98 C ASP A 18 6692 6813 9662 139 -218 -979 C ATOM 99 O ASP A 18 6.424 13.990 -8.558 1.00 61.50 O ANISOU 99 O ASP A 18 6841 7023 9503 77 -206 -1044 O ATOM 100 CB ASP A 18 5.865 10.910 -9.394 1.00 58.91 C ANISOU 100 CB ASP A 18 6423 6241 9717 117 -172 -1212 C ATOM 101 CG ASP A 18 5.404 9.458 -9.225 1.00 88.38 C ANISOU 101 CG ASP A 18 10102 9731 13747 139 -192 -1191 C ATOM 102 OD1 ASP A 18 4.825 9.124 -8.167 1.00 99.87 O ANISOU 102 OD1 ASP A 18 11524 11132 15289 150 -254 -969 O ATOM 103 OD2 ASP A 18 5.630 8.643 -10.148 1.00 91.76 O ANISOU 103 OD2 ASP A 18 10520 10018 14325 143 -140 -1397 O ATOM 104 N GLY A 19 7.748 12.587 -7.394 1.00 57.80 N ANISOU 104 N GLY A 19 6190 6393 9380 222 -221 -901 N ATOM 105 CA GLY A 19 8.857 13.518 -7.364 1.00 57.65 C ANISOU 105 CA GLY A 19 6144 6519 9241 235 -203 -922 C ATOM 106 C GLY A 19 9.401 13.661 -8.770 1.00 64.74 C ANISOU 106 C GLY A 19 7055 7432 10111 207 -100 -1158 C ATOM 107 O GLY A 19 9.408 12.688 -9.531 1.00 69.38 O ANISOU 107 O GLY A 19 7622 7884 10856 227 -41 -1299 O ATOM 108 N GLY A 20 9.844 14.864 -9.124 1.00 61.67 N ANISOU 108 N GLY A 20 6704 7206 9522 159 -74 -1205 N ATOM 109 CA GLY A 20 10.404 15.108 -10.440 1.00 51.18 C ANISOU 109 CA GLY A 20 5389 5925 8133 126 35 -1406 C ATOM 110 C GLY A 20 9.375 15.482 -11.489 1.00 60.33 C ANISOU 110 C GLY A 20 6682 7125 9115 33 56 -1523 C ATOM 111 O GLY A 20 9.719 15.727 -12.642 1.00 65.91 O ANISOU 111 O GLY A 20 7420 7894 9729 -7 146 -1685 O ATOM 112 N THR A 21 8.105 15.523 -11.098 1.00 56.88 N ANISOU 112 N THR A 21 6318 6665 8627 -3 -26 -1434 N ATOM 113 CA THR A 21 7.051 15.899 -12.032 1.00 57.61 C ANISOU 113 CA THR A 21 6527 6802 8558 -92 -32 -1521 C ATOM 114 C THR A 21 6.984 17.414 -12.275 1.00 59.03 C ANISOU 114 C THR A 21 6785 7155 8490 -157 -38 -1486 C ATOM 115 O THR A 21 6.425 17.852 -13.279 1.00 56.44 O ANISOU 115 O THR A 21 6544 6890 8009 -230 -27 -1571 O ATOM 116 CB THR A 21 5.683 15.331 -11.614 1.00 62.03 C ANISOU 116 CB THR A 21 7117 7268 9184 -108 -113 -1443 C ATOM 117 OG1 THR A 21 5.386 15.707 -10.264 1.00 63.23 O ANISOU 117 OG1 THR A 21 7248 7443 9333 -78 -182 -1232 O ATOM 118 CG2 THR A 21 5.708 13.821 -11.705 1.00 63.97 C ANISOU 118 CG2 THR A 21 7300 7323 9683 -66 -98 -1515 C ATOM 119 N GLY A 22 7.576 18.203 -11.373 1.00 61.88 N ANISOU 119 N GLY A 22 7113 7585 8815 -135 -62 -1362 N ATOM 120 CA GLY A 22 7.647 19.649 -11.544 1.00 63.40 C ANISOU 120 CA GLY A 22 7369 7912 8808 -194 -66 -1330 C ATOM 121 C GLY A 22 6.703 20.465 -10.664 1.00 55.28 C ANISOU 121 C GLY A 22 6400 6917 7686 -208 -154 -1187 C ATOM 122 O GLY A 22 6.432 21.631 -10.941 1.00 48.73 O ANISOU 122 O GLY A 22 5642 6170 6702 -261 -165 -1169 O ATOM 123 N LYS A 23 6.205 19.848 -9.598 1.00 54.29 N ANISOU 123 N LYS A 23 6242 6724 7660 -155 -211 -1082 N ATOM 124 CA LYS A 23 5.319 20.516 -8.650 1.00 50.71 C ANISOU 124 CA LYS A 23 5835 6308 7126 -154 -276 -951 C ATOM 125 C LYS A 23 5.911 21.824 -8.156 1.00 44.38 C ANISOU 125 C LYS A 23 5057 5604 6203 -167 -292 -911 C ATOM 126 O LYS A 23 5.291 22.872 -8.246 1.00 49.74 O ANISOU 126 O LYS A 23 5812 6333 6755 -204 -309 -893 O ATOM 127 CB LYS A 23 5.032 19.588 -7.464 1.00 48.98 C ANISOU 127 CB LYS A 23 5556 6019 7034 -89 -316 -829 C ATOM 128 CG LYS A 23 4.600 18.200 -7.895 1.00 49.04 C ANISOU 128 CG LYS A 23 5526 5898 7210 -78 -302 -867 C ATOM 129 CD LYS A 23 4.064 17.407 -6.728 1.00 60.61 C ANISOU 129 CD LYS A 23 6944 7296 8790 -30 -343 -710 C ATOM 130 CE LYS A 23 5.187 16.865 -5.874 1.00 59.83 C ANISOU 130 CE LYS A 23 6756 7172 8804 42 -355 -632 C ATOM 131 NZ LYS A 23 6.087 16.019 -6.699 1.00 67.91 N ANISOU 131 NZ LYS A 23 7715 8098 9989 64 -307 -759 N ATOM 132 N THR A 24 7.126 21.756 -7.638 1.00 51.73 N ANISOU 132 N THR A 24 5913 6551 7190 -137 -291 -900 N ATOM 133 CA THR A 24 7.802 22.949 -7.145 1.00 51.21 C ANISOU 133 CA THR A 24 5857 6570 7029 -160 -317 -876 C ATOM 134 C THR A 24 7.996 24.011 -8.231 1.00 56.90 C ANISOU 134 C THR A 24 6635 7339 7645 -238 -272 -954 C ATOM 135 O THR A 24 7.661 25.180 -8.028 1.00 55.28 O ANISOU 135 O THR A 24 6500 7173 7330 -274 -301 -925 O ATOM 136 CB THR A 24 9.135 22.606 -6.515 1.00 45.10 C ANISOU 136 CB THR A 24 4973 5809 6353 -122 -335 -854 C ATOM 137 OG1 THR A 24 8.895 22.084 -5.207 1.00 54.64 O ANISOU 137 OG1 THR A 24 6153 7008 7597 -61 -406 -735 O ATOM 138 CG2 THR A 24 9.973 23.849 -6.389 1.00 43.56 C ANISOU 138 CG2 THR A 24 4779 5695 6077 -175 -352 -870 C ATOM 139 N THR A 25 8.530 23.606 -9.381 1.00 57.74 N ANISOU 139 N THR A 25 6713 7442 7785 -262 -196 -1051 N ATOM 140 CA THR A 25 8.582 24.497 -10.538 1.00 57.69 C ANISOU 140 CA THR A 25 6768 7491 7662 -341 -144 -1108 C ATOM 141 C THR A 25 7.239 25.177 -10.806 1.00 50.67 C ANISOU 141 C THR A 25 5993 6606 6653 -375 -183 -1071 C ATOM 142 O THR A 25 7.190 26.323 -11.218 1.00 57.48 O ANISOU 142 O THR A 25 6915 7511 7414 -433 -182 -1053 O ATOM 143 CB THR A 25 8.996 23.743 -11.809 1.00 57.68 C ANISOU 143 CB THR A 25 6741 7492 7685 -356 -48 -1228 C ATOM 144 OG1 THR A 25 10.207 23.024 -11.562 1.00 60.96 O ANISOU 144 OG1 THR A 25 7032 7889 8242 -307 -3 -1265 O ATOM 145 CG2 THR A 25 9.209 24.712 -12.965 1.00 46.61 C ANISOU 145 CG2 THR A 25 5397 6173 6141 -443 13 -1265 C ATOM 146 N PHE A 26 6.148 24.467 -10.566 1.00 50.56 N ANISOU 146 N PHE A 26 5998 6542 6671 -339 -220 -1048 N ATOM 147 CA PHE A 26 4.835 24.968 -10.949 1.00 55.65 C ANISOU 147 CA PHE A 26 6728 7192 7227 -368 -256 -1016 C ATOM 148 C PHE A 26 4.270 26.011 -9.979 1.00 56.87 C ANISOU 148 C PHE A 26 6922 7353 7331 -350 -309 -920 C ATOM 149 O PHE A 26 3.916 27.112 -10.394 1.00 60.62 O ANISOU 149 O PHE A 26 7463 7853 7718 -390 -320 -898 O ATOM 150 CB PHE A 26 3.858 23.801 -11.144 1.00 54.08 C ANISOU 150 CB PHE A 26 6519 6934 7096 -348 -274 -1034 C ATOM 151 CG PHE A 26 2.437 24.220 -11.395 1.00 51.22 C ANISOU 151 CG PHE A 26 6216 6576 6669 -369 -326 -985 C ATOM 152 CD1 PHE A 26 2.010 24.553 -12.669 1.00 56.84 C ANISOU 152 CD1 PHE A 26 6985 7330 7283 -433 -330 -1032 C ATOM 153 CD2 PHE A 26 1.524 24.252 -10.361 1.00 46.05 C ANISOU 153 CD2 PHE A 26 5551 5893 6051 -325 -368 -887 C ATOM 154 CE1 PHE A 26 0.692 24.922 -12.903 1.00 50.71 C ANISOU 154 CE1 PHE A 26 6245 6559 6462 -449 -392 -975 C ATOM 155 CE2 PHE A 26 0.198 24.625 -10.587 1.00 50.94 C ANISOU 155 CE2 PHE A 26 6203 6517 6635 -337 -411 -837 C ATOM 156 CZ PHE A 26 -0.215 24.960 -11.859 1.00 46.77 C ANISOU 156 CZ PHE A 26 5721 6022 6026 -399 -431 -879 C ATOM 157 N VAL A 27 4.181 25.663 -8.698 1.00 49.93 N ANISOU 157 N VAL A 27 6008 6453 6509 -290 -340 -861 N ATOM 158 CA VAL A 27 3.684 26.600 -7.696 1.00 56.47 C ANISOU 158 CA VAL A 27 6877 7297 7280 -265 -377 -793 C ATOM 159 C VAL A 27 4.516 27.897 -7.688 1.00 57.59 C ANISOU 159 C VAL A 27 7052 7470 7361 -307 -379 -815 C ATOM 160 O VAL A 27 4.012 28.978 -7.342 1.00 52.18 O ANISOU 160 O VAL A 27 6427 6782 6618 -308 -401 -789 O ATOM 161 CB VAL A 27 3.654 25.963 -6.282 1.00 46.26 C ANISOU 161 CB VAL A 27 5540 6004 6033 -198 -402 -727 C ATOM 162 CG1 VAL A 27 5.057 25.750 -5.753 1.00 48.78 C ANISOU 162 CG1 VAL A 27 5799 6347 6389 -189 -412 -740 C ATOM 163 CG2 VAL A 27 2.880 26.838 -5.321 1.00 49.10 C ANISOU 163 CG2 VAL A 27 5951 6388 6315 -167 -424 -674 C ATOM 164 N LYS A 28 5.780 27.783 -8.094 1.00 58.63 N ANISOU 164 N LYS A 28 7136 7620 7521 -342 -353 -864 N ATOM 165 CA LYS A 28 6.711 28.917 -8.071 1.00 58.69 C ANISOU 165 CA LYS A 28 7151 7650 7498 -395 -355 -880 C ATOM 166 C LYS A 28 6.532 29.935 -9.199 1.00 50.23 C ANISOU 166 C LYS A 28 6145 6578 6361 -468 -328 -884 C ATOM 167 O LYS A 28 7.065 31.020 -9.111 1.00 55.59 O ANISOU 167 O LYS A 28 6843 7253 7024 -516 -337 -879 O ATOM 168 CB LYS A 28 8.171 28.437 -8.037 1.00 52.17 C ANISOU 168 CB LYS A 28 6225 6852 6745 -407 -334 -916 C ATOM 169 CG LYS A 28 8.571 27.788 -6.717 1.00 61.88 C ANISOU 169 CG LYS A 28 7389 8091 8033 -343 -389 -885 C ATOM 170 CD LYS A 28 10.061 27.513 -6.647 1.00 76.45 C ANISOU 170 CD LYS A 28 9120 9964 9963 -356 -384 -909 C ATOM 171 CE LYS A 28 10.481 26.957 -5.281 1.00 89.45 C ANISOU 171 CE LYS A 28 10700 11632 11656 -295 -463 -856 C ATOM 172 NZ LYS A 28 10.329 27.927 -4.151 1.00 95.97 N ANISOU 172 NZ LYS A 28 11583 12493 12388 -306 -547 -832 N ATOM 173 N ARG A 29 5.805 29.595 -10.257 1.00 45.57 N ANISOU 173 N ARG A 29 5588 5992 5736 -482 -302 -887 N ATOM 174 CA ARG A 29 5.599 30.546 -11.343 1.00 45.87 C ANISOU 174 CA ARG A 29 5690 6042 5697 -550 -285 -865 C ATOM 175 C ARG A 29 4.952 31.843 -10.841 1.00 53.89 C ANISOU 175 C ARG A 29 6773 7010 6693 -547 -335 -803 C ATOM 176 O ARG A 29 5.047 32.882 -11.496 1.00 55.17 O ANISOU 176 O ARG A 29 6980 7162 6819 -606 -330 -765 O ATOM 177 CB ARG A 29 4.725 29.935 -12.440 1.00 47.52 C ANISOU 177 CB ARG A 29 5929 6274 5852 -560 -277 -874 C ATOM 178 CG ARG A 29 5.229 28.630 -12.960 1.00 41.37 C ANISOU 178 CG ARG A 29 5096 5523 5100 -557 -225 -961 C ATOM 179 CD ARG A 29 6.664 28.732 -13.318 1.00 51.65 C ANISOU 179 CD ARG A 29 6347 6866 6410 -599 -151 -1007 C ATOM 180 NE ARG A 29 6.897 29.607 -14.462 1.00 64.88 N ANISOU 180 NE ARG A 29 8074 8601 7978 -683 -108 -986 N ATOM 181 CZ ARG A 29 8.114 29.936 -14.889 1.00 62.38 C ANISOU 181 CZ ARG A 29 7714 8332 7656 -737 -30 -1004 C ATOM 182 NH1 ARG A 29 9.183 29.466 -14.253 1.00 52.29 N ANISOU 182 NH1 ARG A 29 6335 7047 6486 -710 2 -1050 N ATOM 183 NH2 ARG A 29 8.265 30.728 -15.942 1.00 60.60 N ANISOU 183 NH2 ARG A 29 7536 8165 7323 -820 14 -963 N ATOM 184 N HIS A 30 4.291 31.761 -9.686 1.00 47.64 N ANISOU 184 N HIS A 30 5985 6186 5930 -475 -376 -790 N ATOM 185 CA HIS A 30 3.486 32.853 -9.144 1.00 48.27 C ANISOU 185 CA HIS A 30 6125 6214 6002 -448 -412 -750 C ATOM 186 C HIS A 30 4.354 33.620 -8.171 1.00 50.15 C ANISOU 186 C HIS A 30 6365 6430 6259 -458 -429 -785 C ATOM 187 O HIS A 30 4.587 33.166 -7.040 1.00 55.41 O ANISOU 187 O HIS A 30 7001 7117 6933 -412 -448 -813 O ATOM 188 CB HIS A 30 2.240 32.293 -8.436 1.00 57.70 C ANISOU 188 CB HIS A 30 7316 7402 7207 -362 -429 -725 C ATOM 189 CG HIS A 30 1.241 33.334 -8.018 1.00 55.77 C ANISOU 189 CG HIS A 30 7122 7104 6963 -319 -448 -689 C ATOM 190 ND1 HIS A 30 1.306 33.992 -6.811 1.00 59.12 N ANISOU 190 ND1 HIS A 30 7571 7503 7389 -277 -454 -719 N ATOM 191 CD2 HIS A 30 0.128 33.801 -8.645 1.00 47.32 C ANISOU 191 CD2 HIS A 30 6079 6003 5899 -305 -462 -630 C ATOM 192 CE1 HIS A 30 0.286 34.839 -6.714 1.00 48.82 C ANISOU 192 CE1 HIS A 30 6306 6143 6101 -232 -456 -691 C ATOM 193 NE2 HIS A 30 -0.431 34.747 -7.810 1.00 43.94 N ANISOU 193 NE2 HIS A 30 5684 5519 5494 -246 -465 -627 N ATOM 194 N LEU A 31 4.834 34.776 -8.631 1.00 43.63 N ANISOU 194 N LEU A 31 5575 5563 5440 -527 -429 -777 N ATOM 195 CA LEU A 31 5.829 35.588 -7.928 1.00 44.61 C ANISOU 195 CA LEU A 31 5695 5657 5597 -569 -453 -820 C ATOM 196 C LEU A 31 5.456 35.972 -6.496 1.00 54.08 C ANISOU 196 C LEU A 31 6927 6826 6793 -505 -498 -867 C ATOM 197 O LEU A 31 6.283 35.891 -5.590 1.00 57.04 O ANISOU 197 O LEU A 31 7271 7231 7170 -514 -531 -922 O ATOM 198 CB LEU A 31 6.144 36.846 -8.741 1.00 45.59 C ANISOU 198 CB LEU A 31 5859 5714 5747 -656 -445 -783 C ATOM 199 CG LEU A 31 6.754 36.579 -10.121 1.00 60.43 C ANISOU 199 CG LEU A 31 7706 7648 7605 -736 -389 -739 C ATOM 200 CD1 LEU A 31 6.894 37.859 -10.928 1.00 63.12 C ANISOU 200 CD1 LEU A 31 8094 7923 7964 -821 -380 -665 C ATOM 201 CD2 LEU A 31 8.105 35.870 -9.997 1.00 48.43 C ANISOU 201 CD2 LEU A 31 6089 6201 6111 -773 -360 -792 C ATOM 202 N THR A 32 4.218 36.397 -6.287 1.00 51.94 N ANISOU 202 N THR A 32 6715 6506 6513 -441 -498 -847 N ATOM 203 CA THR A 32 3.828 36.855 -4.966 1.00 50.16 C ANISOU 203 CA THR A 32 6529 6258 6270 -377 -520 -906 C ATOM 204 C THR A 32 3.715 35.675 -4.021 1.00 49.40 C ANISOU 204 C THR A 32 6391 6260 6120 -311 -521 -914 C ATOM 205 O THR A 32 4.104 35.770 -2.853 1.00 50.43 O ANISOU 205 O THR A 32 6530 6425 6207 -293 -552 -973 O ATOM 206 CB THR A 32 2.521 37.660 -4.998 1.00 47.88 C ANISOU 206 CB THR A 32 6303 5887 6004 -314 -505 -883 C ATOM 207 OG1 THR A 32 2.661 38.736 -5.933 1.00 51.52 O ANISOU 207 OG1 THR A 32 6799 6247 6528 -378 -511 -849 O ATOM 208 CG2 THR A 32 2.192 38.222 -3.607 1.00 40.48 C ANISOU 208 CG2 THR A 32 5412 4928 5041 -247 -510 -972 C ATOM 209 N GLY A 33 3.181 34.566 -4.535 1.00 47.69 N ANISOU 209 N GLY A 33 6129 6086 5904 -282 -493 -850 N ATOM 210 CA GLY A 33 3.089 33.341 -3.771 1.00 46.62 C ANISOU 210 CA GLY A 33 5944 6027 5743 -227 -491 -830 C ATOM 211 C GLY A 33 4.470 32.899 -3.350 1.00 48.38 C ANISOU 211 C GLY A 33 6113 6301 5966 -265 -526 -860 C ATOM 212 O GLY A 33 4.704 32.597 -2.186 1.00 42.25 O ANISOU 212 O GLY A 33 5326 5582 5144 -228 -557 -869 O ATOM 213 N GLU A 34 5.389 32.885 -4.307 1.00 55.02 N ANISOU 213 N GLU A 34 6917 7132 6857 -337 -521 -870 N ATOM 214 CA GLU A 34 6.780 32.513 -4.044 1.00 56.45 C ANISOU 214 CA GLU A 34 7023 7358 7066 -376 -551 -895 C ATOM 215 C GLU A 34 7.457 33.351 -2.957 1.00 52.19 C ANISOU 215 C GLU A 34 6501 6833 6496 -399 -619 -951 C ATOM 216 O GLU A 34 8.196 32.807 -2.135 1.00 57.52 O ANISOU 216 O GLU A 34 7118 7575 7163 -387 -670 -953 O ATOM 217 CB GLU A 34 7.613 32.577 -5.324 1.00 56.21 C ANISOU 217 CB GLU A 34 6949 7315 7093 -455 -513 -903 C ATOM 218 CG GLU A 34 9.114 32.574 -5.084 1.00 62.64 C ANISOU 218 CG GLU A 34 7676 8165 7957 -507 -542 -933 C ATOM 219 CD GLU A 34 9.648 31.228 -4.621 1.00 80.62 C ANISOU 219 CD GLU A 34 9855 10501 10278 -454 -555 -914 C ATOM 220 OE1 GLU A 34 9.131 30.192 -5.088 1.00 91.78 O ANISOU 220 OE1 GLU A 34 11250 11910 11713 -406 -509 -887 O ATOM 221 OE2 GLU A 34 10.595 31.205 -3.800 1.00 81.65 O ANISOU 221 OE2 GLU A 34 9919 10673 10431 -463 -619 -924 O ATOM 222 N SER A 35 7.210 34.660 -2.952 1.00 41.88 N ANISOU 222 N SER A 35 5274 5461 5178 -433 -628 -997 N ATOM 223 CA SER A 35 7.903 35.574 -2.031 1.00 57.74 C ANISOU 223 CA SER A 35 7306 7464 7168 -474 -699 -1079 C ATOM 224 C SER A 35 7.255 35.651 -0.650 1.00 53.45 C ANISOU 224 C SER A 35 6824 6963 6520 -399 -730 -1121 C ATOM 225 O SER A 35 7.901 36.017 0.329 1.00 48.05 O ANISOU 225 O SER A 35 6149 6321 5788 -423 -805 -1193 O ATOM 226 CB SER A 35 8.036 36.986 -2.637 1.00 65.70 C ANISOU 226 CB SER A 35 8370 8359 8236 -554 -696 -1118 C ATOM 227 OG SER A 35 6.768 37.602 -2.819 1.00 68.01 O ANISOU 227 OG SER A 35 8752 8571 8518 -502 -656 -1110 O ATOM 228 N GLU A 36 5.976 35.308 -0.576 1.00 61.72 N ANISOU 228 N GLU A 36 7912 8012 7528 -312 -672 -1078 N ATOM 229 CA GLU A 36 5.247 35.360 0.686 1.00 63.47 C ANISOU 229 CA GLU A 36 8189 8286 7639 -234 -673 -1110 C ATOM 230 C GLU A 36 5.066 33.974 1.255 1.00 59.22 C ANISOU 230 C GLU A 36 7594 7860 7047 -172 -667 -1021 C ATOM 231 O GLU A 36 4.486 33.806 2.331 1.00 57.64 O ANISOU 231 O GLU A 36 7429 7734 6739 -106 -657 -1018 O ATOM 232 CB GLU A 36 3.888 36.037 0.507 1.00 69.00 C ANISOU 232 CB GLU A 36 8962 8910 8345 -174 -603 -1120 C ATOM 233 CG GLU A 36 3.947 37.543 0.683 1.00 80.26 C ANISOU 233 CG GLU A 36 10472 10234 9791 -202 -620 -1237 C ATOM 234 CD GLU A 36 2.616 38.215 0.432 1.00 85.69 C ANISOU 234 CD GLU A 36 11213 10829 10516 -130 -549 -1236 C ATOM 235 OE1 GLU A 36 1.650 37.503 0.088 1.00 89.17 O ANISOU 235 OE1 GLU A 36 11620 11298 10964 -67 -492 -1140 O ATOM 236 OE2 GLU A 36 2.534 39.454 0.578 1.00 91.18 O ANISOU 236 OE2 GLU A 36 11978 11416 11251 -137 -554 -1330 O ATOM 237 N LYS A 37 5.571 32.982 0.528 1.00 57.59 N ANISOU 237 N LYS A 37 7300 7662 6920 -193 -666 -945 N ATOM 238 CA LYS A 37 5.408 31.592 0.938 1.00 62.21 C ANISOU 238 CA LYS A 37 7821 8319 7496 -137 -660 -845 C ATOM 239 C LYS A 37 5.962 31.419 2.335 1.00 60.48 C ANISOU 239 C LYS A 37 7600 8211 7169 -118 -732 -844 C ATOM 240 O LYS A 37 6.858 32.161 2.758 1.00 53.70 O ANISOU 240 O LYS A 37 6756 7376 6274 -170 -807 -928 O ATOM 241 CB LYS A 37 6.143 30.651 -0.001 1.00 61.76 C ANISOU 241 CB LYS A 37 7668 8240 7557 -168 -658 -798 C ATOM 242 CG LYS A 37 7.541 30.352 0.450 1.00 54.42 C ANISOU 242 CG LYS A 37 6663 7368 6648 -198 -736 -802 C ATOM 243 CD LYS A 37 8.388 29.869 -0.697 1.00 62.03 C ANISOU 243 CD LYS A 37 7536 8288 7743 -241 -714 -800 C ATOM 244 CE LYS A 37 9.870 29.990 -0.355 1.00 71.10 C ANISOU 244 CE LYS A 37 8601 9484 8929 -288 -791 -825 C ATOM 245 NZ LYS A 37 10.707 29.982 -1.583 1.00 72.34 N ANISOU 245 NZ LYS A 37 8683 9598 9205 -347 -746 -854 N ATOM 246 N LYS A 38 5.427 30.442 3.055 1.00 50.54 N ANISOU 246 N LYS A 38 6319 7024 5858 -51 -716 -743 N ATOM 247 CA LYS A 38 5.866 30.206 4.419 1.00 59.12 C ANISOU 247 CA LYS A 38 7408 8240 6814 -28 -787 -716 C ATOM 248 C LYS A 38 6.380 28.779 4.572 1.00 69.75 C ANISOU 248 C LYS A 38 8648 9628 8225 -4 -823 -573 C ATOM 249 O LYS A 38 6.403 28.011 3.609 1.00 63.13 O ANISOU 249 O LYS A 38 7741 8707 7541 -4 -785 -522 O ATOM 250 CB LYS A 38 4.752 30.548 5.404 1.00 59.96 C ANISOU 250 CB LYS A 38 7603 8417 6762 33 -734 -722 C ATOM 251 CG LYS A 38 4.117 31.915 5.099 1.00 69.65 C ANISOU 251 CG LYS A 38 8924 9566 7974 26 -681 -862 C ATOM 252 CD LYS A 38 3.524 32.582 6.334 1.00 82.19 C ANISOU 252 CD LYS A 38 10608 11244 9377 74 -656 -937 C ATOM 253 CE LYS A 38 4.601 33.207 7.218 1.00 90.37 C ANISOU 253 CE LYS A 38 11687 12360 10289 24 -772 -1050 C ATOM 254 NZ LYS A 38 4.005 33.946 8.370 1.00 95.27 N ANISOU 254 NZ LYS A 38 12418 13066 10714 70 -739 -1161 N ATOM 255 N TYR A 39 6.827 28.432 5.771 1.00 76.36 N ANISOU 255 N TYR A 39 9474 10591 8948 17 -901 -512 N ATOM 256 CA TYR A 39 7.536 27.173 5.953 1.00 65.60 C ANISOU 256 CA TYR A 39 7999 9258 7668 39 -959 -371 C ATOM 257 C TYR A 39 7.146 26.469 7.242 1.00 72.20 C ANISOU 257 C TYR A 39 8845 10223 8366 98 -982 -224 C ATOM 258 O TYR A 39 7.624 26.816 8.319 1.00 80.81 O ANISOU 258 O TYR A 39 9967 11452 9287 91 -1074 -231 O ATOM 259 CB TYR A 39 9.055 27.397 5.912 1.00 65.72 C ANISOU 259 CB TYR A 39 7940 9295 7737 -15 -1078 -419 C ATOM 260 CG TYR A 39 9.838 26.103 5.995 1.00 86.29 C ANISOU 260 CG TYR A 39 10410 11908 10469 19 -1136 -273 C ATOM 261 CD1 TYR A 39 9.979 25.279 4.882 1.00 88.73 C ANISOU 261 CD1 TYR A 39 10628 12091 10993 33 -1072 -241 C ATOM 262 CD2 TYR A 39 10.419 25.695 7.188 1.00 94.22 C ANISOU 262 CD2 TYR A 39 11376 13046 11377 41 -1256 -168 C ATOM 263 CE1 TYR A 39 10.675 24.095 4.955 1.00 91.73 C ANISOU 263 CE1 TYR A 39 10881 12455 11516 76 -1117 -116 C ATOM 264 CE2 TYR A 39 11.122 24.509 7.272 1.00 97.26 C ANISOU 264 CE2 TYR A 39 11628 13425 11901 83 -1314 -16 C ATOM 265 CZ TYR A 39 11.246 23.711 6.152 1.00103.71 C ANISOU 265 CZ TYR A 39 12353 14093 12959 104 -1239 5 C ATOM 266 OH TYR A 39 11.947 22.527 6.229 1.00116.57 O ANISOU 266 OH TYR A 39 13844 15692 14755 157 -1290 147 O ATOM 267 N VAL A 40 6.262 25.483 7.123 1.00 71.08 N ANISOU 267 N VAL A 40 8674 10040 8291 149 -900 -89 N ATOM 268 CA VAL A 40 5.963 24.578 8.222 1.00 63.83 C ANISOU 268 CA VAL A 40 7739 9229 7284 201 -914 100 C ATOM 269 C VAL A 40 7.117 23.593 8.362 1.00 68.74 C ANISOU 269 C VAL A 40 8243 9853 8024 210 -1024 226 C ATOM 270 O VAL A 40 7.274 22.697 7.530 1.00 60.41 O ANISOU 270 O VAL A 40 7096 8662 7195 223 -999 283 O ATOM 271 CB VAL A 40 4.697 23.793 7.932 1.00 68.32 C ANISOU 271 CB VAL A 40 8295 9726 7939 239 -793 213 C ATOM 272 CG1 VAL A 40 4.482 22.734 8.993 1.00 81.49 C ANISOU 272 CG1 VAL A 40 9926 11487 9551 285 -806 442 C ATOM 273 CG2 VAL A 40 3.525 24.727 7.871 1.00 71.10 C ANISOU 273 CG2 VAL A 40 8742 10087 8187 243 -686 109 C ATOM 274 N ALA A 41 7.931 23.769 9.400 1.00 77.74 N ANISOU 274 N ALA A 41 9382 11143 9014 206 -1149 261 N ATOM 275 CA ALA A 41 9.159 22.983 9.550 1.00 79.54 C ANISOU 275 CA ALA A 41 9483 11379 9361 216 -1276 374 C ATOM 276 C ALA A 41 8.889 21.639 10.220 1.00 79.28 C ANISOU 276 C ALA A 41 9390 11371 9361 281 -1286 636 C ATOM 277 O ALA A 41 9.685 20.711 10.118 1.00 86.68 O ANISOU 277 O ALA A 41 10202 12253 10478 310 -1358 762 O ATOM 278 CB ALA A 41 10.225 23.776 10.322 1.00 80.74 C ANISOU 278 CB ALA A 41 9644 11682 9353 172 -1432 300 C ATOM 279 N THR A 42 7.752 21.541 10.893 1.00 74.31 N ANISOU 279 N THR A 42 8842 10818 8573 305 -1206 725 N ATOM 280 CA THR A 42 7.375 20.321 11.583 1.00 75.16 C ANISOU 280 CA THR A 42 8902 10955 8700 357 -1201 996 C ATOM 281 C THR A 42 6.749 19.323 10.613 1.00 70.28 C ANISOU 281 C THR A 42 8213 10121 8370 379 -1094 1068 C ATOM 282 O THR A 42 6.331 18.235 11.011 1.00 73.48 O ANISOU 282 O THR A 42 8569 10499 8852 415 -1072 1294 O ATOM 283 CB THR A 42 6.374 20.620 12.722 1.00 83.32 C ANISOU 283 CB THR A 42 10046 12174 9437 369 -1140 1070 C ATOM 284 OG1 THR A 42 5.085 20.912 12.168 1.00 84.78 O ANISOU 284 OG1 THR A 42 10288 12277 9649 367 -971 988 O ATOM 285 CG2 THR A 42 6.841 21.816 13.544 1.00 85.93 C ANISOU 285 CG2 THR A 42 10477 12705 9467 338 -1226 921 C ATOM 286 N LEU A 43 6.688 19.697 9.338 1.00 64.17 N ANISOU 286 N LEU A 43 7436 9194 7753 350 -1030 876 N ATOM 287 CA LEU A 43 6.061 18.857 8.321 1.00 62.72 C ANISOU 287 CA LEU A 43 7198 8809 7823 357 -933 898 C ATOM 288 C LEU A 43 6.840 18.875 7.018 1.00 67.49 C ANISOU 288 C LEU A 43 7742 9262 8640 337 -940 736 C ATOM 289 O LEU A 43 6.510 18.152 6.078 1.00 72.91 O ANISOU 289 O LEU A 43 8381 9777 9543 340 -874 723 O ATOM 290 CB LEU A 43 4.631 19.321 8.045 1.00 56.40 C ANISOU 290 CB LEU A 43 6483 7996 6952 338 -801 833 C ATOM 291 CG LEU A 43 3.541 18.771 8.964 1.00 68.96 C ANISOU 291 CG LEU A 43 8088 9658 8456 364 -735 1036 C ATOM 292 CD1 LEU A 43 2.180 19.331 8.573 1.00 56.71 C ANISOU 292 CD1 LEU A 43 6597 8088 6862 346 -604 948 C ATOM 293 CD2 LEU A 43 3.533 17.235 8.938 1.00 82.07 C ANISOU 293 CD2 LEU A 43 9639 11188 10355 389 -743 1255 C ATOM 294 N GLY A 44 7.865 19.717 6.964 1.00 67.57 N ANISOU 294 N GLY A 44 7753 9339 8581 311 -1016 606 N ATOM 295 CA GLY A 44 8.659 19.871 5.763 1.00 75.45 C ANISOU 295 CA GLY A 44 8693 10223 9751 286 -1009 450 C ATOM 296 C GLY A 44 7.802 20.309 4.597 1.00 77.79 C ANISOU 296 C GLY A 44 9054 10417 10085 248 -891 297 C ATOM 297 O GLY A 44 7.587 19.548 3.650 1.00 81.80 O ANISOU 297 O GLY A 44 9515 10779 10788 255 -829 280 O ATOM 298 N VAL A 45 7.314 21.544 4.662 1.00 63.76 N ANISOU 298 N VAL A 45 7386 8716 8124 207 -866 181 N ATOM 299 CA VAL A 45 6.355 22.023 3.678 1.00 54.23 C ANISOU 299 CA VAL A 45 6244 7429 6931 176 -765 66 C ATOM 300 C VAL A 45 6.341 23.540 3.548 1.00 56.39 C ANISOU 300 C VAL A 45 6612 7759 7054 129 -763 -91 C ATOM 301 O VAL A 45 6.199 24.257 4.533 1.00 60.25 O ANISOU 301 O VAL A 45 7168 8363 7360 132 -794 -95 O ATOM 302 CB VAL A 45 4.947 21.539 4.031 1.00 60.11 C ANISOU 302 CB VAL A 45 7022 8165 7652 204 -695 175 C ATOM 303 CG1 VAL A 45 3.871 22.494 3.478 1.00 63.70 C ANISOU 303 CG1 VAL A 45 7565 8607 8032 176 -616 61 C ATOM 304 CG2 VAL A 45 4.741 20.125 3.534 1.00 56.10 C ANISOU 304 CG2 VAL A 45 6428 7522 7368 225 -667 273 C ATOM 305 N GLU A 46 6.497 24.012 2.317 1.00 52.17 N ANISOU 305 N GLU A 46 6083 7141 6598 84 -724 -221 N ATOM 306 CA GLU A 46 6.398 25.420 2.003 1.00 47.42 C ANISOU 306 CA GLU A 46 5568 6555 5896 35 -712 -356 C ATOM 307 C GLU A 46 4.983 25.687 1.511 1.00 57.47 C ANISOU 307 C GLU A 46 6908 7778 7150 41 -626 -372 C ATOM 308 O GLU A 46 4.553 25.126 0.498 1.00 63.65 O ANISOU 308 O GLU A 46 7664 8471 8049 33 -577 -373 O ATOM 309 CB GLU A 46 7.415 25.807 0.928 1.00 55.02 C ANISOU 309 CB GLU A 46 6490 7464 6951 -23 -717 -462 C ATOM 310 CG GLU A 46 8.826 26.078 1.461 1.00 73.89 C ANISOU 310 CG GLU A 46 8820 9921 9335 -48 -811 -481 C ATOM 311 CD GLU A 46 9.864 26.301 0.358 1.00 90.31 C ANISOU 311 CD GLU A 46 10831 11949 11534 -104 -795 -565 C ATOM 312 OE1 GLU A 46 9.491 26.677 -0.775 1.00 93.62 O ANISOU 312 OE1 GLU A 46 11289 12302 11982 -141 -717 -635 O ATOM 313 OE2 GLU A 46 11.066 26.099 0.627 1.00 94.85 O ANISOU 313 OE2 GLU A 46 11307 12562 12171 -112 -861 -553 O ATOM 314 N VAL A 47 4.250 26.519 2.251 1.00 47.85 N ANISOU 314 N VAL A 47 5772 6620 5787 57 -612 -388 N ATOM 315 CA VAL A 47 2.937 26.971 1.827 1.00 45.06 C ANISOU 315 CA VAL A 47 5472 6225 5423 68 -535 -409 C ATOM 316 C VAL A 47 3.046 28.256 0.994 1.00 42.28 C ANISOU 316 C VAL A 47 5180 5820 5065 20 -530 -539 C ATOM 317 O VAL A 47 3.743 29.193 1.372 1.00 51.49 O ANISOU 317 O VAL A 47 6389 7015 6161 -7 -574 -621 O ATOM 318 CB VAL A 47 2.033 27.206 3.035 1.00 49.71 C ANISOU 318 CB VAL A 47 6110 6904 5875 123 -500 -360 C ATOM 319 CG1 VAL A 47 0.835 28.033 2.629 1.00 43.85 C ANISOU 319 CG1 VAL A 47 5420 6118 5122 137 -428 -412 C ATOM 320 CG2 VAL A 47 1.602 25.871 3.659 1.00 45.67 C ANISOU 320 CG2 VAL A 47 5535 6427 5390 165 -481 -194 C ATOM 321 N HIS A 48 2.365 28.291 -0.145 1.00 43.18 N ANISOU 321 N HIS A 48 5295 5852 5257 3 -486 -552 N ATOM 322 CA HIS A 48 2.469 29.411 -1.083 1.00 53.35 C ANISOU 322 CA HIS A 48 6632 7083 6554 -47 -483 -642 C ATOM 323 C HIS A 48 1.138 30.134 -1.311 1.00 52.21 C ANISOU 323 C HIS A 48 6540 6903 6395 -19 -438 -643 C ATOM 324 O HIS A 48 0.303 29.633 -2.054 1.00 53.43 O ANISOU 324 O HIS A 48 6667 7022 6614 -15 -411 -597 O ATOM 325 CB HIS A 48 2.917 28.883 -2.448 1.00 48.91 C ANISOU 325 CB HIS A 48 6025 6467 6092 -98 -477 -654 C ATOM 326 CG HIS A 48 4.308 28.377 -2.478 1.00 47.10 C ANISOU 326 CG HIS A 48 5734 6256 5906 -127 -509 -672 C ATOM 327 ND1 HIS A 48 5.352 29.085 -3.063 1.00 57.46 N ANISOU 327 ND1 HIS A 48 7045 7558 7228 -191 -522 -741 N ATOM 328 CD2 HIS A 48 4.867 27.231 -2.021 1.00 46.45 C ANISOU 328 CD2 HIS A 48 5575 6195 5878 -98 -528 -620 C ATOM 329 CE1 HIS A 48 6.463 28.406 -2.947 1.00 53.55 C ANISOU 329 CE1 HIS A 48 6468 7087 6790 -198 -545 -739 C ATOM 330 NE2 HIS A 48 6.200 27.264 -2.316 1.00 46.99 N ANISOU 330 NE2 HIS A 48 5591 6270 5991 -137 -553 -665 N ATOM 331 N PRO A 49 0.945 31.327 -0.717 1.00 53.08 N ANISOU 331 N PRO A 49 6719 7015 6434 -1 -434 -703 N ATOM 332 CA PRO A 49 -0.343 32.013 -0.924 1.00 48.52 C ANISOU 332 CA PRO A 49 6175 6393 5868 42 -387 -699 C ATOM 333 C PRO A 49 -0.469 32.514 -2.357 1.00 47.31 C ANISOU 333 C PRO A 49 6030 6153 5792 -8 -397 -705 C ATOM 334 O PRO A 49 0.169 33.512 -2.656 1.00 49.18 O ANISOU 334 O PRO A 49 6314 6343 6028 -52 -421 -766 O ATOM 335 CB PRO A 49 -0.276 33.213 0.032 1.00 35.13 C ANISOU 335 CB PRO A 49 4555 4702 4091 70 -383 -790 C ATOM 336 CG PRO A 49 0.924 33.000 0.893 1.00 46.68 C ANISOU 336 CG PRO A 49 6022 6239 5474 43 -437 -830 C ATOM 337 CD PRO A 49 1.854 32.088 0.154 1.00 55.16 C ANISOU 337 CD PRO A 49 7028 7314 6618 -16 -478 -784 C ATOM 338 N LEU A 50 -1.242 31.850 -3.215 1.00 33.98 N ANISOU 338 N LEU A 50 4296 4448 4164 -10 -385 -639 N ATOM 339 CA LEU A 50 -1.490 32.346 -4.568 1.00 41.75 C ANISOU 339 CA LEU A 50 5295 5373 5194 -56 -402 -631 C ATOM 340 C LEU A 50 -2.850 33.047 -4.692 1.00 44.33 C ANISOU 340 C LEU A 50 5629 5659 5554 -1 -386 -591 C ATOM 341 O LEU A 50 -3.885 32.393 -4.766 1.00 49.74 O ANISOU 341 O LEU A 50 6259 6362 6278 32 -372 -529 O ATOM 342 CB LEU A 50 -1.430 31.219 -5.601 1.00 40.72 C ANISOU 342 CB LEU A 50 5114 5255 5102 -104 -416 -601 C ATOM 343 CG LEU A 50 -0.275 30.227 -5.645 1.00 50.34 C ANISOU 343 CG LEU A 50 6297 6504 6327 -142 -421 -630 C ATOM 344 CD1 LEU A 50 -0.188 29.620 -7.034 1.00 46.42 C ANISOU 344 CD1 LEU A 50 5781 5998 5860 -201 -428 -641 C ATOM 345 CD2 LEU A 50 1.006 30.906 -5.267 1.00 56.33 C ANISOU 345 CD2 LEU A 50 7082 7270 7050 -171 -433 -688 C ATOM 346 N VAL A 51 -2.842 34.374 -4.738 1.00 46.53 N ANISOU 346 N VAL A 51 5967 5875 5839 6 -390 -624 N ATOM 347 CA VAL A 51 -4.072 35.129 -4.929 1.00 45.56 C ANISOU 347 CA VAL A 51 5842 5696 5773 66 -377 -582 C ATOM 348 C VAL A 51 -4.443 35.283 -6.395 1.00 49.27 C ANISOU 348 C VAL A 51 6301 6131 6288 18 -426 -510 C ATOM 349 O VAL A 51 -3.608 35.597 -7.238 1.00 57.45 O ANISOU 349 O VAL A 51 7374 7148 7304 -61 -459 -516 O ATOM 350 CB VAL A 51 -4.001 36.520 -4.300 1.00 45.89 C ANISOU 350 CB VAL A 51 5951 5660 5826 109 -358 -650 C ATOM 351 CG1 VAL A 51 -5.280 37.262 -4.585 1.00 48.93 C ANISOU 351 CG1 VAL A 51 6318 5973 6299 182 -344 -598 C ATOM 352 CG2 VAL A 51 -3.791 36.410 -2.797 1.00 51.17 C ANISOU 352 CG2 VAL A 51 6638 6383 6420 162 -312 -731 C ATOM 353 N PHE A 52 -5.714 35.051 -6.689 1.00 52.27 N ANISOU 353 N PHE A 52 6622 6515 6723 63 -431 -436 N ATOM 354 CA PHE A 52 -6.241 35.242 -8.030 1.00 50.98 C ANISOU 354 CA PHE A 52 6445 6334 6592 24 -494 -356 C ATOM 355 C PHE A 52 -7.399 36.223 -7.928 1.00 55.05 C ANISOU 355 C PHE A 52 6937 6781 7199 112 -493 -297 C ATOM 356 O PHE A 52 -8.172 36.187 -6.962 1.00 63.65 O ANISOU 356 O PHE A 52 7980 7872 8332 203 -435 -304 O ATOM 357 CB PHE A 52 -6.744 33.918 -8.612 1.00 43.72 C ANISOU 357 CB PHE A 52 5454 5485 5672 -12 -526 -317 C ATOM 358 CG PHE A 52 -5.661 32.919 -8.911 1.00 40.95 C ANISOU 358 CG PHE A 52 5118 5184 5257 -92 -528 -376 C ATOM 359 CD1 PHE A 52 -5.114 32.137 -7.902 1.00 43.71 C ANISOU 359 CD1 PHE A 52 5451 5561 5595 -74 -480 -425 C ATOM 360 CD2 PHE A 52 -5.213 32.733 -10.211 1.00 40.14 C ANISOU 360 CD2 PHE A 52 5041 5107 5105 -180 -575 -377 C ATOM 361 CE1 PHE A 52 -4.127 31.214 -8.189 1.00 39.27 C ANISOU 361 CE1 PHE A 52 4889 5030 5003 -135 -481 -474 C ATOM 362 CE2 PHE A 52 -4.222 31.807 -10.496 1.00 35.02 C ANISOU 362 CE2 PHE A 52 4396 4498 4410 -241 -562 -445 C ATOM 363 CZ PHE A 52 -3.687 31.053 -9.486 1.00 35.50 C ANISOU 363 CZ PHE A 52 4431 4566 4490 -214 -516 -493 C ATOM 364 N HIS A 53 -7.539 37.091 -8.920 1.00 53.37 N ANISOU 364 N HIS A 53 6751 6511 7018 88 -552 -230 N ATOM 365 CA HIS A 53 -8.596 38.095 -8.870 1.00 45.25 C ANISOU 365 CA HIS A 53 5694 5397 6104 180 -557 -164 C ATOM 366 C HIS A 53 -9.786 37.694 -9.736 1.00 51.71 C ANISOU 366 C HIS A 53 6419 6256 6972 187 -629 -44 C ATOM 367 O HIS A 53 -9.737 37.724 -10.971 1.00 54.62 O ANISOU 367 O HIS A 53 6800 6647 7306 112 -718 34 O ATOM 368 CB HIS A 53 -8.054 39.492 -9.206 1.00 43.68 C ANISOU 368 CB HIS A 53 5577 5078 5943 169 -576 -153 C ATOM 369 CG HIS A 53 -7.074 40.005 -8.196 1.00 57.19 C ANISOU 369 CG HIS A 53 7363 6732 7634 172 -512 -283 C ATOM 370 ND1 HIS A 53 -7.466 40.585 -7.001 1.00 55.69 N ANISOU 370 ND1 HIS A 53 7179 6478 7504 279 -441 -366 N ATOM 371 CD2 HIS A 53 -5.716 39.991 -8.170 1.00 51.68 C ANISOU 371 CD2 HIS A 53 6732 6045 6859 80 -511 -354 C ATOM 372 CE1 HIS A 53 -6.398 40.911 -6.301 1.00 56.60 C ANISOU 372 CE1 HIS A 53 7369 6566 7569 245 -414 -486 C ATOM 373 NE2 HIS A 53 -5.318 40.559 -6.986 1.00 51.03 N ANISOU 373 NE2 HIS A 53 6695 5904 6791 124 -459 -474 N ATOM 374 N THR A 54 -10.857 37.289 -9.070 1.00 47.95 N ANISOU 374 N THR A 54 5844 5802 6571 271 -589 -28 N ATOM 375 CA THR A 54 -12.041 36.863 -9.780 1.00 50.99 C ANISOU 375 CA THR A 54 6119 6230 7025 276 -664 83 C ATOM 376 C THR A 54 -12.987 38.038 -9.946 1.00 55.88 C ANISOU 376 C THR A 54 6690 6760 7783 374 -687 176 C ATOM 377 O THR A 54 -12.888 39.038 -9.226 1.00 56.27 O ANISOU 377 O THR A 54 6777 6708 7893 461 -614 132 O ATOM 378 CB THR A 54 -12.759 35.739 -9.041 1.00 52.40 C ANISOU 378 CB THR A 54 6191 6481 7238 305 -611 73 C ATOM 379 OG1 THR A 54 -13.476 36.281 -7.921 1.00 54.20 O ANISOU 379 OG1 THR A 54 6364 6670 7561 436 -506 66 O ATOM 380 CG2 THR A 54 -11.748 34.676 -8.567 1.00 50.01 C ANISOU 380 CG2 THR A 54 5939 6238 6825 236 -565 -22 C ATOM 381 N ASN A 55 -13.899 37.909 -10.907 1.00 51.41 N ANISOU 381 N ASN A 55 6036 6225 7272 359 -797 301 N ATOM 382 CA ASN A 55 -14.907 38.923 -11.173 1.00 56.68 C ANISOU 382 CA ASN A 55 6628 6813 8093 456 -840 420 C ATOM 383 C ASN A 55 -15.829 39.102 -9.962 1.00 66.45 C ANISOU 383 C ASN A 55 7760 8012 9476 603 -720 393 C ATOM 384 O ASN A 55 -16.699 39.981 -9.939 1.00 72.01 O ANISOU 384 O ASN A 55 8386 8634 10341 716 -722 471 O ATOM 385 CB ASN A 55 -15.691 38.559 -12.436 1.00 50.12 C ANISOU 385 CB ASN A 55 5713 6057 7275 397 -1000 561 C ATOM 386 CG ASN A 55 -16.498 37.282 -12.277 1.00 64.72 C ANISOU 386 CG ASN A 55 7431 8012 9148 374 -1013 559 C ATOM 387 OD1 ASN A 55 -17.297 36.934 -13.144 1.00 80.52 O ANISOU 387 OD1 ASN A 55 9337 10075 11181 333 -1145 660 O ATOM 388 ND2 ASN A 55 -16.304 36.584 -11.164 1.00 55.96 N ANISOU 388 ND2 ASN A 55 6311 6923 8029 395 -884 452 N ATOM 389 N ARG A 56 -15.601 38.265 -8.951 1.00 63.15 N ANISOU 389 N ARG A 56 7339 7658 8997 604 -610 288 N ATOM 390 CA ARG A 56 -16.366 38.268 -7.713 1.00 63.97 C ANISOU 390 CA ARG A 56 7351 7762 9192 729 -471 251 C ATOM 391 C ARG A 56 -15.516 38.802 -6.564 1.00 65.23 C ANISOU 391 C ARG A 56 7632 7873 9280 780 -339 101 C ATOM 392 O ARG A 56 -16.030 39.075 -5.479 1.00 62.87 O ANISOU 392 O ARG A 56 7290 7564 9032 896 -207 46 O ATOM 393 CB ARG A 56 -16.772 36.838 -7.373 1.00 74.25 C ANISOU 393 CB ARG A 56 8556 9188 10467 682 -443 262 C ATOM 394 CG ARG A 56 -18.197 36.657 -6.901 1.00 76.41 C ANISOU 394 CG ARG A 56 8642 9492 10898 780 -382 340 C ATOM 395 CD ARG A 56 -18.978 35.843 -7.908 1.00 79.72 C ANISOU 395 CD ARG A 56 8931 9975 11386 697 -522 462 C ATOM 396 NE ARG A 56 -19.823 34.791 -7.320 1.00 83.55 N ANISOU 396 NE ARG A 56 9259 10541 11944 697 -458 503 N ATOM 397 CZ ARG A 56 -19.980 34.535 -6.018 1.00 76.13 C ANISOU 397 CZ ARG A 56 8286 9636 11006 769 -282 461 C ATOM 398 NH1 ARG A 56 -19.348 35.246 -5.083 1.00 74.39 N ANISOU 398 NH1 ARG A 56 8182 9381 10702 852 -151 354 N ATOM 399 NH2 ARG A 56 -20.784 33.544 -5.648 1.00 57.25 N ANISOU 399 NH2 ARG A 56 5741 7319 8694 749 -238 530 N ATOM 400 N GLY A 57 -14.211 38.934 -6.807 1.00 62.34 N ANISOU 400 N GLY A 57 7414 7486 8788 687 -376 30 N ATOM 401 CA GLY A 57 -13.265 39.340 -5.783 1.00 52.92 C ANISOU 401 CA GLY A 57 6337 6260 7510 706 -281 -119 C ATOM 402 C GLY A 57 -11.996 38.492 -5.764 1.00 62.15 C ANISOU 402 C GLY A 57 7594 7507 8513 582 -303 -185 C ATOM 403 O GLY A 57 -11.796 37.630 -6.628 1.00 58.50 O ANISOU 403 O GLY A 57 7114 7111 8004 481 -385 -125 O ATOM 404 N PRO A 58 -11.128 38.741 -4.768 1.00 57.10 N ANISOU 404 N PRO A 58 7048 6861 7787 590 -231 -316 N ATOM 405 CA PRO A 58 -9.853 38.067 -4.486 1.00 49.58 C ANISOU 405 CA PRO A 58 6172 5977 6690 495 -239 -391 C ATOM 406 C PRO A 58 -10.048 36.678 -3.890 1.00 53.57 C ANISOU 406 C PRO A 58 6611 6611 7130 486 -197 -373 C ATOM 407 O PRO A 58 -10.839 36.525 -2.954 1.00 66.27 O ANISOU 407 O PRO A 58 8163 8264 8754 575 -103 -374 O ATOM 408 CB PRO A 58 -9.221 38.950 -3.401 1.00 50.06 C ANISOU 408 CB PRO A 58 6328 5986 6708 540 -174 -533 C ATOM 409 CG PRO A 58 -10.118 40.143 -3.249 1.00 52.80 C ANISOU 409 CG PRO A 58 6661 6215 7186 656 -131 -543 C ATOM 410 CD PRO A 58 -11.446 39.760 -3.756 1.00 56.72 C ANISOU 410 CD PRO A 58 7026 6737 7788 711 -133 -409 C ATOM 411 N ILE A 59 -9.340 35.680 -4.401 1.00 44.29 N ANISOU 411 N ILE A 59 5441 5494 5892 384 -254 -355 N ATOM 412 CA ILE A 59 -9.369 34.369 -3.759 1.00 52.26 C ANISOU 412 CA ILE A 59 6399 6603 6855 372 -215 -338 C ATOM 413 C ILE A 59 -7.960 33.859 -3.552 1.00 51.23 C ANISOU 413 C ILE A 59 6339 6507 6621 298 -237 -402 C ATOM 414 O ILE A 59 -7.112 33.983 -4.436 1.00 49.18 O ANISOU 414 O ILE A 59 6126 6216 6344 218 -304 -424 O ATOM 415 CB ILE A 59 -10.155 33.329 -4.569 1.00 53.29 C ANISOU 415 CB ILE A 59 6425 6765 7059 330 -263 -235 C ATOM 416 CG1 ILE A 59 -9.418 32.989 -5.854 1.00 50.39 C ANISOU 416 CG1 ILE A 59 6094 6384 6667 219 -365 -239 C ATOM 417 CG2 ILE A 59 -11.571 33.839 -4.901 1.00 50.69 C ANISOU 417 CG2 ILE A 59 6003 6405 6851 397 -263 -155 C ATOM 418 CD1 ILE A 59 -10.182 32.006 -6.691 1.00 62.01 C ANISOU 418 CD1 ILE A 59 7476 7883 8204 168 -425 -166 C ATOM 419 N LYS A 60 -7.704 33.295 -2.379 1.00 48.54 N ANISOU 419 N LYS A 60 5996 6238 6207 325 -177 -424 N ATOM 420 CA LYS A 60 -6.372 32.800 -2.071 1.00 45.43 C ANISOU 420 CA LYS A 60 5653 5882 5726 266 -205 -473 C ATOM 421 C LYS A 60 -6.329 31.272 -2.050 1.00 50.19 C ANISOU 421 C LYS A 60 6186 6541 6343 231 -211 -400 C ATOM 422 O LYS A 60 -7.003 30.645 -1.231 1.00 61.00 O ANISOU 422 O LYS A 60 7500 7967 7712 277 -152 -336 O ATOM 423 CB LYS A 60 -5.923 33.353 -0.725 1.00 44.37 C ANISOU 423 CB LYS A 60 5583 5790 5487 316 -156 -554 C ATOM 424 CG LYS A 60 -4.433 33.306 -0.506 1.00 51.68 C ANISOU 424 CG LYS A 60 6568 6735 6334 252 -210 -623 C ATOM 425 CD LYS A 60 -4.101 33.392 0.972 1.00 55.60 C ANISOU 425 CD LYS A 60 7105 7319 6703 296 -174 -678 C ATOM 426 CE LYS A 60 -3.913 34.829 1.428 1.00 70.73 C ANISOU 426 CE LYS A 60 9112 9187 8577 323 -165 -811 C ATOM 427 NZ LYS A 60 -3.415 34.865 2.844 1.00 80.03 N ANISOU 427 NZ LYS A 60 10341 10469 9598 348 -150 -884 N ATOM 428 N PHE A 61 -5.565 30.672 -2.960 1.00 41.74 N ANISOU 428 N PHE A 61 5115 5449 5294 150 -275 -407 N ATOM 429 CA PHE A 61 -5.222 29.240 -2.843 1.00 41.14 C ANISOU 429 CA PHE A 61 4986 5403 5241 118 -283 -362 C ATOM 430 C PHE A 61 -3.936 29.125 -2.057 1.00 38.90 C ANISOU 430 C PHE A 61 4743 5160 4878 112 -290 -405 C ATOM 431 O PHE A 61 -2.910 29.625 -2.502 1.00 38.04 O ANISOU 431 O PHE A 61 4682 5029 4742 68 -329 -478 O ATOM 432 CB PHE A 61 -5.033 28.576 -4.208 1.00 32.60 C ANISOU 432 CB PHE A 61 3880 4278 4228 41 -341 -369 C ATOM 433 CG PHE A 61 -6.312 28.363 -4.964 1.00 46.80 C ANISOU 433 CG PHE A 61 5620 6054 6109 32 -359 -315 C ATOM 434 CD1 PHE A 61 -7.173 27.306 -4.631 1.00 50.55 C ANISOU 434 CD1 PHE A 61 6006 6535 6667 41 -340 -235 C ATOM 435 CD2 PHE A 61 -6.665 29.211 -6.009 1.00 51.07 C ANISOU 435 CD2 PHE A 61 6186 6566 6651 10 -403 -330 C ATOM 436 CE1 PHE A 61 -8.360 27.100 -5.330 1.00 47.36 C ANISOU 436 CE1 PHE A 61 5531 6111 6352 23 -370 -186 C ATOM 437 CE2 PHE A 61 -7.855 29.019 -6.709 1.00 56.69 C ANISOU 437 CE2 PHE A 61 6834 7268 7439 -1 -440 -272 C ATOM 438 CZ PHE A 61 -8.703 27.954 -6.370 1.00 56.20 C ANISOU 438 CZ PHE A 61 6675 7215 7464 3 -426 -208 C ATOM 439 N ASN A 62 -3.999 28.499 -0.883 1.00 35.49 N ANISOU 439 N ASN A 62 4285 4791 4407 154 -254 -348 N ATOM 440 CA ASN A 62 -2.803 28.228 -0.079 1.00 41.76 C ANISOU 440 CA ASN A 62 5102 5638 5126 149 -278 -364 C ATOM 441 C ASN A 62 -2.136 26.903 -0.440 1.00 53.09 C ANISOU 441 C ASN A 62 6477 7051 6645 110 -315 -316 C ATOM 442 O ASN A 62 -2.385 25.877 0.191 1.00 63.46 O ANISOU 442 O ASN A 62 7737 8389 7988 132 -297 -213 O ATOM 443 CB ASN A 62 -3.138 28.245 1.404 1.00 39.28 C ANISOU 443 CB ASN A 62 4799 5423 4703 213 -228 -318 C ATOM 444 CG ASN A 62 -3.402 29.637 1.909 1.00 48.02 C ANISOU 444 CG ASN A 62 5983 6551 5712 255 -195 -412 C ATOM 445 OD1 ASN A 62 -4.137 29.830 2.873 1.00 55.15 O ANISOU 445 OD1 ASN A 62 6894 7526 6537 319 -123 -390 O ATOM 446 ND2 ASN A 62 -2.807 30.625 1.252 1.00 47.08 N ANISOU 446 ND2 ASN A 62 5920 6366 5602 218 -240 -520 N ATOM 447 N VAL A 63 -1.289 26.925 -1.456 1.00 36.32 N ANISOU 447 N VAL A 63 4359 4875 4567 54 -358 -386 N ATOM 448 CA VAL A 63 -0.746 25.692 -1.994 1.00 42.35 C ANISOU 448 CA VAL A 63 5061 5595 5434 24 -379 -366 C ATOM 449 C VAL A 63 0.351 25.064 -1.131 1.00 44.57 C ANISOU 449 C VAL A 63 5312 5913 5708 42 -406 -330 C ATOM 450 O VAL A 63 1.388 25.678 -0.912 1.00 55.58 O ANISOU 450 O VAL A 63 6732 7343 7041 29 -439 -389 O ATOM 451 CB VAL A 63 -0.219 25.924 -3.401 1.00 44.73 C ANISOU 451 CB VAL A 63 5377 5844 5773 -37 -399 -460 C ATOM 452 CG1 VAL A 63 0.339 24.624 -3.994 1.00 40.61 C ANISOU 452 CG1 VAL A 63 4793 5271 5364 -60 -406 -468 C ATOM 453 CG2 VAL A 63 -1.336 26.517 -4.260 1.00 43.34 C ANISOU 453 CG2 VAL A 63 5228 5642 5597 -55 -391 -472 C ATOM 454 N TRP A 64 0.115 23.848 -0.633 1.00 41.28 N ANISOU 454 N TRP A 64 4832 5486 5366 67 -400 -221 N ATOM 455 CA TRP A 64 1.141 23.141 0.141 1.00 55.26 C ANISOU 455 CA TRP A 64 6561 7284 7153 90 -437 -159 C ATOM 456 C TRP A 64 2.088 22.368 -0.764 1.00 49.48 C ANISOU 456 C TRP A 64 5771 6466 6562 65 -460 -208 C ATOM 457 O TRP A 64 1.684 21.400 -1.410 1.00 44.32 O ANISOU 457 O TRP A 64 5072 5719 6047 55 -442 -194 O ATOM 458 CB TRP A 64 0.523 22.182 1.153 1.00 55.78 C ANISOU 458 CB TRP A 64 6581 7372 7242 132 -419 6 C ATOM 459 CG TRP A 64 -0.175 22.852 2.279 1.00 49.84 C ANISOU 459 CG TRP A 64 5877 6736 6326 168 -385 60 C ATOM 460 CD1 TRP A 64 -0.995 23.929 2.203 1.00 46.09 C ANISOU 460 CD1 TRP A 64 5461 6292 5760 173 -340 -9 C ATOM 461 CD2 TRP A 64 -0.142 22.463 3.658 1.00 48.79 C ANISOU 461 CD2 TRP A 64 5735 6706 6097 211 -386 198 C ATOM 462 NE1 TRP A 64 -1.471 24.247 3.452 1.00 50.74 N ANISOU 462 NE1 TRP A 64 6080 6996 6204 220 -300 56 N ATOM 463 CE2 TRP A 64 -0.958 23.367 4.360 1.00 53.58 C ANISOU 463 CE2 TRP A 64 6403 7413 6541 239 -328 184 C ATOM 464 CE3 TRP A 64 0.507 21.450 4.360 1.00 53.59 C ANISOU 464 CE3 TRP A 64 6288 7333 6741 231 -430 336 C ATOM 465 CZ2 TRP A 64 -1.148 23.279 5.741 1.00 55.05 C ANISOU 465 CZ2 TRP A 64 6607 7738 6573 281 -304 294 C ATOM 466 CZ3 TRP A 64 0.317 21.367 5.730 1.00 61.15 C ANISOU 466 CZ3 TRP A 64 7260 8427 7546 269 -421 468 C ATOM 467 CH2 TRP A 64 -0.505 22.279 6.405 1.00 58.46 C ANISOU 467 CH2 TRP A 64 6991 8204 7017 291 -354 440 C ATOM 468 N ASP A 65 3.342 22.809 -0.818 1.00 47.42 N ANISOU 468 N ASP A 65 5509 6236 6274 52 -497 -277 N ATOM 469 CA ASP A 65 4.345 22.126 -1.632 1.00 53.84 C ANISOU 469 CA ASP A 65 6255 6980 7222 39 -503 -332 C ATOM 470 C ASP A 65 5.336 21.376 -0.747 1.00 58.45 C ANISOU 470 C ASP A 65 6760 7582 7868 84 -554 -241 C ATOM 471 O ASP A 65 5.747 21.857 0.316 1.00 55.43 O ANISOU 471 O ASP A 65 6389 7299 7374 100 -606 -190 O ATOM 472 CB ASP A 65 5.077 23.101 -2.556 1.00 52.53 C ANISOU 472 CB ASP A 65 6119 6827 7014 -14 -495 -468 C ATOM 473 CG ASP A 65 6.049 22.399 -3.489 1.00 52.77 C ANISOU 473 CG ASP A 65 6076 6797 7177 -26 -473 -538 C ATOM 474 OD1 ASP A 65 5.626 21.503 -4.248 1.00 52.64 O ANISOU 474 OD1 ASP A 65 6038 6696 7266 -25 -436 -563 O ATOM 475 OD2 ASP A 65 7.241 22.748 -3.471 1.00 56.61 O ANISOU 475 OD2 ASP A 65 6522 7320 7668 -37 -491 -577 O ATOM 476 N THR A 66 5.712 20.187 -1.194 1.00 64.35 N ANISOU 476 N THR A 66 7425 8230 8796 105 -544 -225 N ATOM 477 CA THR A 66 6.516 19.275 -0.387 1.00 60.56 C ANISOU 477 CA THR A 66 6852 7739 8418 161 -594 -108 C ATOM 478 C THR A 66 7.965 19.706 -0.397 1.00 55.72 C ANISOU 478 C THR A 66 6185 7178 7807 160 -638 -166 C ATOM 479 O THR A 66 8.405 20.363 -1.332 1.00 58.98 O ANISOU 479 O THR A 66 6612 7591 8206 114 -603 -308 O ATOM 480 CB THR A 66 6.465 17.876 -0.981 1.00 55.02 C ANISOU 480 CB THR A 66 6074 6881 7948 188 -563 -92 C ATOM 481 OG1 THR A 66 7.277 17.860 -2.159 1.00 61.78 O ANISOU 481 OG1 THR A 66 6897 7682 8895 171 -524 -252 O ATOM 482 CG2 THR A 66 5.023 17.500 -1.355 1.00 47.40 C ANISOU 482 CG2 THR A 66 5155 5843 7011 163 -516 -80 C ATOM 483 N ALA A 67 8.701 19.343 0.646 1.00 53.82 N ANISOU 483 N ALA A 67 5876 6990 7583 205 -717 -45 N ATOM 484 CA ALA A 67 10.157 19.504 0.632 1.00 62.36 C ANISOU 484 CA ALA A 67 6865 8106 8722 210 -769 -81 C ATOM 485 C ALA A 67 10.839 18.217 0.136 1.00 66.93 C ANISOU 485 C ALA A 67 7313 8556 9561 269 -748 -60 C ATOM 486 O ALA A 67 11.917 17.839 0.603 1.00 62.73 O ANISOU 486 O ALA A 67 6666 8041 9128 314 -815 9 O ATOM 487 CB ALA A 67 10.685 19.916 2.022 1.00 57.22 C ANISOU 487 CB ALA A 67 6203 7599 7938 223 -888 28 C ATOM 488 N GLY A 68 10.178 17.544 -0.801 1.00 66.28 N ANISOU 488 N GLY A 68 7246 8341 9597 270 -659 -124 N ATOM 489 CA GLY A 68 10.715 16.366 -1.450 1.00 66.79 C ANISOU 489 CA GLY A 68 7203 8258 9916 323 -617 -154 C ATOM 490 C GLY A 68 10.409 14.998 -0.854 1.00 66.51 C ANISOU 490 C GLY A 68 7105 8099 10068 394 -645 10 C ATOM 491 O GLY A 68 10.839 13.997 -1.420 1.00 66.64 O ANISOU 491 O GLY A 68 7032 7965 10321 444 -605 -29 O ATOM 492 N GLN A 69 9.681 14.932 0.258 1.00 55.46 N ANISOU 492 N GLN A 69 5747 6753 8570 401 -703 190 N ATOM 493 CA GLN A 69 9.524 13.663 0.978 1.00 58.18 C ANISOU 493 CA GLN A 69 6021 6993 9093 467 -741 392 C ATOM 494 C GLN A 69 8.831 12.550 0.187 1.00 68.11 C ANISOU 494 C GLN A 69 7265 8035 10581 472 -667 353 C ATOM 495 O GLN A 69 8.764 11.407 0.637 1.00 74.31 O ANISOU 495 O GLN A 69 7977 8689 11567 526 -690 510 O ATOM 496 CB GLN A 69 8.801 13.861 2.311 1.00 59.91 C ANISOU 496 CB GLN A 69 6296 7335 9131 462 -800 600 C ATOM 497 CG GLN A 69 9.601 14.618 3.343 1.00 69.47 C ANISOU 497 CG GLN A 69 7499 8741 10153 472 -903 678 C ATOM 498 CD GLN A 69 9.539 16.106 3.104 1.00 68.62 C ANISOU 498 CD GLN A 69 7494 8778 9802 402 -889 507 C ATOM 499 OE1 GLN A 69 8.629 16.586 2.436 1.00 66.23 O ANISOU 499 OE1 GLN A 69 7283 8453 9429 352 -807 388 O ATOM 500 NE2 GLN A 69 10.504 16.846 3.642 1.00 62.90 N ANISOU 500 NE2 GLN A 69 6748 8192 8959 396 -976 496 N ATOM 501 N GLU A 70 8.318 12.881 -0.990 1.00 71.21 N ANISOU 501 N GLU A 70 7725 8387 10944 413 -585 146 N ATOM 502 CA GLU A 70 7.536 11.929 -1.773 1.00 68.99 C ANISOU 502 CA GLU A 70 7448 7917 10849 398 -527 80 C ATOM 503 C GLU A 70 8.378 10.873 -2.501 1.00 78.28 C ANISOU 503 C GLU A 70 8523 8906 12314 457 -490 -20 C ATOM 504 O GLU A 70 7.889 9.789 -2.810 1.00 91.97 O ANISOU 504 O GLU A 70 10233 10446 14268 466 -467 -23 O ATOM 505 CB GLU A 70 6.607 12.661 -2.757 1.00 65.84 C ANISOU 505 CB GLU A 70 7161 7557 10297 308 -470 -97 C ATOM 506 CG GLU A 70 7.310 13.403 -3.898 1.00 66.00 C ANISOU 506 CG GLU A 70 7207 7635 10236 279 -417 -328 C ATOM 507 CD GLU A 70 7.679 14.852 -3.553 1.00 63.01 C ANISOU 507 CD GLU A 70 6880 7459 9603 250 -442 -330 C ATOM 508 OE1 GLU A 70 7.888 15.165 -2.358 1.00 58.11 O ANISOU 508 OE1 GLU A 70 6245 6933 8900 277 -510 -171 O ATOM 509 OE2 GLU A 70 7.762 15.682 -4.490 1.00 54.95 O ANISOU 509 OE2 GLU A 70 5917 6500 8462 195 -397 -491 O ATOM 510 N LYS A 71 9.638 11.181 -2.777 1.00 77.80 N ANISOU 510 N LYS A 71 8396 8894 12269 497 -480 -109 N ATOM 511 CA LYS A 71 10.506 10.214 -3.451 1.00 82.60 C ANISOU 511 CA LYS A 71 8894 9331 13158 569 -429 -216 C ATOM 512 C LYS A 71 10.739 8.982 -2.587 1.00 82.28 C ANISOU 512 C LYS A 71 8742 9132 13390 661 -488 -4 C ATOM 513 O LYS A 71 11.105 7.931 -3.095 1.00 81.85 O ANISOU 513 O LYS A 71 8605 8870 13622 724 -443 -74 O ATOM 514 CB LYS A 71 11.852 10.838 -3.838 1.00 83.49 C ANISOU 514 CB LYS A 71 8936 9548 13239 596 -400 -331 C ATOM 515 CG LYS A 71 11.731 12.251 -4.384 1.00 90.41 C ANISOU 515 CG LYS A 71 9917 10614 13821 501 -367 -466 C ATOM 516 CD LYS A 71 12.815 12.579 -5.389 1.00 87.78 C ANISOU 516 CD LYS A 71 9525 10315 13512 506 -276 -661 C ATOM 517 CE LYS A 71 12.658 14.016 -5.876 1.00 83.02 C ANISOU 517 CE LYS A 71 9028 9894 12622 404 -251 -759 C ATOM 518 NZ LYS A 71 12.742 14.961 -4.729 1.00 81.36 N ANISOU 518 NZ LYS A 71 8836 9836 12240 380 -359 -600 N ATOM 519 N PHE A 72 10.518 9.112 -1.282 1.00 82.53 N ANISOU 519 N PHE A 72 8772 9256 13327 671 -586 256 N ATOM 520 CA PHE A 72 10.803 8.026 -0.350 1.00 81.78 C ANISOU 520 CA PHE A 72 8569 9039 13466 759 -657 504 C ATOM 521 C PHE A 72 9.559 7.562 0.405 1.00 81.21 C ANISOU 521 C PHE A 72 8554 8923 13380 723 -688 715 C ATOM 522 O PHE A 72 9.649 7.154 1.564 1.00 75.53 O ANISOU 522 O PHE A 72 7783 8223 12691 768 -771 993 O ATOM 523 CB PHE A 72 11.879 8.441 0.659 1.00 75.47 C ANISOU 523 CB PHE A 72 7685 8403 12588 816 -763 672 C ATOM 524 CG PHE A 72 12.805 9.505 0.160 1.00 68.98 C ANISOU 524 CG PHE A 72 6851 7739 11620 798 -746 487 C ATOM 525 CD1 PHE A 72 14.003 9.173 -0.451 1.00 68.78 C ANISOU 525 CD1 PHE A 72 6691 7636 11807 869 -710 374 C ATOM 526 CD2 PHE A 72 12.484 10.849 0.317 1.00 73.74 C ANISOU 526 CD2 PHE A 72 7570 8563 11887 709 -760 433 C ATOM 527 CE1 PHE A 72 14.873 10.164 -0.911 1.00 76.75 C ANISOU 527 CE1 PHE A 72 7674 8796 12690 842 -686 219 C ATOM 528 CE2 PHE A 72 13.341 11.853 -0.134 1.00 72.71 C ANISOU 528 CE2 PHE A 72 7424 8566 11637 680 -746 277 C ATOM 529 CZ PHE A 72 14.542 11.508 -0.751 1.00 75.88 C ANISOU 529 CZ PHE A 72 7684 8899 12248 742 -709 176 C ATOM 530 N GLY A 73 8.400 7.634 -0.243 1.00 89.96 N ANISOU 530 N GLY A 73 9761 9984 14437 638 -623 596 N ATOM 531 CA GLY A 73 7.173 7.111 0.341 1.00 89.63 C ANISOU 531 CA GLY A 73 9753 9877 14425 596 -634 782 C ATOM 532 C GLY A 73 5.995 8.069 0.374 1.00 94.30 C ANISOU 532 C GLY A 73 10468 10635 14727 498 -609 753 C ATOM 533 O GLY A 73 6.056 9.179 -0.162 1.00 89.74 O ANISOU 533 O GLY A 73 9965 10207 13924 456 -583 570 O ATOM 534 N GLY A 74 4.915 7.629 1.016 1.00 96.37 N ANISOU 534 N GLY A 74 10742 10863 15011 463 -612 948 N ATOM 535 CA GLY A 74 3.699 8.417 1.114 1.00 84.46 C ANISOU 535 CA GLY A 74 9328 9494 13269 380 -580 944 C ATOM 536 C GLY A 74 3.733 9.468 2.208 1.00 77.57 C ANISOU 536 C GLY A 74 8507 8891 12075 389 -610 1075 C ATOM 537 O GLY A 74 4.480 9.349 3.180 1.00 78.24 O ANISOU 537 O GLY A 74 8549 9051 12126 451 -672 1253 O ATOM 538 N LEU A 75 2.895 10.490 2.051 1.00 74.18 N ANISOU 538 N LEU A 75 8169 8604 11411 329 -571 984 N ATOM 539 CA LEU A 75 2.845 11.638 2.960 1.00 69.41 C ANISOU 539 CA LEU A 75 7632 8251 10487 332 -585 1047 C ATOM 540 C LEU A 75 1.973 11.419 4.197 1.00 76.95 C ANISOU 540 C LEU A 75 8590 9295 11353 332 -572 1311 C ATOM 541 O LEU A 75 1.055 10.591 4.196 1.00 89.42 O ANISOU 541 O LEU A 75 10131 10753 13094 302 -533 1426 O ATOM 542 CB LEU A 75 2.349 12.859 2.198 1.00 63.41 C ANISOU 542 CB LEU A 75 6966 7587 9541 277 -541 826 C ATOM 543 CG LEU A 75 3.165 13.134 0.935 1.00 63.53 C ANISOU 543 CG LEU A 75 6986 7537 9616 268 -540 575 C ATOM 544 CD1 LEU A 75 2.374 13.956 -0.088 1.00 65.80 C ANISOU 544 CD1 LEU A 75 7351 7848 9801 200 -492 383 C ATOM 545 CD2 LEU A 75 4.477 13.806 1.312 1.00 51.00 C ANISOU 545 CD2 LEU A 75 5395 6074 7909 308 -592 546 C ATOM 546 N ARG A 76 2.261 12.186 5.244 1.00 69.67 N ANISOU 546 N ARG A 76 7713 8593 10166 358 -601 1399 N ATOM 547 CA ARG A 76 1.587 12.046 6.531 1.00 74.74 C ANISOU 547 CA ARG A 76 8363 9364 10671 365 -583 1653 C ATOM 548 C ARG A 76 0.267 12.807 6.573 1.00 77.80 C ANISOU 548 C ARG A 76 8818 9856 10888 320 -489 1608 C ATOM 549 O ARG A 76 0.121 13.850 5.945 1.00 70.97 O ANISOU 549 O ARG A 76 8019 9044 9902 297 -466 1388 O ATOM 550 CB ARG A 76 2.501 12.548 7.647 1.00 76.12 C ANISOU 550 CB ARG A 76 8563 9747 10613 412 -663 1748 C ATOM 551 CG ARG A 76 3.907 11.983 7.573 1.00 76.15 C ANISOU 551 CG ARG A 76 8488 9671 10775 464 -769 1773 C ATOM 552 CD ARG A 76 4.952 13.064 7.795 1.00 80.26 C ANISOU 552 CD ARG A 76 9049 10367 11078 477 -847 1641 C ATOM 553 NE ARG A 76 5.065 13.470 9.193 1.00 83.28 N ANISOU 553 NE ARG A 76 9475 10988 11180 493 -905 1805 N ATOM 554 CZ ARG A 76 5.922 14.386 9.631 1.00 83.79 C ANISOU 554 CZ ARG A 76 9577 11228 11031 496 -992 1719 C ATOM 555 NH1 ARG A 76 6.740 14.995 8.778 1.00 73.25 N ANISOU 555 NH1 ARG A 76 8232 9850 9750 483 -1022 1488 N ATOM 556 NH2 ARG A 76 5.963 14.694 10.922 1.00 89.71 N ANISOU 556 NH2 ARG A 76 10373 12201 11511 506 -1049 1863 N ATOM 557 N ASP A 77 -0.691 12.283 7.327 1.00 86.32 N ANISOU 557 N ASP A 77 9869 10961 11968 309 -431 1831 N ATOM 558 CA ASP A 77 -2.005 12.905 7.435 1.00 77.48 C ANISOU 558 CA ASP A 77 8786 9938 10715 274 -328 1815 C ATOM 559 C ASP A 77 -1.908 14.402 7.716 1.00 69.47 C ANISOU 559 C ASP A 77 7877 9137 9381 293 -314 1654 C ATOM 560 O ASP A 77 -2.666 15.191 7.165 1.00 77.70 O ANISOU 560 O ASP A 77 8956 10197 10368 269 -253 1499 O ATOM 561 CB ASP A 77 -2.840 12.214 8.516 1.00 87.87 C ANISOU 561 CB ASP A 77 10054 11311 12020 270 -262 2117 C ATOM 562 CG ASP A 77 -3.040 10.730 8.243 1.00 98.31 C ANISOU 562 CG ASP A 77 11269 12395 13691 241 -272 2288 C ATOM 563 OD1 ASP A 77 -2.715 10.272 7.123 1.00 98.21 O ANISOU 563 OD1 ASP A 77 11223 12166 13928 221 -317 2135 O ATOM 564 OD2 ASP A 77 -3.523 10.022 9.154 1.00102.46 O ANISOU 564 OD2 ASP A 77 11743 12946 14240 236 -232 2574 O ATOM 565 N GLY A 78 -0.980 14.794 8.578 1.00 65.71 N ANISOU 565 N GLY A 78 7445 8817 8705 334 -378 1691 N ATOM 566 CA GLY A 78 -0.756 16.201 8.848 1.00 61.30 C ANISOU 566 CA GLY A 78 6989 8438 7863 347 -380 1518 C ATOM 567 C GLY A 78 -0.661 17.044 7.587 1.00 65.71 C ANISOU 567 C GLY A 78 7585 8910 8471 319 -382 1237 C ATOM 568 O GLY A 78 -0.901 18.251 7.619 1.00 77.78 O ANISOU 568 O GLY A 78 9194 10545 9813 319 -351 1087 O ATOM 569 N TYR A 79 -0.322 16.419 6.467 1.00 61.18 N ANISOU 569 N TYR A 79 6955 8142 8149 296 -414 1164 N ATOM 570 CA TYR A 79 -0.194 17.151 5.211 1.00 63.59 C ANISOU 570 CA TYR A 79 7294 8373 8492 265 -415 915 C ATOM 571 C TYR A 79 -1.541 17.320 4.524 1.00 64.35 C ANISOU 571 C TYR A 79 7393 8412 8647 228 -334 861 C ATOM 572 O TYR A 79 -1.866 18.402 4.038 1.00 56.91 O ANISOU 572 O TYR A 79 6510 7511 7601 215 -311 704 O ATOM 573 CB TYR A 79 0.795 16.460 4.267 1.00 66.97 C ANISOU 573 CB TYR A 79 7667 8640 9138 257 -475 837 C ATOM 574 CG TYR A 79 0.815 17.041 2.864 1.00 65.93 C ANISOU 574 CG TYR A 79 7567 8430 9055 216 -462 602 C ATOM 575 CD1 TYR A 79 1.745 18.017 2.502 1.00 50.20 C ANISOU 575 CD1 TYR A 79 5621 6497 6956 211 -497 440 C ATOM 576 CD2 TYR A 79 -0.102 16.615 1.900 1.00 63.73 C ANISOU 576 CD2 TYR A 79 7267 8023 8925 174 -419 550 C ATOM 577 CE1 TYR A 79 1.765 18.548 1.221 1.00 47.81 C ANISOU 577 CE1 TYR A 79 5347 6134 6683 169 -480 250 C ATOM 578 CE2 TYR A 79 -0.089 17.139 0.616 1.00 62.05 C ANISOU 578 CE2 TYR A 79 7087 7759 8728 132 -415 348 C ATOM 579 CZ TYR A 79 0.843 18.104 0.284 1.00 65.24 C ANISOU 579 CZ TYR A 79 7543 8231 9015 132 -440 207 C ATOM 580 OH TYR A 79 0.848 18.622 -0.990 1.00 76.07 O ANISOU 580 OH TYR A 79 8950 9563 10391 88 -429 30 O ATOM 581 N TYR A 80 -2.321 16.243 4.493 1.00 68.73 N ANISOU 581 N TYR A 80 7872 8862 9381 209 -300 1002 N ATOM 582 CA TYR A 80 -3.610 16.228 3.802 1.00 66.45 C ANISOU 582 CA TYR A 80 7557 8504 9189 164 -240 968 C ATOM 583 C TYR A 80 -4.721 16.857 4.622 1.00 68.43 C ANISOU 583 C TYR A 80 7820 8901 9278 181 -151 1053 C ATOM 584 O TYR A 80 -5.777 17.195 4.094 1.00 70.56 O ANISOU 584 O TYR A 80 8071 9152 9585 154 -103 1002 O ATOM 585 CB TYR A 80 -4.009 14.794 3.456 1.00 64.64 C ANISOU 585 CB TYR A 80 7229 8091 9239 126 -244 1081 C ATOM 586 CG TYR A 80 -3.091 14.095 2.474 1.00 64.67 C ANISOU 586 CG TYR A 80 7212 7920 9439 111 -313 964 C ATOM 587 CD1 TYR A 80 -3.192 14.339 1.112 1.00 58.36 C ANISOU 587 CD1 TYR A 80 6433 7033 8709 65 -329 748 C ATOM 588 CD2 TYR A 80 -2.140 13.174 2.907 1.00 69.24 C ANISOU 588 CD2 TYR A 80 7746 8424 10137 146 -357 1074 C ATOM 589 CE1 TYR A 80 -2.372 13.698 0.208 1.00 52.07 C ANISOU 589 CE1 TYR A 80 5619 6089 8077 55 -372 624 C ATOM 590 CE2 TYR A 80 -1.312 12.523 2.007 1.00 64.47 C ANISOU 590 CE2 TYR A 80 7114 7653 9730 144 -403 954 C ATOM 591 CZ TYR A 80 -1.437 12.788 0.657 1.00 58.16 C ANISOU 591 CZ TYR A 80 6341 6777 8980 98 -403 720 C ATOM 592 OH TYR A 80 -0.615 12.154 -0.249 1.00 57.90 O ANISOU 592 OH TYR A 80 6283 6592 9124 100 -430 582 O ATOM 593 N ILE A 81 -4.493 16.994 5.919 1.00 75.13 N ANISOU 593 N ILE A 81 8695 9905 9947 227 -128 1186 N ATOM 594 CA ILE A 81 -5.513 17.526 6.813 1.00 84.58 C ANISOU 594 CA ILE A 81 9902 11258 10976 252 -21 1272 C ATOM 595 C ILE A 81 -6.155 18.811 6.279 1.00 75.87 C ANISOU 595 C ILE A 81 8849 10196 9783 259 24 1080 C ATOM 596 O ILE A 81 -5.484 19.672 5.712 1.00 77.67 O ANISOU 596 O ILE A 81 9150 10417 9946 262 -32 889 O ATOM 597 CB ILE A 81 -4.943 17.747 8.220 1.00 97.14 C ANISOU 597 CB ILE A 81 11548 13042 12318 302 -17 1380 C ATOM 598 CG1 ILE A 81 -5.381 16.604 9.135 1.00106.78 C ANISOU 598 CG1 ILE A 81 12694 14291 13587 301 32 1673 C ATOM 599 CG2 ILE A 81 -5.407 19.078 8.782 1.00104.35 C ANISOU 599 CG2 ILE A 81 12545 14133 12971 342 60 1271 C ATOM 600 CD1 ILE A 81 -4.315 16.177 10.117 1.00116.33 C ANISOU 600 CD1 ILE A 81 13927 15595 14678 331 -43 1818 C ATOM 601 N GLN A 82 -7.463 18.925 6.455 1.00 64.40 N ANISOU 601 N GLN A 82 7345 8781 8344 261 128 1146 N ATOM 602 CA GLN A 82 -8.206 20.097 6.010 1.00 55.61 C ANISOU 602 CA GLN A 82 6258 7699 7173 280 178 995 C ATOM 603 C GLN A 82 -7.955 20.561 4.577 1.00 49.64 C ANISOU 603 C GLN A 82 5526 6813 6522 244 93 800 C ATOM 604 O GLN A 82 -8.372 21.653 4.210 1.00 65.48 O ANISOU 604 O GLN A 82 7568 8843 8468 266 115 674 O ATOM 605 CB GLN A 82 -8.021 21.268 6.976 1.00 62.10 C ANISOU 605 CB GLN A 82 7178 8698 7718 350 233 923 C ATOM 606 CG GLN A 82 -9.191 21.486 7.930 1.00 77.18 C ANISOU 606 CG GLN A 82 9051 10747 9528 397 386 1029 C ATOM 607 CD GLN A 82 -8.934 20.925 9.314 1.00 90.31 C ANISOU 607 CD GLN A 82 10726 12565 11025 421 435 1210 C ATOM 608 OE1 GLN A 82 -7.922 20.259 9.548 1.00 93.15 O ANISOU 608 OE1 GLN A 82 11106 12911 11375 400 341 1283 O ATOM 609 NE2 GLN A 82 -9.845 21.201 10.245 1.00 92.17 N ANISOU 609 NE2 GLN A 82 10943 12955 11124 468 586 1291 N ATOM 610 N ALA A 83 -7.288 19.758 3.761 1.00 45.98 N ANISOU 610 N ALA A 83 5043 6213 6215 192 2 776 N ATOM 611 CA ALA A 83 -7.245 20.057 2.338 1.00 47.56 C ANISOU 611 CA ALA A 83 5254 6302 6516 148 -63 611 C ATOM 612 C ALA A 83 -8.676 20.287 1.866 1.00 60.27 C ANISOU 612 C ALA A 83 6797 7895 8209 131 -19 623 C ATOM 613 O ALA A 83 -9.599 19.580 2.295 1.00 69.10 O ANISOU 613 O ALA A 83 7819 9011 9426 118 38 774 O ATOM 614 CB ALA A 83 -6.627 18.911 1.576 1.00 37.25 C ANISOU 614 CB ALA A 83 3911 4849 5394 93 -138 603 C ATOM 615 N GLN A 84 -8.868 21.270 0.996 1.00 55.59 N ANISOU 615 N GLN A 84 6244 7292 7587 128 -47 479 N ATOM 616 CA GLN A 84 -10.209 21.568 0.483 1.00 56.66 C ANISOU 616 CA GLN A 84 6306 7414 7808 117 -24 491 C ATOM 617 C GLN A 84 -10.196 21.528 -1.032 1.00 61.93 C ANISOU 617 C GLN A 84 6975 7978 8578 48 -126 375 C ATOM 618 O GLN A 84 -11.186 21.843 -1.697 1.00 69.64 O ANISOU 618 O GLN A 84 7896 8940 9625 29 -144 365 O ATOM 619 CB GLN A 84 -10.726 22.901 1.017 1.00 41.50 C ANISOU 619 CB GLN A 84 4420 5599 5751 196 52 459 C ATOM 620 CG GLN A 84 -10.850 22.879 2.523 1.00 60.57 C ANISOU 620 CG GLN A 84 6833 8137 8045 260 165 567 C ATOM 621 CD GLN A 84 -10.563 24.217 3.148 1.00 73.40 C ANISOU 621 CD GLN A 84 8559 9859 9472 339 214 463 C ATOM 622 OE1 GLN A 84 -10.210 24.311 4.328 1.00 76.76 O ANISOU 622 OE1 GLN A 84 9031 10395 9738 386 276 497 O ATOM 623 NE2 GLN A 84 -10.708 25.268 2.359 1.00 76.13 N ANISOU 623 NE2 GLN A 84 8942 10160 9825 352 181 334 N ATOM 624 N CYS A 85 -9.058 21.110 -1.563 1.00 51.32 N ANISOU 624 N CYS A 85 5687 6572 7239 12 -193 290 N ATOM 625 CA CYS A 85 -8.922 20.866 -2.982 1.00 51.55 C ANISOU 625 CA CYS A 85 5725 6512 7350 -60 -282 176 C ATOM 626 C CYS A 85 -7.484 20.448 -3.252 1.00 47.41 C ANISOU 626 C CYS A 85 5263 5943 6809 -74 -318 89 C ATOM 627 O CYS A 85 -6.637 20.582 -2.376 1.00 43.03 O ANISOU 627 O CYS A 85 4746 5435 6167 -26 -289 117 O ATOM 628 CB CYS A 85 -9.291 22.109 -3.778 1.00 47.15 C ANISOU 628 CB CYS A 85 5211 5991 6713 -57 -312 86 C ATOM 629 SG CYS A 85 -8.310 23.537 -3.397 1.00 53.56 S ANISOU 629 SG CYS A 85 6146 6878 7327 6 -287 4 S ATOM 630 N ALA A 86 -7.207 19.946 -4.450 1.00 46.35 N ANISOU 630 N ALA A 86 5134 5725 6753 -139 -382 -19 N ATOM 631 CA ALA A 86 -5.913 19.338 -4.711 1.00 44.86 C ANISOU 631 CA ALA A 86 4977 5479 6590 -148 -400 -96 C ATOM 632 C ALA A 86 -5.633 19.329 -6.186 1.00 39.57 C ANISOU 632 C ALA A 86 4343 4765 5925 -210 -453 -258 C ATOM 633 O ALA A 86 -6.544 19.407 -6.999 1.00 39.90 O ANISOU 633 O ALA A 86 4371 4799 5991 -262 -494 -292 O ATOM 634 CB ALA A 86 -5.857 17.900 -4.151 1.00 42.24 C ANISOU 634 CB ALA A 86 4568 5048 6431 -151 -390 2 C ATOM 635 N ILE A 87 -4.354 19.246 -6.514 1.00 38.85 N ANISOU 635 N ILE A 87 4297 4661 5804 -205 -451 -356 N ATOM 636 CA ILE A 87 -3.907 19.072 -7.877 1.00 46.65 C ANISOU 636 CA ILE A 87 5320 5614 6791 -262 -480 -517 C ATOM 637 C ILE A 87 -3.027 17.858 -7.856 1.00 44.29 C ANISOU 637 C ILE A 87 4985 5211 6632 -253 -465 -561 C ATOM 638 O ILE A 87 -2.151 17.749 -7.007 1.00 50.10 O ANISOU 638 O ILE A 87 5706 5950 7378 -195 -436 -503 O ATOM 639 CB ILE A 87 -3.048 20.254 -8.371 1.00 45.55 C ANISOU 639 CB ILE A 87 5262 5564 6481 -259 -469 -602 C ATOM 640 CG1 ILE A 87 -3.896 21.517 -8.496 1.00 45.35 C ANISOU 640 CG1 ILE A 87 5275 5619 6335 -263 -489 -562 C ATOM 641 CG2 ILE A 87 -2.377 19.905 -9.709 1.00 43.60 C ANISOU 641 CG2 ILE A 87 5047 5293 6226 -312 -475 -766 C ATOM 642 CD1 ILE A 87 -3.112 22.735 -8.837 1.00 43.16 C ANISOU 642 CD1 ILE A 87 5074 5413 5913 -262 -478 -615 C ATOM 643 N ILE A 88 -3.278 16.931 -8.771 1.00 50.55 N ANISOU 643 N ILE A 88 5759 5907 7542 -308 -491 -663 N ATOM 644 CA ILE A 88 -2.398 15.785 -8.942 1.00 52.95 C ANISOU 644 CA ILE A 88 6032 6089 7997 -296 -471 -741 C ATOM 645 C ILE A 88 -1.593 15.993 -10.206 1.00 53.50 C ANISOU 645 C ILE A 88 6160 6185 7981 -325 -456 -943 C ATOM 646 O ILE A 88 -2.136 16.322 -11.266 1.00 51.92 O ANISOU 646 O ILE A 88 6009 6030 7688 -392 -488 -1047 O ATOM 647 CB ILE A 88 -3.161 14.458 -9.042 1.00 48.37 C ANISOU 647 CB ILE A 88 5387 5352 7641 -337 -501 -735 C ATOM 648 CG1 ILE A 88 -3.922 14.174 -7.737 1.00 49.07 C ANISOU 648 CG1 ILE A 88 5404 5417 7822 -310 -499 -508 C ATOM 649 CG2 ILE A 88 -2.188 13.315 -9.383 1.00 40.84 C ANISOU 649 CG2 ILE A 88 4407 4251 6858 -317 -476 -850 C ATOM 650 CD1 ILE A 88 -4.918 12.979 -7.820 1.00 44.16 C ANISOU 650 CD1 ILE A 88 4707 4641 7432 -372 -534 -471 C ATOM 651 N MET A 89 -0.289 15.799 -10.092 1.00 54.05 N ANISOU 651 N MET A 89 6219 6239 8078 -274 -405 -991 N ATOM 652 CA MET A 89 0.574 16.084 -11.213 1.00 59.04 C ANISOU 652 CA MET A 89 6898 6919 8614 -295 -365 -1171 C ATOM 653 C MET A 89 1.394 14.873 -11.621 1.00 58.90 C ANISOU 653 C MET A 89 6836 6771 8772 -270 -320 -1304 C ATOM 654 O MET A 89 1.871 14.122 -10.779 1.00 66.79 O ANISOU 654 O MET A 89 7761 7668 9947 -204 -308 -1224 O ATOM 655 CB MET A 89 1.481 17.281 -10.888 1.00 52.71 C ANISOU 655 CB MET A 89 6124 6248 7656 -264 -332 -1129 C ATOM 656 CG MET A 89 1.898 18.048 -12.109 1.00 47.13 C ANISOU 656 CG MET A 89 5485 5642 6779 -315 -301 -1264 C ATOM 657 SD MET A 89 2.810 19.529 -11.681 1.00 57.72 S ANISOU 657 SD MET A 89 6852 7116 7963 -298 -273 -1193 S ATOM 658 CE MET A 89 1.495 20.678 -11.216 1.00 39.40 C ANISOU 658 CE MET A 89 4589 4863 5519 -319 -342 -1056 C ATOM 659 N PHE A 90 1.541 14.693 -12.926 1.00 60.89 N ANISOU 659 N PHE A 90 7135 7030 8972 -320 -295 -1506 N ATOM 660 CA PHE A 90 2.500 13.731 -13.457 1.00 65.31 C ANISOU 660 CA PHE A 90 7659 7487 9667 -286 -224 -1674 C ATOM 661 C PHE A 90 3.347 14.361 -14.570 1.00 65.24 C ANISOU 661 C PHE A 90 7706 7608 9475 -308 -147 -1840 C ATOM 662 O PHE A 90 3.055 15.453 -15.055 1.00 54.44 O ANISOU 662 O PHE A 90 6412 6395 7879 -365 -162 -1828 O ATOM 663 CB PHE A 90 1.806 12.441 -13.943 1.00 64.60 C ANISOU 663 CB PHE A 90 7558 7225 9761 -323 -255 -1795 C ATOM 664 CG PHE A 90 0.866 12.648 -15.102 1.00 62.34 C ANISOU 664 CG PHE A 90 7357 7004 9325 -430 -306 -1932 C ATOM 665 CD1 PHE A 90 -0.440 13.062 -14.892 1.00 62.61 C ANISOU 665 CD1 PHE A 90 7407 7081 9301 -492 -404 -1810 C ATOM 666 CD2 PHE A 90 1.291 12.435 -16.401 1.00 64.23 C ANISOU 666 CD2 PHE A 90 7654 7275 9475 -467 -257 -2180 C ATOM 667 CE1 PHE A 90 -1.297 13.263 -15.955 1.00 63.33 C ANISOU 667 CE1 PHE A 90 7564 7241 9257 -591 -471 -1922 C ATOM 668 CE2 PHE A 90 0.435 12.635 -17.466 1.00 66.06 C ANISOU 668 CE2 PHE A 90 7967 7587 9544 -571 -320 -2299 C ATOM 669 CZ PHE A 90 -0.860 13.045 -17.241 1.00 64.91 C ANISOU 669 CZ PHE A 90 7830 7479 9352 -634 -437 -2164 C ATOM 670 N ASP A 91 4.399 13.650 -14.961 1.00 72.22 N ANISOU 670 N ASP A 91 8546 8425 10470 -259 -56 -1987 N ATOM 671 CA ASP A 91 5.307 14.096 -16.007 1.00 70.91 C ANISOU 671 CA ASP A 91 8414 8378 10151 -273 46 -2150 C ATOM 672 C ASP A 91 4.954 13.385 -17.315 1.00 65.64 C ANISOU 672 C ASP A 91 7809 7679 9452 -330 72 -2399 C ATOM 673 O ASP A 91 4.929 12.159 -17.359 1.00 68.04 O ANISOU 673 O ASP A 91 8073 7805 9974 -300 82 -2514 O ATOM 674 CB ASP A 91 6.741 13.780 -15.579 1.00 73.51 C ANISOU 674 CB ASP A 91 8636 8664 10630 -174 141 -2156 C ATOM 675 CG ASP A 91 7.768 14.179 -16.614 1.00 78.48 C ANISOU 675 CG ASP A 91 9276 9417 11127 -182 271 -2318 C ATOM 676 OD1 ASP A 91 7.373 14.745 -17.652 1.00 91.21 O ANISOU 676 OD1 ASP A 91 10990 11159 12505 -269 285 -2413 O ATOM 677 OD2 ASP A 91 8.973 13.928 -16.387 1.00 70.81 O ANISOU 677 OD2 ASP A 91 8202 8420 10283 -103 359 -2339 O ATOM 678 N VAL A 92 4.664 14.140 -18.373 1.00 55.88 N ANISOU 678 N VAL A 92 6674 6610 7948 -416 76 -2483 N ATOM 679 CA VAL A 92 4.237 13.521 -19.632 1.00 63.24 C ANISOU 679 CA VAL A 92 7681 7541 8806 -485 81 -2725 C ATOM 680 C VAL A 92 5.389 12.848 -20.378 1.00 73.05 C ANISOU 680 C VAL A 92 8903 8760 10093 -437 236 -2966 C ATOM 681 O VAL A 92 5.178 12.135 -21.357 1.00 88.43 O ANISOU 681 O VAL A 92 10906 10680 12013 -478 259 -3206 O ATOM 682 CB VAL A 92 3.461 14.496 -20.580 1.00 57.03 C ANISOU 682 CB VAL A 92 7014 6955 7700 -598 18 -2729 C ATOM 683 CG1 VAL A 92 2.179 14.990 -19.916 1.00 54.47 C ANISOU 683 CG1 VAL A 92 6697 6627 7373 -637 -137 -2520 C ATOM 684 CG2 VAL A 92 4.339 15.656 -21.040 1.00 55.37 C ANISOU 684 CG2 VAL A 92 6838 6946 7256 -606 114 -2693 C ATOM 685 N THR A 93 6.607 13.068 -19.908 1.00 59.71 N ANISOU 685 N THR A 93 7127 7084 8476 -351 343 -2909 N ATOM 686 CA THR A 93 7.765 12.409 -20.489 1.00 74.03 C ANISOU 686 CA THR A 93 8889 8865 10374 -286 506 -3120 C ATOM 687 C THR A 93 8.036 11.096 -19.754 1.00 80.15 C ANISOU 687 C THR A 93 9553 9378 11524 -181 511 -3149 C ATOM 688 O THR A 93 8.945 10.350 -20.111 1.00 92.54 O ANISOU 688 O THR A 93 11058 10865 13238 -103 640 -3328 O ATOM 689 CB THR A 93 9.014 13.311 -20.409 1.00 79.23 C ANISOU 689 CB THR A 93 9486 9674 10943 -248 624 -3042 C ATOM 690 OG1 THR A 93 9.359 13.536 -19.037 1.00 80.10 O ANISOU 690 OG1 THR A 93 9490 9716 11228 -178 568 -2806 O ATOM 691 CG2 THR A 93 8.752 14.652 -21.082 1.00 74.53 C ANISOU 691 CG2 THR A 93 8997 9320 10002 -354 616 -2979 C ATOM 692 N SER A 94 7.223 10.816 -18.738 1.00 73.44 N ANISOU 692 N SER A 94 8678 8395 10832 -177 374 -2967 N ATOM 693 CA SER A 94 7.479 9.716 -17.813 1.00 74.71 C ANISOU 693 CA SER A 94 8722 8312 11351 -76 361 -2908 C ATOM 694 C SER A 94 6.198 8.932 -17.476 1.00 78.34 C ANISOU 694 C SER A 94 9207 8595 11965 -123 231 -2869 C ATOM 695 O SER A 94 5.416 9.341 -16.618 1.00 72.13 O ANISOU 695 O SER A 94 8420 7825 11160 -153 119 -2637 O ATOM 696 CB SER A 94 8.121 10.271 -16.538 1.00 70.06 C ANISOU 696 CB SER A 94 8034 7757 10828 -1 341 -2636 C ATOM 697 OG SER A 94 8.653 9.250 -15.715 1.00 77.16 O ANISOU 697 OG SER A 94 8807 8448 12063 111 346 -2573 O ATOM 698 N ARG A 95 6.006 7.797 -18.144 1.00 72.71 N ANISOU 698 N ARG A 95 8506 7708 11412 -130 254 -3104 N ATOM 699 CA ARG A 95 4.801 6.991 -17.984 1.00 81.15 C ANISOU 699 CA ARG A 95 9593 8597 12642 -194 134 -3100 C ATOM 700 C ARG A 95 4.544 6.519 -16.550 1.00 85.66 C ANISOU 700 C ARG A 95 10062 8995 13491 -137 57 -2819 C ATOM 701 O ARG A 95 3.389 6.422 -16.123 1.00 87.33 O ANISOU 701 O ARG A 95 10286 9156 13739 -209 -60 -2687 O ATOM 702 CB ARG A 95 4.822 5.783 -18.935 1.00 96.57 C ANISOU 702 CB ARG A 95 11570 10364 14758 -203 182 -3430 C ATOM 703 CG ARG A 95 4.885 6.139 -20.419 1.00104.24 C ANISOU 703 CG ARG A 95 12663 11516 15428 -278 246 -3728 C ATOM 704 CD ARG A 95 4.646 4.921 -21.316 1.00108.18 C ANISOU 704 CD ARG A 95 13204 11825 16074 -310 262 -4068 C ATOM 705 NE ARG A 95 4.549 5.291 -22.729 1.00113.52 N ANISOU 705 NE ARG A 95 14013 12705 16413 -400 302 -4344 N ATOM 706 CZ ARG A 95 5.554 5.222 -23.602 1.00124.16 C ANISOU 706 CZ ARG A 95 15386 14133 17654 -349 474 -4598 C ATOM 707 NH1 ARG A 95 6.750 4.782 -23.222 1.00124.05 N ANISOU 707 NH1 ARG A 95 15260 14002 17873 -202 623 -4620 N ATOM 708 NH2 ARG A 95 5.361 5.590 -24.863 1.00127.40 N ANISOU 708 NH2 ARG A 95 15928 14754 17723 -445 499 -4825 N ATOM 709 N VAL A 96 5.605 6.209 -15.811 1.00 84.39 N ANISOU 709 N VAL A 96 9791 8748 13525 -10 121 -2720 N ATOM 710 CA VAL A 96 5.430 5.677 -14.460 1.00 85.47 C ANISOU 710 CA VAL A 96 9831 8724 13922 49 50 -2446 C ATOM 711 C VAL A 96 4.758 6.696 -13.538 1.00 84.23 C ANISOU 711 C VAL A 96 9693 8739 13572 4 -43 -2156 C ATOM 712 O VAL A 96 3.953 6.338 -12.681 1.00 88.57 O ANISOU 712 O VAL A 96 10212 9192 14249 -14 -127 -1955 O ATOM 713 CB VAL A 96 6.756 5.168 -13.848 1.00 78.13 C ANISOU 713 CB VAL A 96 8771 7684 13233 200 123 -2382 C ATOM 714 CG1 VAL A 96 7.844 6.214 -13.981 1.00 81.64 C ANISOU 714 CG1 VAL A 96 9201 8362 13458 245 204 -2386 C ATOM 715 CG2 VAL A 96 6.554 4.767 -12.391 1.00 64.33 C ANISOU 715 CG2 VAL A 96 6931 5816 11695 252 34 -2053 C ATOM 716 N THR A 97 5.075 7.971 -13.727 1.00 78.86 N ANISOU 716 N THR A 97 9063 8311 12588 -15 -19 -2137 N ATOM 717 CA THR A 97 4.425 9.011 -12.946 1.00 75.83 C ANISOU 717 CA THR A 97 8710 8090 12014 -55 -97 -1900 C ATOM 718 C THR A 97 2.927 9.012 -13.217 1.00 73.64 C ANISOU 718 C THR A 97 8498 7806 11675 -167 -185 -1896 C ATOM 719 O THR A 97 2.137 9.265 -12.314 1.00 81.49 O ANISOU 719 O THR A 97 9478 8820 12665 -185 -256 -1676 O ATOM 720 CB THR A 97 4.989 10.400 -13.245 1.00 67.39 C ANISOU 720 CB THR A 97 7691 7271 10644 -68 -56 -1908 C ATOM 721 OG1 THR A 97 4.549 10.824 -14.542 1.00 71.09 O ANISOU 721 OG1 THR A 97 8264 7845 10903 -160 -41 -2106 O ATOM 722 CG2 THR A 97 6.506 10.377 -13.195 1.00 57.45 C ANISOU 722 CG2 THR A 97 6354 6025 9451 28 39 -1951 C ATOM 723 N TYR A 98 2.530 8.729 -14.453 1.00 71.17 N ANISOU 723 N TYR A 98 8254 7476 11311 -243 -182 -2140 N ATOM 724 CA TYR A 98 1.107 8.620 -14.748 1.00 74.55 C ANISOU 724 CA TYR A 98 8727 7886 11715 -354 -283 -2144 C ATOM 725 C TYR A 98 0.504 7.360 -14.123 1.00 70.35 C ANISOU 725 C TYR A 98 8118 7098 11516 -357 -335 -2067 C ATOM 726 O TYR A 98 -0.646 7.362 -13.684 1.00 59.30 O ANISOU 726 O TYR A 98 6703 5682 10147 -422 -421 -1920 O ATOM 727 CB TYR A 98 0.832 8.641 -16.251 1.00 71.40 C ANISOU 727 CB TYR A 98 8423 7550 11155 -446 -285 -2429 C ATOM 728 CG TYR A 98 -0.632 8.440 -16.554 1.00 64.36 C ANISOU 728 CG TYR A 98 7558 6629 10265 -565 -410 -2435 C ATOM 729 CD1 TYR A 98 -1.561 9.410 -16.212 1.00 63.31 C ANISOU 729 CD1 TYR A 98 7440 6649 9966 -616 -490 -2245 C ATOM 730 CD2 TYR A 98 -1.092 7.276 -17.154 1.00 65.96 C ANISOU 730 CD2 TYR A 98 7761 6642 10658 -627 -450 -2631 C ATOM 731 CE1 TYR A 98 -2.904 9.239 -16.468 1.00 64.87 C ANISOU 731 CE1 TYR A 98 7639 6826 10183 -723 -607 -2237 C ATOM 732 CE2 TYR A 98 -2.441 7.096 -17.418 1.00 67.10 C ANISOU 732 CE2 TYR A 98 7914 6763 10818 -747 -578 -2631 C ATOM 733 CZ TYR A 98 -3.341 8.087 -17.070 1.00 69.77 C ANISOU 733 CZ TYR A 98 8252 7269 10987 -793 -656 -2424 C ATOM 734 OH TYR A 98 -4.686 7.944 -17.314 1.00 79.68 O ANISOU 734 OH TYR A 98 9494 8511 12269 -910 -786 -2408 O ATOM 735 N LYS A 99 1.290 6.287 -14.086 1.00 74.20 N ANISOU 735 N LYS A 99 8546 7378 12267 -283 -277 -2157 N ATOM 736 CA LYS A 99 0.833 5.028 -13.512 1.00 73.52 C ANISOU 736 CA LYS A 99 8383 7018 12535 -281 -320 -2078 C ATOM 737 C LYS A 99 0.698 5.090 -11.986 1.00 71.21 C ANISOU 737 C LYS A 99 8006 6711 12340 -226 -350 -1717 C ATOM 738 O LYS A 99 -0.058 4.327 -11.393 1.00 66.23 O ANISOU 738 O LYS A 99 7318 5911 11935 -258 -405 -1573 O ATOM 739 CB LYS A 99 1.737 3.879 -13.949 1.00 78.30 C ANISOU 739 CB LYS A 99 8949 7391 13412 -208 -246 -2286 C ATOM 740 CG LYS A 99 1.511 3.446 -15.393 1.00 96.04 C ANISOU 740 CG LYS A 99 11278 9585 15630 -288 -234 -2655 C ATOM 741 CD LYS A 99 2.459 2.318 -15.821 1.00110.65 C ANISOU 741 CD LYS A 99 13087 11195 17758 -200 -141 -2886 C ATOM 742 CE LYS A 99 2.067 0.966 -15.223 1.00109.83 C ANISOU 742 CE LYS A 99 12898 10741 18090 -190 -190 -2809 C ATOM 743 NZ LYS A 99 2.302 0.893 -13.750 1.00104.32 N ANISOU 743 NZ LYS A 99 12090 9985 17561 -101 -209 -2429 N ATOM 744 N ASN A 100 1.406 6.019 -11.353 1.00 71.92 N ANISOU 744 N ASN A 100 8090 6986 12250 -152 -317 -1571 N ATOM 745 CA ASN A 100 1.219 6.246 -9.921 1.00 76.60 C ANISOU 745 CA ASN A 100 8625 7619 12860 -110 -350 -1239 C ATOM 746 C ASN A 100 0.139 7.268 -9.568 1.00 72.77 C ANISOU 746 C ASN A 100 8186 7329 12135 -183 -401 -1096 C ATOM 747 O ASN A 100 -0.079 7.551 -8.390 1.00 69.54 O ANISOU 747 O ASN A 100 7739 6982 11700 -152 -418 -836 O ATOM 748 CB ASN A 100 2.526 6.654 -9.254 1.00 84.20 C ANISOU 748 CB ASN A 100 9546 8671 13777 7 -305 -1139 C ATOM 749 CG ASN A 100 3.540 5.548 -9.253 1.00 86.43 C ANISOU 749 CG ASN A 100 9744 8739 14358 104 -262 -1196 C ATOM 750 OD1 ASN A 100 4.727 5.789 -9.446 1.00 82.23 O ANISOU 750 OD1 ASN A 100 9185 8262 13795 183 -203 -1278 O ATOM 751 ND2 ASN A 100 3.077 4.315 -9.052 1.00 96.17 N ANISOU 751 ND2 ASN A 100 10922 9714 15903 98 -290 -1150 N ATOM 752 N VAL A 101 -0.538 7.815 -10.575 1.00 71.84 N ANISOU 752 N VAL A 101 8146 7310 11841 -276 -425 -1262 N ATOM 753 CA VAL A 101 -1.603 8.794 -10.331 1.00 62.28 C ANISOU 753 CA VAL A 101 6967 6271 10424 -338 -473 -1138 C ATOM 754 C VAL A 101 -2.750 8.227 -9.496 1.00 63.35 C ANISOU 754 C VAL A 101 7032 6309 10730 -378 -521 -928 C ATOM 755 O VAL A 101 -3.220 8.886 -8.564 1.00 57.50 O ANISOU 755 O VAL A 101 6274 5691 9881 -362 -524 -712 O ATOM 756 CB VAL A 101 -2.167 9.379 -11.636 1.00 54.75 C ANISOU 756 CB VAL A 101 6099 5427 9278 -432 -507 -1344 C ATOM 757 CG1 VAL A 101 -3.546 9.961 -11.397 1.00 49.20 C ANISOU 757 CG1 VAL A 101 5391 4818 8484 -504 -576 -1209 C ATOM 758 CG2 VAL A 101 -1.210 10.427 -12.193 1.00 56.67 C ANISOU 758 CG2 VAL A 101 6416 5853 9264 -398 -453 -1454 C ATOM 759 N PRO A 102 -3.209 7.006 -9.832 1.00 75.32 N ANISOU 759 N PRO A 102 8503 7601 12516 -433 -553 -996 N ATOM 760 CA PRO A 102 -4.259 6.380 -9.020 1.00 77.50 C ANISOU 760 CA PRO A 102 8694 7765 12987 -479 -590 -778 C ATOM 761 C PRO A 102 -3.802 6.236 -7.577 1.00 74.40 C ANISOU 761 C PRO A 102 8239 7367 12663 -384 -549 -490 C ATOM 762 O PRO A 102 -4.602 6.443 -6.664 1.00 71.16 O ANISOU 762 O PRO A 102 7784 7021 12231 -400 -553 -252 O ATOM 763 CB PRO A 102 -4.423 5.001 -9.666 1.00 69.59 C ANISOU 763 CB PRO A 102 7657 6484 12300 -539 -622 -934 C ATOM 764 CG PRO A 102 -4.036 5.209 -11.080 1.00 71.13 C ANISOU 764 CG PRO A 102 7942 6718 12365 -571 -626 -1271 C ATOM 765 CD PRO A 102 -2.890 6.197 -11.023 1.00 75.59 C ANISOU 765 CD PRO A 102 8564 7478 12677 -469 -556 -1289 C ATOM 766 N ASN A 103 -2.530 5.887 -7.387 1.00 65.25 N ANISOU 766 N ASN A 103 7072 6140 11579 -285 -510 -512 N ATOM 767 CA ASN A 103 -1.954 5.756 -6.055 1.00 69.01 C ANISOU 767 CA ASN A 103 7492 6627 12103 -190 -487 -243 C ATOM 768 C ASN A 103 -2.125 7.022 -5.246 1.00 73.70 C ANISOU 768 C ASN A 103 8121 7492 12392 -166 -477 -81 C ATOM 769 O ASN A 103 -2.589 6.974 -4.113 1.00 83.21 O ANISOU 769 O ASN A 103 9280 8735 13599 -154 -474 182 O ATOM 770 CB ASN A 103 -0.465 5.415 -6.122 1.00 76.45 C ANISOU 770 CB ASN A 103 8419 7497 13132 -83 -456 -322 C ATOM 771 CG ASN A 103 -0.204 4.038 -6.680 1.00 85.52 C ANISOU 771 CG ASN A 103 9518 8344 14632 -78 -454 -450 C ATOM 772 OD1 ASN A 103 0.851 3.791 -7.260 1.00 88.60 O ANISOU 772 OD1 ASN A 103 9908 8667 15091 -12 -416 -634 O ATOM 773 ND2 ASN A 103 -1.165 3.132 -6.516 1.00 87.38 N ANISOU 773 ND2 ASN A 103 9704 8388 15107 -150 -488 -359 N ATOM 774 N TRP A 104 -1.736 8.157 -5.818 1.00 70.50 N ANISOU 774 N TRP A 104 7794 7270 11720 -159 -464 -237 N ATOM 775 CA TRP A 104 -1.899 9.432 -5.117 1.00 70.89 C ANISOU 775 CA TRP A 104 7885 7562 11488 -138 -455 -116 C ATOM 776 C TRP A 104 -3.355 9.709 -4.843 1.00 64.68 C ANISOU 776 C TRP A 104 7088 6833 10654 -207 -466 -2 C ATOM 777 O TRP A 104 -3.714 10.056 -3.721 1.00 64.56 O ANISOU 777 O TRP A 104 7052 6923 10554 -178 -447 213 O ATOM 778 CB TRP A 104 -1.263 10.607 -5.873 1.00 65.25 C ANISOU 778 CB TRP A 104 7256 7010 10524 -130 -441 -306 C ATOM 779 CG TRP A 104 0.228 10.547 -5.880 1.00 62.54 C ANISOU 779 CG TRP A 104 6906 6661 10197 -52 -418 -370 C ATOM 780 CD1 TRP A 104 1.028 10.178 -6.922 1.00 66.75 C ANISOU 780 CD1 TRP A 104 7445 7111 10806 -45 -392 -590 C ATOM 781 CD2 TRP A 104 1.105 10.834 -4.780 1.00 62.64 C ANISOU 781 CD2 TRP A 104 6891 6758 10153 31 -417 -212 C ATOM 782 NE1 TRP A 104 2.350 10.230 -6.545 1.00 66.18 N ANISOU 782 NE1 TRP A 104 7336 7062 10746 41 -369 -572 N ATOM 783 CE2 TRP A 104 2.424 10.629 -5.242 1.00 64.06 C ANISOU 783 CE2 TRP A 104 7047 6895 10399 85 -395 -341 C ATOM 784 CE3 TRP A 104 0.901 11.251 -3.463 1.00 65.52 C ANISOU 784 CE3 TRP A 104 7246 7241 10408 64 -432 17 C ATOM 785 CZ2 TRP A 104 3.538 10.831 -4.419 1.00 61.67 C ANISOU 785 CZ2 TRP A 104 6700 6660 10070 166 -406 -235 C ATOM 786 CZ3 TRP A 104 2.004 11.450 -2.653 1.00 73.45 C ANISOU 786 CZ3 TRP A 104 8225 8319 11364 140 -447 111 C ATOM 787 CH2 TRP A 104 3.308 11.239 -3.135 1.00 71.48 C ANISOU 787 CH2 TRP A 104 7940 8020 11197 188 -441 -10 C ATOM 788 N HIS A 105 -4.192 9.551 -5.863 1.00 64.34 N ANISOU 788 N HIS A 105 7053 6730 10662 -297 -498 -148 N ATOM 789 CA HIS A 105 -5.620 9.827 -5.714 1.00 70.20 C ANISOU 789 CA HIS A 105 7764 7528 11380 -367 -515 -50 C ATOM 790 C HIS A 105 -6.233 9.087 -4.523 1.00 71.85 C ANISOU 790 C HIS A 105 7878 7666 11757 -366 -493 223 C ATOM 791 O HIS A 105 -7.018 9.655 -3.763 1.00 68.03 O ANISOU 791 O HIS A 105 7369 7313 11165 -364 -463 391 O ATOM 792 CB HIS A 105 -6.388 9.500 -6.995 1.00 71.67 C ANISOU 792 CB HIS A 105 7953 7629 11651 -475 -576 -243 C ATOM 793 CG HIS A 105 -7.852 9.769 -6.901 1.00 69.99 C ANISOU 793 CG HIS A 105 7686 7471 11436 -548 -605 -142 C ATOM 794 ND1 HIS A 105 -8.747 8.869 -6.345 1.00 70.43 N ANISOU 794 ND1 HIS A 105 7633 7402 11725 -601 -610 24 N ATOM 795 CD2 HIS A 105 -8.598 10.838 -7.276 1.00 63.66 C ANISOU 795 CD2 HIS A 105 6908 6833 10446 -576 -628 -170 C ATOM 796 CE1 HIS A 105 -9.961 9.370 -6.390 1.00 64.33 C ANISOU 796 CE1 HIS A 105 6814 6722 10906 -658 -631 85 C ATOM 797 NE2 HIS A 105 -9.901 10.566 -6.952 1.00 60.58 N ANISOU 797 NE2 HIS A 105 6417 6420 10179 -639 -645 -31 N ATOM 798 N ARG A 106 -5.859 7.824 -4.357 1.00 74.01 N ANISOU 798 N ARG A 106 8096 7728 12297 -362 -499 271 N ATOM 799 CA ARG A 106 -6.339 7.025 -3.239 1.00 81.88 C ANISOU 799 CA ARG A 106 8999 8640 13472 -364 -477 554 C ATOM 800 C ARG A 106 -5.905 7.593 -1.884 1.00 77.89 C ANISOU 800 C ARG A 106 8502 8312 12779 -270 -426 785 C ATOM 801 O ARG A 106 -6.745 7.849 -1.019 1.00 72.45 O ANISOU 801 O ARG A 106 7776 7733 12019 -281 -386 991 O ATOM 802 CB ARG A 106 -5.879 5.572 -3.395 1.00 97.43 C ANISOU 802 CB ARG A 106 10912 10322 15783 -370 -500 551 C ATOM 803 CG ARG A 106 -5.965 4.746 -2.124 1.00107.59 C ANISOU 803 CG ARG A 106 12112 11520 17246 -343 -474 878 C ATOM 804 CD ARG A 106 -5.520 3.306 -2.356 1.00117.07 C ANISOU 804 CD ARG A 106 13255 12403 18824 -347 -502 868 C ATOM 805 NE ARG A 106 -4.426 3.208 -3.321 1.00118.57 N ANISOU 805 NE ARG A 106 13500 12506 19044 -297 -520 581 N ATOM 806 CZ ARG A 106 -3.134 3.292 -3.014 1.00113.94 C ANISOU 806 CZ ARG A 106 12931 11949 18414 -181 -507 588 C ATOM 807 NH1 ARG A 106 -2.752 3.481 -1.759 1.00112.85 N ANISOU 807 NH1 ARG A 106 12767 11927 18185 -105 -493 867 N ATOM 808 NH2 ARG A 106 -2.221 3.189 -3.970 1.00113.25 N ANISOU 808 NH2 ARG A 106 12879 11783 18367 -142 -507 315 N ATOM 809 N ASP A 107 -4.598 7.793 -1.706 1.00 80.91 N ANISOU 809 N ASP A 107 8931 8733 13078 -181 -429 744 N ATOM 810 CA ASP A 107 -4.040 8.283 -0.433 1.00 92.61 C ANISOU 810 CA ASP A 107 10426 10385 14378 -95 -403 944 C ATOM 811 C ASP A 107 -4.633 9.627 -0.025 1.00 87.76 C ANISOU 811 C ASP A 107 9866 10024 13453 -93 -366 964 C ATOM 812 O ASP A 107 -4.504 10.072 1.121 1.00 83.30 O ANISOU 812 O ASP A 107 9313 9620 12717 -39 -337 1138 O ATOM 813 CB ASP A 107 -2.520 8.419 -0.533 1.00 99.00 C ANISOU 813 CB ASP A 107 11269 11204 15143 -12 -428 846 C ATOM 814 CG ASP A 107 -1.853 7.144 -1.008 1.00115.62 C ANISOU 814 CG ASP A 107 13316 13050 17566 5 -454 796 C ATOM 815 OD1 ASP A 107 -2.469 6.057 -0.873 1.00115.58 O ANISOU 815 OD1 ASP A 107 13239 12853 17822 -36 -457 916 O ATOM 816 OD2 ASP A 107 -0.713 7.232 -1.518 1.00120.02 O ANISOU 816 OD2 ASP A 107 13891 13587 18125 59 -465 635 O ATOM 817 N LEU A 108 -5.282 10.257 -0.996 1.00 84.57 N ANISOU 817 N LEU A 108 9497 9653 12984 -150 -372 778 N ATOM 818 CA LEU A 108 -5.844 11.586 -0.878 1.00 81.00 C ANISOU 818 CA LEU A 108 9097 9408 12272 -145 -343 748 C ATOM 819 C LEU A 108 -7.284 11.473 -0.381 1.00 80.64 C ANISOU 819 C LEU A 108 8978 9391 12270 -191 -298 915 C ATOM 820 O LEU A 108 -7.620 11.908 0.724 1.00 74.88 O ANISOU 820 O LEU A 108 8242 8809 11400 -150 -236 1087 O ATOM 821 CB LEU A 108 -5.802 12.223 -2.266 1.00 72.82 C ANISOU 821 CB LEU A 108 8121 8372 11173 -185 -381 481 C ATOM 822 CG LEU A 108 -6.033 13.712 -2.482 1.00 64.21 C ANISOU 822 CG LEU A 108 7105 7465 9826 -172 -369 390 C ATOM 823 CD1 LEU A 108 -5.272 14.520 -1.464 1.00 60.99 C ANISOU 823 CD1 LEU A 108 6750 7210 9212 -90 -337 460 C ATOM 824 CD2 LEU A 108 -5.612 14.081 -3.899 1.00 57.73 C ANISOU 824 CD2 LEU A 108 6346 6618 8969 -208 -416 144 C ATOM 825 N VAL A 109 -8.125 10.873 -1.213 1.00 80.42 N ANISOU 825 N VAL A 109 8891 9226 12440 -279 -330 855 N ATOM 826 CA VAL A 109 -9.519 10.597 -0.882 1.00 75.76 C ANISOU 826 CA VAL A 109 8201 8631 11954 -340 -296 1009 C ATOM 827 C VAL A 109 -9.685 9.973 0.510 1.00 73.36 C ANISOU 827 C VAL A 109 7829 8340 11706 -313 -225 1309 C ATOM 828 O VAL A 109 -10.592 10.320 1.258 1.00 80.35 O ANISOU 828 O VAL A 109 8662 9351 12515 -312 -148 1470 O ATOM 829 CB VAL A 109 -10.123 9.673 -1.954 1.00 76.16 C ANISOU 829 CB VAL A 109 8187 8476 12275 -451 -366 905 C ATOM 830 CG1 VAL A 109 -11.470 9.124 -1.509 1.00 95.62 C ANISOU 830 CG1 VAL A 109 10518 10899 14914 -525 -335 1101 C ATOM 831 CG2 VAL A 109 -10.235 10.419 -3.275 1.00 63.24 C ANISOU 831 CG2 VAL A 109 6613 6880 10535 -487 -432 640 C ATOM 832 N ARG A 110 -8.797 9.054 0.854 1.00 73.56 N ANISOU 832 N ARG A 110 7849 8238 11861 -287 -245 1390 N ATOM 833 CA ARG A 110 -8.785 8.455 2.185 1.00 75.91 C ANISOU 833 CA ARG A 110 8093 8557 12192 -256 -190 1694 C ATOM 834 C ARG A 110 -8.792 9.497 3.319 1.00 77.96 C ANISOU 834 C ARG A 110 8402 9095 12123 -179 -112 1813 C ATOM 835 O ARG A 110 -9.437 9.293 4.350 1.00 79.15 O ANISOU 835 O ARG A 110 8496 9331 12247 -180 -33 2062 O ATOM 836 CB ARG A 110 -7.576 7.523 2.322 1.00 70.29 C ANISOU 836 CB ARG A 110 7387 7687 11634 -214 -242 1736 C ATOM 837 CG ARG A 110 -7.306 7.055 3.733 1.00 68.71 C ANISOU 837 CG ARG A 110 7152 7544 11409 -163 -203 2057 C ATOM 838 CD ARG A 110 -5.937 6.398 3.842 1.00 75.62 C ANISOU 838 CD ARG A 110 8040 8299 12393 -95 -270 2077 C ATOM 839 NE ARG A 110 -5.412 6.515 5.200 1.00 82.48 N ANISOU 839 NE ARG A 110 8922 9337 13081 -20 -253 2330 N ATOM 840 CZ ARG A 110 -4.547 7.446 5.600 1.00 85.47 C ANISOU 840 CZ ARG A 110 9383 9920 13170 57 -274 2266 C ATOM 841 NH1 ARG A 110 -4.072 8.352 4.743 1.00 81.35 N ANISOU 841 NH1 ARG A 110 8937 9450 12523 71 -302 1969 N ATOM 842 NH2 ARG A 110 -4.146 7.468 6.866 1.00 83.30 N ANISOU 842 NH2 ARG A 110 9116 9803 12730 114 -271 2507 N ATOM 843 N VAL A 111 -8.067 10.600 3.137 1.00 72.15 N ANISOU 843 N VAL A 111 7774 8499 11140 -117 -132 1634 N ATOM 844 CA VAL A 111 -8.007 11.640 4.153 1.00 73.29 C ANISOU 844 CA VAL A 111 7979 8895 10973 -47 -69 1701 C ATOM 845 C VAL A 111 -8.983 12.758 3.798 1.00 84.89 C ANISOU 845 C VAL A 111 9463 10483 12307 -57 -18 1580 C ATOM 846 O VAL A 111 -9.574 13.376 4.679 1.00 86.61 O ANISOU 846 O VAL A 111 9681 10878 12349 -22 74 1683 O ATOM 847 CB VAL A 111 -6.588 12.216 4.303 1.00 76.73 C ANISOU 847 CB VAL A 111 8517 9411 11227 26 -125 1593 C ATOM 848 CG1 VAL A 111 -6.571 13.338 5.358 1.00 78.09 C ANISOU 848 CG1 VAL A 111 8760 9841 11069 89 -67 1634 C ATOM 849 CG2 VAL A 111 -5.602 11.123 4.663 1.00 76.23 C ANISOU 849 CG2 VAL A 111 8422 9230 11313 49 -181 1722 C ATOM 850 N CYS A 112 -9.158 13.019 2.505 1.00 90.82 N ANISOU 850 N CYS A 112 10224 11142 13140 -103 -76 1364 N ATOM 851 CA CYS A 112 -10.087 14.074 2.092 1.00 94.36 C ANISOU 851 CA CYS A 112 10676 11690 13485 -109 -44 1261 C ATOM 852 C CYS A 112 -11.262 13.507 1.335 1.00107.52 C ANISOU 852 C CYS A 112 12233 13237 15382 -200 -61 1268 C ATOM 853 O CYS A 112 -11.286 13.532 0.100 1.00112.03 O ANISOU 853 O CYS A 112 12816 13713 16037 -252 -145 1084 O ATOM 854 CB CYS A 112 -9.398 15.170 1.279 1.00 85.76 C ANISOU 854 CB CYS A 112 9699 10646 12241 -81 -100 1017 C ATOM 855 SG CYS A 112 -7.721 15.470 1.820 1.00 91.48 S ANISOU 855 SG CYS A 112 10532 11434 12793 -8 -129 974 S ATOM 856 N GLU A 113 -12.221 12.981 2.100 1.00109.62 N ANISOU 856 N GLU A 113 12388 13519 15743 -224 18 1487 N ATOM 857 CA GLU A 113 -13.463 12.469 1.549 1.00116.05 C ANISOU 857 CA GLU A 113 13072 14238 16786 -318 9 1525 C ATOM 858 C GLU A 113 -13.879 13.528 0.552 1.00121.81 C ANISOU 858 C GLU A 113 13830 15022 17430 -320 -39 1318 C ATOM 859 O GLU A 113 -13.973 14.696 0.920 1.00126.82 O ANISOU 859 O GLU A 113 14515 15823 17849 -242 20 1288 O ATOM 860 CB GLU A 113 -14.557 12.316 2.630 1.00123.70 C ANISOU 860 CB GLU A 113 13919 15305 17778 -319 140 1780 C ATOM 861 CG GLU A 113 -14.082 12.016 4.035 1.00127.30 C ANISOU 861 CG GLU A 113 14396 15856 18116 -259 235 2002 C ATOM 862 CD GLU A 113 -13.584 10.572 4.276 1.00133.12 C ANISOU 862 CD GLU A 113 15092 16412 19074 -310 196 2162 C ATOM 863 OE1 GLU A 113 -14.169 9.595 3.758 1.00131.16 O ANISOU 863 OE1 GLU A 113 14735 15974 19125 -411 156 2211 O ATOM 864 OE2 GLU A 113 -12.636 10.404 5.075 1.00137.24 O ANISOU 864 OE2 GLU A 113 15684 16983 19476 -247 206 2260 O ATOM 865 N ASN A 114 -14.010 13.151 -0.719 1.00120.34 N ANISOU 865 N ASN A 114 13629 14697 17399 -404 -154 1164 N ATOM 866 CA ASN A 114 -14.696 13.986 -1.727 1.00120.68 C ANISOU 866 CA ASN A 114 13663 14784 17405 -430 -215 1015 C ATOM 867 C ASN A 114 -14.361 15.495 -1.748 1.00109.10 C ANISOU 867 C ASN A 114 12305 13479 15669 -334 -192 907 C ATOM 868 O ASN A 114 -15.141 16.332 -1.275 1.00113.86 O ANISOU 868 O ASN A 114 12865 14208 16191 -283 -117 973 O ATOM 869 CB ASN A 114 -16.219 13.817 -1.597 1.00122.45 C ANISOU 869 CB ASN A 114 13718 15023 17787 -486 -184 1151 C ATOM 870 CG ASN A 114 -16.921 13.641 -2.943 1.00119.83 C ANISOU 870 CG ASN A 114 13323 14602 17604 -592 -320 1019 C ATOM 871 OD1 ASN A 114 -16.278 13.547 -3.989 1.00112.82 O ANISOU 871 OD1 ASN A 114 12527 13639 16700 -630 -432 823 O ATOM 872 ND2 ASN A 114 -18.252 13.563 -2.910 1.00122.78 N ANISOU 872 ND2 ASN A 114 13533 14994 18124 -645 -310 1129 N ATOM 873 N ILE A 115 -13.188 15.832 -2.270 1.00 87.11 N ANISOU 873 N ILE A 115 9654 10681 12762 -310 -247 743 N ATOM 874 CA ILE A 115 -12.838 17.218 -2.520 1.00 74.13 C ANISOU 874 CA ILE A 115 8113 9154 10901 -244 -248 624 C ATOM 875 C ILE A 115 -12.514 17.319 -4.007 1.00 67.27 C ANISOU 875 C ILE A 115 7301 8218 10042 -306 -369 428 C ATOM 876 O ILE A 115 -12.218 16.306 -4.642 1.00 67.41 O ANISOU 876 O ILE A 115 7309 8110 10194 -378 -435 364 O ATOM 877 CB ILE A 115 -11.631 17.680 -1.671 1.00 66.21 C ANISOU 877 CB ILE A 115 7222 8226 9710 -157 -194 619 C ATOM 878 CG1 ILE A 115 -10.443 16.738 -1.892 1.00 64.97 C ANISOU 878 CG1 ILE A 115 7109 7958 9619 -183 -244 570 C ATOM 879 CG2 ILE A 115 -12.018 17.772 -0.189 1.00 59.59 C ANISOU 879 CG2 ILE A 115 6344 7496 8803 -92 -72 802 C ATOM 880 CD1 ILE A 115 -9.104 17.341 -1.562 1.00 60.07 C ANISOU 880 CD1 ILE A 115 6603 7401 8819 -118 -239 498 C ATOM 881 N PRO A 116 -12.608 18.533 -4.575 1.00 57.35 N ANISOU 881 N PRO A 116 6101 7044 8644 -278 -396 335 N ATOM 882 CA PRO A 116 -12.357 18.766 -6.002 1.00 58.27 C ANISOU 882 CA PRO A 116 6279 7131 8731 -336 -506 167 C ATOM 883 C PRO A 116 -10.910 18.486 -6.313 1.00 57.70 C ANISOU 883 C PRO A 116 6315 7015 8593 -337 -519 45 C ATOM 884 O PRO A 116 -10.045 18.872 -5.525 1.00 57.40 O ANISOU 884 O PRO A 116 6338 7023 8448 -266 -455 66 O ATOM 885 CB PRO A 116 -12.640 20.262 -6.176 1.00 59.32 C ANISOU 885 CB PRO A 116 6454 7372 8712 -279 -502 147 C ATOM 886 CG PRO A 116 -13.534 20.602 -5.038 1.00 65.53 C ANISOU 886 CG PRO A 116 7154 8222 9522 -211 -404 298 C ATOM 887 CD PRO A 116 -13.114 19.734 -3.894 1.00 60.10 C ANISOU 887 CD PRO A 116 6449 7515 8872 -191 -320 397 C ATOM 888 N ILE A 117 -10.651 17.815 -7.430 1.00 54.90 N ANISOU 888 N ILE A 117 5979 6578 8303 -417 -600 -87 N ATOM 889 CA ILE A 117 -9.292 17.475 -7.812 1.00 51.57 C ANISOU 889 CA ILE A 117 5643 6110 7841 -415 -600 -215 C ATOM 890 C ILE A 117 -9.082 17.728 -9.294 1.00 51.44 C ANISOU 890 C ILE A 117 5694 6105 7745 -479 -678 -394 C ATOM 891 O ILE A 117 -9.966 17.474 -10.111 1.00 60.87 O ANISOU 891 O ILE A 117 6851 7282 8997 -555 -759 -436 O ATOM 892 CB ILE A 117 -8.971 16.008 -7.489 1.00 59.54 C ANISOU 892 CB ILE A 117 6600 6976 9047 -438 -590 -194 C ATOM 893 CG1 ILE A 117 -9.305 15.698 -6.027 1.00 59.62 C ANISOU 893 CG1 ILE A 117 6537 6988 9130 -386 -516 17 C ATOM 894 CG2 ILE A 117 -7.512 15.696 -7.787 1.00 62.71 C ANISOU 894 CG2 ILE A 117 7075 7332 9421 -415 -575 -319 C ATOM 895 CD1 ILE A 117 -9.097 14.252 -5.645 1.00 65.16 C ANISOU 895 CD1 ILE A 117 7175 7534 10050 -410 -509 81 C ATOM 896 N VAL A 118 -7.913 18.259 -9.630 1.00 46.08 N ANISOU 896 N VAL A 118 5112 5468 6926 -451 -655 -493 N ATOM 897 CA VAL A 118 -7.549 18.472 -11.018 1.00 47.63 C ANISOU 897 CA VAL A 118 5383 5693 7023 -509 -708 -659 C ATOM 898 C VAL A 118 -6.312 17.644 -11.277 1.00 47.68 C ANISOU 898 C VAL A 118 5422 5624 7072 -509 -671 -785 C ATOM 899 O VAL A 118 -5.397 17.620 -10.464 1.00 39.28 O ANISOU 899 O VAL A 118 4361 4548 6016 -442 -604 -743 O ATOM 900 CB VAL A 118 -7.248 19.956 -11.341 1.00 52.25 C ANISOU 900 CB VAL A 118 6049 6403 7402 -483 -703 -663 C ATOM 901 CG1 VAL A 118 -7.000 20.132 -12.837 1.00 53.85 C ANISOU 901 CG1 VAL A 118 6323 6649 7487 -555 -760 -810 C ATOM 902 CG2 VAL A 118 -8.378 20.849 -10.881 1.00 42.45 C ANISOU 902 CG2 VAL A 118 4768 5221 6142 -453 -721 -528 C ATOM 903 N LEU A 119 -6.318 16.941 -12.402 1.00 48.85 N ANISOU 903 N LEU A 119 5587 5722 7252 -583 -718 -944 N ATOM 904 CA LEU A 119 -5.191 16.142 -12.829 1.00 56.63 C ANISOU 904 CA LEU A 119 6600 6631 8285 -581 -676 -1097 C ATOM 905 C LEU A 119 -4.409 16.955 -13.852 1.00 59.20 C ANISOU 905 C LEU A 119 7023 7075 8397 -596 -658 -1227 C ATOM 906 O LEU A 119 -5.002 17.551 -14.752 1.00 64.75 O ANISOU 906 O LEU A 119 7772 7870 8962 -657 -720 -1266 O ATOM 907 CB LEU A 119 -5.680 14.828 -13.444 1.00 53.98 C ANISOU 907 CB LEU A 119 6229 6159 8122 -655 -728 -1216 C ATOM 908 CG LEU A 119 -4.592 13.921 -14.032 1.00 66.00 C ANISOU 908 CG LEU A 119 7779 7584 9714 -650 -680 -1412 C ATOM 909 CD1 LEU A 119 -3.593 13.480 -12.959 1.00 67.20 C ANISOU 909 CD1 LEU A 119 7885 7648 10000 -552 -594 -1327 C ATOM 910 CD2 LEU A 119 -5.185 12.707 -14.744 1.00 66.68 C ANISOU 910 CD2 LEU A 119 7843 7530 9964 -735 -744 -1560 C ATOM 911 N CYS A 120 -3.084 16.973 -13.716 1.00 52.00 N ANISOU 911 N CYS A 120 6133 6163 7461 -543 -574 -1279 N ATOM 912 CA CYS A 120 -2.242 17.786 -14.587 1.00 49.84 C ANISOU 912 CA CYS A 120 5939 6007 6992 -557 -535 -1379 C ATOM 913 C CYS A 120 -1.091 17.053 -15.243 1.00 55.77 C ANISOU 913 C CYS A 120 6702 6717 7771 -552 -461 -1562 C ATOM 914 O CYS A 120 -0.297 16.380 -14.584 1.00 55.78 O ANISOU 914 O CYS A 120 6647 6622 7923 -487 -403 -1560 O ATOM 915 CB CYS A 120 -1.670 18.967 -13.815 1.00 55.30 C ANISOU 915 CB CYS A 120 6644 6782 7585 -499 -493 -1251 C ATOM 916 SG CYS A 120 -2.778 20.341 -13.703 1.00 54.46 S ANISOU 916 SG CYS A 120 6570 6779 7345 -515 -559 -1110 S ATOM 917 N GLY A 121 -0.998 17.218 -16.554 1.00 54.15 N ANISOU 917 N GLY A 121 6568 6594 7412 -617 -461 -1714 N ATOM 918 CA GLY A 121 0.133 16.726 -17.298 1.00 51.42 C ANISOU 918 CA GLY A 121 6241 6246 7048 -611 -367 -1902 C ATOM 919 C GLY A 121 1.143 17.831 -17.517 1.00 53.51 C ANISOU 919 C GLY A 121 6544 6651 7138 -597 -287 -1878 C ATOM 920 O GLY A 121 0.974 18.664 -18.404 1.00 67.21 O ANISOU 920 O GLY A 121 8355 8525 8657 -659 -301 -1894 O ATOM 921 N ASN A 122 2.196 17.832 -16.705 1.00 53.89 N ANISOU 921 N ASN A 122 6531 6662 7284 -520 -212 -1828 N ATOM 922 CA ASN A 122 3.257 18.829 -16.805 1.00 60.46 C ANISOU 922 CA ASN A 122 7375 7609 7988 -509 -135 -1800 C ATOM 923 C ASN A 122 4.271 18.514 -17.907 1.00 63.00 C ANISOU 923 C ASN A 122 7710 7984 8244 -525 -20 -1990 C ATOM 924 O ASN A 122 4.299 17.403 -18.428 1.00 64.33 O ANISOU 924 O ASN A 122 7869 8075 8499 -521 10 -2159 O ATOM 925 CB ASN A 122 3.985 18.969 -15.461 1.00 61.16 C ANISOU 925 CB ASN A 122 7382 7649 8208 -428 -115 -1670 C ATOM 926 CG ASN A 122 4.868 20.208 -15.402 1.00 68.30 C ANISOU 926 CG ASN A 122 8295 8669 8986 -434 -69 -1607 C ATOM 927 OD1 ASN A 122 4.719 21.129 -16.209 1.00 72.51 O ANISOU 927 OD1 ASN A 122 8902 9313 9334 -500 -64 -1609 O ATOM 928 ND2 ASN A 122 5.785 20.241 -14.438 1.00 59.82 N ANISOU 928 ND2 ASN A 122 7144 7568 8018 -372 -43 -1540 N ATOM 929 N LYS A 123 5.084 19.510 -18.259 1.00 61.31 N ANISOU 929 N LYS A 123 7515 7899 7882 -544 50 -1964 N ATOM 930 CA LYS A 123 6.199 19.360 -19.200 1.00 59.20 C ANISOU 930 CA LYS A 123 7242 7706 7545 -553 188 -2118 C ATOM 931 C LYS A 123 5.793 19.175 -20.662 1.00 64.68 C ANISOU 931 C LYS A 123 8033 8497 8045 -632 209 -2282 C ATOM 932 O LYS A 123 6.518 18.550 -21.432 1.00 69.56 O ANISOU 932 O LYS A 123 8643 9137 8648 -625 327 -2470 O ATOM 933 CB LYS A 123 7.146 18.239 -18.752 1.00 63.07 C ANISOU 933 CB LYS A 123 7620 8071 8271 -461 272 -2216 C ATOM 934 CG LYS A 123 7.975 18.605 -17.523 1.00 62.45 C ANISOU 934 CG LYS A 123 7440 7960 8329 -392 278 -2064 C ATOM 935 CD LYS A 123 8.890 17.488 -17.081 1.00 59.00 C ANISOU 935 CD LYS A 123 6880 7398 8139 -295 345 -2136 C ATOM 936 CE LYS A 123 9.090 17.537 -15.582 1.00 72.97 C ANISOU 936 CE LYS A 123 8563 9093 10068 -227 269 -1950 C ATOM 937 NZ LYS A 123 10.158 16.609 -15.143 1.00 63.67 N ANISOU 937 NZ LYS A 123 7249 7814 9129 -128 330 -1987 N ATOM 938 N VAL A 124 4.652 19.743 -21.049 1.00 67.04 N ANISOU 938 N VAL A 124 8420 8863 8188 -705 96 -2212 N ATOM 939 CA VAL A 124 4.155 19.581 -22.414 1.00 67.92 C ANISOU 939 CA VAL A 124 8631 9084 8092 -789 83 -2354 C ATOM 940 C VAL A 124 5.000 20.348 -23.411 1.00 69.22 C ANISOU 940 C VAL A 124 8847 9435 8019 -838 201 -2383 C ATOM 941 O VAL A 124 4.770 20.271 -24.617 1.00 61.40 O ANISOU 941 O VAL A 124 7944 8571 6814 -910 213 -2503 O ATOM 942 CB VAL A 124 2.691 20.043 -22.562 1.00 67.18 C ANISOU 942 CB VAL A 124 8602 9023 7899 -854 -87 -2246 C ATOM 943 CG1 VAL A 124 1.752 19.126 -21.785 1.00 61.17 C ANISOU 943 CG1 VAL A 124 7790 8091 7362 -824 -194 -2243 C ATOM 944 CG2 VAL A 124 2.544 21.477 -22.102 1.00 64.21 C ANISOU 944 CG2 VAL A 124 8237 8714 7446 -860 -129 -2007 C ATOM 945 N ASP A 125 5.977 21.091 -22.899 1.00 77.04 N ANISOU 945 N ASP A 125 9778 10448 9044 -806 286 -2268 N ATOM 946 CA ASP A 125 6.842 21.917 -23.738 1.00 74.46 C ANISOU 946 CA ASP A 125 9481 10293 8516 -858 409 -2256 C ATOM 947 C ASP A 125 7.821 21.050 -24.516 1.00 78.50 C ANISOU 947 C ASP A 125 9967 10850 9010 -840 583 -2488 C ATOM 948 O ASP A 125 8.201 21.383 -25.643 1.00 79.68 O ANISOU 948 O ASP A 125 10177 11174 8925 -904 684 -2552 O ATOM 949 CB ASP A 125 7.581 22.982 -22.908 1.00 67.17 C ANISOU 949 CB ASP A 125 8492 9366 7664 -840 437 -2064 C ATOM 950 CG ASP A 125 8.350 22.394 -21.729 1.00 73.44 C ANISOU 950 CG ASP A 125 9154 10017 8734 -741 473 -2074 C ATOM 951 OD1 ASP A 125 7.751 22.229 -20.646 1.00 65.85 O ANISOU 951 OD1 ASP A 125 8165 8928 7927 -692 359 -1987 O ATOM 952 OD2 ASP A 125 9.567 22.129 -21.880 1.00 83.42 O ANISOU 952 OD2 ASP A 125 10335 11305 10055 -711 618 -2156 O ATOM 953 N ILE A 126 8.200 19.928 -23.906 1.00 72.77 N ANISOU 953 N ILE A 126 9148 9965 8535 -749 620 -2609 N ATOM 954 CA ILE A 126 9.138 18.977 -24.496 1.00 71.63 C ANISOU 954 CA ILE A 126 8956 9820 8441 -704 790 -2845 C ATOM 955 C ILE A 126 8.552 18.281 -25.722 1.00 90.03 C ANISOU 955 C ILE A 126 11399 12215 10594 -759 799 -3077 C ATOM 956 O ILE A 126 7.394 17.850 -25.719 1.00 94.23 O ANISOU 956 O ILE A 126 11995 12676 11134 -790 648 -3106 O ATOM 957 CB ILE A 126 9.566 17.919 -23.460 1.00 68.54 C ANISOU 957 CB ILE A 126 8434 9210 8397 -584 801 -2894 C ATOM 958 CG1 ILE A 126 10.318 18.589 -22.311 1.00 67.57 C ANISOU 958 CG1 ILE A 126 8196 9054 8423 -533 801 -2686 C ATOM 959 CG2 ILE A 126 10.419 16.841 -24.104 1.00 63.38 C ANISOU 959 CG2 ILE A 126 7730 8526 7826 -525 973 -3158 C ATOM 960 CD1 ILE A 126 10.492 17.717 -21.102 1.00 70.86 C ANISOU 960 CD1 ILE A 126 8496 9266 9160 -425 754 -2657 C ATOM 961 N LYS A 127 9.361 18.165 -26.768 1.00101.71 N ANISOU 961 N LYS A 127 12897 13836 11912 -776 977 -3247 N ATOM 962 CA LYS A 127 8.898 17.581 -28.022 1.00113.51 C ANISOU 962 CA LYS A 127 14512 15429 13188 -837 998 -3488 C ATOM 963 C LYS A 127 8.583 16.088 -27.932 1.00115.83 C ANISOU 963 C LYS A 127 14789 15522 13697 -779 975 -3739 C ATOM 964 O LYS A 127 7.460 15.672 -28.231 1.00117.88 O ANISOU 964 O LYS A 127 15140 15748 13902 -839 826 -3816 O ATOM 965 CB LYS A 127 9.889 17.866 -29.147 1.00120.08 C ANISOU 965 CB LYS A 127 15369 16482 13774 -868 1217 -3607 C ATOM 966 CG LYS A 127 9.923 19.331 -29.514 1.00127.43 C ANISOU 966 CG LYS A 127 16355 17626 14436 -962 1212 -3364 C ATOM 967 CD LYS A 127 10.282 19.544 -30.972 1.00135.51 C ANISOU 967 CD LYS A 127 17477 18915 15094 -1042 1363 -3491 C ATOM 968 CE LYS A 127 9.910 20.949 -31.435 1.00137.43 C ANISOU 968 CE LYS A 127 17812 19358 15046 -1158 1294 -3227 C ATOM 969 NZ LYS A 127 10.619 21.326 -32.692 1.00140.36 N ANISOU 969 NZ LYS A 127 18242 20003 15087 -1227 1492 -3285 N ATOM 970 N ASP A 128 9.563 15.285 -27.526 1.00113.78 N ANISOU 970 N ASP A 128 14407 15123 13700 -665 1116 -3861 N ATOM 971 CA ASP A 128 9.322 13.854 -27.385 1.00114.93 C ANISOU 971 CA ASP A 128 14528 15044 14097 -602 1100 -4087 C ATOM 972 C ASP A 128 8.486 13.543 -26.151 1.00100.69 C ANISOU 972 C ASP A 128 12674 13016 12567 -573 904 -3916 C ATOM 973 O ASP A 128 9.010 13.268 -25.071 1.00 96.51 O ANISOU 973 O ASP A 128 12014 12325 12332 -472 918 -3805 O ATOM 974 CB ASP A 128 10.619 13.047 -27.366 1.00125.48 C ANISOU 974 CB ASP A 128 15739 16285 15652 -477 1313 -4270 C ATOM 975 CG ASP A 128 10.365 11.552 -27.494 1.00136.10 C ANISOU 975 CG ASP A 128 17081 17402 17227 -421 1314 -4551 C ATOM 976 OD1 ASP A 128 10.438 11.025 -28.624 1.00138.91 O ANISOU 976 OD1 ASP A 128 17521 17827 17429 -448 1419 -4855 O ATOM 977 OD2 ASP A 128 10.059 10.905 -26.470 1.00140.39 O ANISOU 977 OD2 ASP A 128 17546 17696 18102 -357 1206 -4469 O ATOM 978 N ARG A 129 7.174 13.584 -26.336 1.00 90.08 N ANISOU 978 N ARG A 129 11432 11676 11118 -666 723 -3891 N ATOM 979 CA ARG A 129 6.232 13.274 -25.280 1.00 85.69 C ANISOU 979 CA ARG A 129 10836 10928 10795 -655 543 -3737 C ATOM 980 C ARG A 129 5.946 11.774 -25.289 1.00 89.22 C ANISOU 980 C ARG A 129 11262 11139 11500 -622 525 -3965 C ATOM 981 O ARG A 129 5.969 11.139 -26.342 1.00 85.58 O ANISOU 981 O ARG A 129 10873 10702 10943 -657 584 -4256 O ATOM 982 CB ARG A 129 4.946 14.070 -25.498 1.00 79.22 C ANISOU 982 CB ARG A 129 10115 10229 9755 -771 360 -3592 C ATOM 983 CG ARG A 129 3.792 13.690 -24.603 1.00 77.75 C ANISOU 983 CG ARG A 129 9895 9867 9778 -778 177 -3463 C ATOM 984 CD ARG A 129 2.557 14.476 -24.991 1.00 86.16 C ANISOU 984 CD ARG A 129 11047 11070 10618 -890 10 -3345 C ATOM 985 NE ARG A 129 1.485 14.359 -24.004 1.00 92.65 N ANISOU 985 NE ARG A 129 11815 11753 11634 -891 -149 -3166 N ATOM 986 CZ ARG A 129 0.541 15.279 -23.812 1.00 87.74 C ANISOU 986 CZ ARG A 129 11215 11222 10899 -942 -281 -2958 C ATOM 987 NH1 ARG A 129 0.538 16.392 -24.530 1.00 78.75 N ANISOU 987 NH1 ARG A 129 10156 10300 9464 -997 -287 -2890 N ATOM 988 NH2 ARG A 129 -0.395 15.095 -22.890 1.00 84.70 N ANISOU 988 NH2 ARG A 129 10766 10709 10706 -935 -400 -2806 N ATOM 989 N LYS A 130 5.682 11.212 -24.114 1.00 91.74 N ANISOU 989 N LYS A 130 11484 11230 12144 -559 445 -3834 N ATOM 990 CA LYS A 130 5.439 9.779 -23.997 1.00 93.46 C ANISOU 990 CA LYS A 130 11665 11185 12659 -524 426 -4014 C ATOM 991 C LYS A 130 3.978 9.467 -23.685 1.00 91.04 C ANISOU 991 C LYS A 130 11390 10772 12432 -609 221 -3937 C ATOM 992 O LYS A 130 3.418 8.515 -24.230 1.00 98.59 O ANISOU 992 O LYS A 130 12386 11603 13472 -660 172 -4159 O ATOM 993 CB LYS A 130 6.352 9.155 -22.936 1.00 97.93 C ANISOU 993 CB LYS A 130 12081 11544 13585 -379 506 -3933 C ATOM 994 CG LYS A 130 7.852 9.341 -23.185 1.00103.81 C ANISOU 994 CG LYS A 130 12759 12370 14312 -284 711 -4012 C ATOM 995 CD LYS A 130 8.312 8.709 -24.500 1.00104.88 C ANISOU 995 CD LYS A 130 12954 12535 14360 -286 860 -4383 C ATOM 996 CE LYS A 130 9.792 8.345 -24.456 1.00101.93 C ANISOU 996 CE LYS A 130 12455 12115 14159 -147 1069 -4479 C ATOM 997 NZ LYS A 130 10.590 9.291 -23.625 1.00 98.71 N ANISOU 997 NZ LYS A 130 11939 11811 13754 -93 1101 -4195 N ATOM 998 N VAL A 131 3.367 10.264 -22.809 1.00 83.47 N ANISOU 998 N VAL A 131 10404 9858 11454 -626 108 -3632 N ATOM 999 CA VAL A 131 1.972 10.048 -22.419 1.00 75.41 C ANISOU 999 CA VAL A 131 9387 8747 10517 -702 -75 -3525 C ATOM 1000 C VAL A 131 1.025 10.946 -23.204 1.00 78.92 C ANISOU 1000 C VAL A 131 9936 9411 10638 -826 -189 -3500 C ATOM 1001 O VAL A 131 0.673 12.029 -22.747 1.00 83.72 O ANISOU 1001 O VAL A 131 10543 10145 11122 -837 -247 -3255 O ATOM 1002 CB VAL A 131 1.738 10.295 -20.914 1.00 64.46 C ANISOU 1002 CB VAL A 131 7899 7268 9324 -641 -132 -3203 C ATOM 1003 CG1 VAL A 131 0.382 9.743 -20.497 1.00 56.59 C ANISOU 1003 CG1 VAL A 131 6879 6133 8491 -708 -288 -3124 C ATOM 1004 CG2 VAL A 131 2.833 9.665 -20.083 1.00 58.26 C ANISOU 1004 CG2 VAL A 131 7007 6319 8812 -509 -23 -3170 C ATOM 1005 N LYS A 132 0.609 10.490 -24.381 1.00 83.27 N ANISOU 1005 N LYS A 132 10578 10006 11057 -918 -228 -3757 N ATOM 1006 CA LYS A 132 -0.262 11.276 -25.245 1.00 94.82 C ANISOU 1006 CA LYS A 132 12140 11689 12199 -1040 -349 -3745 C ATOM 1007 C LYS A 132 -1.656 11.433 -24.635 1.00 97.53 C ANISOU 1007 C LYS A 132 12440 11979 12638 -1100 -544 -3539 C ATOM 1008 O LYS A 132 -1.956 10.847 -23.598 1.00 96.44 O ANISOU 1008 O LYS A 132 12203 11633 12807 -1057 -575 -3427 O ATOM 1009 CB LYS A 132 -0.347 10.632 -26.628 1.00101.63 C ANISOU 1009 CB LYS A 132 13108 12609 12897 -1126 -351 -4092 C ATOM 1010 CG LYS A 132 1.004 10.317 -27.250 1.00107.15 C ANISOU 1010 CG LYS A 132 13840 13345 13527 -1060 -136 -4332 C ATOM 1011 CD LYS A 132 1.678 11.573 -27.769 1.00112.29 C ANISOU 1011 CD LYS A 132 14550 14284 13831 -1060 -36 -4236 C ATOM 1012 CE LYS A 132 0.743 12.343 -28.687 1.00114.69 C ANISOU 1012 CE LYS A 132 14969 14827 13780 -1195 -182 -4201 C ATOM 1013 NZ LYS A 132 1.467 13.344 -29.510 1.00113.02 N ANISOU 1013 NZ LYS A 132 14839 14898 13207 -1213 -65 -4181 N ATOM 1014 N ALA A 133 -2.503 12.223 -25.288 1.00 98.18 N ANISOU 1014 N ALA A 133 12590 12255 12461 -1199 -672 -3479 N ATOM 1015 CA ALA A 133 -3.843 12.515 -24.780 1.00 92.42 C ANISOU 1015 CA ALA A 133 11806 11506 11804 -1253 -851 -3271 C ATOM 1016 C ALA A 133 -4.706 11.263 -24.689 1.00 96.42 C ANISOU 1016 C ALA A 133 12259 11804 12571 -1316 -964 -3393 C ATOM 1017 O ALA A 133 -5.505 11.105 -23.762 1.00 95.50 O ANISOU 1017 O ALA A 133 12042 11563 12681 -1314 -1046 -3206 O ATOM 1018 CB ALA A 133 -4.519 13.553 -25.656 1.00 87.03 C ANISOU 1018 CB ALA A 133 11203 11074 10792 -1344 -969 -3205 C ATOM 1019 N LYS A 134 -4.538 10.378 -25.663 1.00 98.16 N ANISOU 1019 N LYS A 134 12548 11989 12760 -1377 -962 -3713 N ATOM 1020 CA LYS A 134 -5.303 9.143 -25.725 1.00106.20 C ANISOU 1020 CA LYS A 134 13527 12796 14028 -1455 -1073 -3873 C ATOM 1021 C LYS A 134 -5.055 8.247 -24.511 1.00 98.66 C ANISOU 1021 C LYS A 134 12452 11542 13492 -1367 -1004 -3792 C ATOM 1022 O LYS A 134 -5.943 7.506 -24.088 1.00 91.55 O ANISOU 1022 O LYS A 134 11473 10457 12855 -1424 -1115 -3758 O ATOM 1023 CB LYS A 134 -4.976 8.393 -27.016 1.00117.70 C ANISOU 1023 CB LYS A 134 15095 14271 15355 -1523 -1056 -4270 C ATOM 1024 CG LYS A 134 -5.267 9.193 -28.276 1.00125.07 C ANISOU 1024 CG LYS A 134 16155 15515 15850 -1624 -1138 -4353 C ATOM 1025 CD LYS A 134 -5.155 8.322 -29.514 1.00130.71 C ANISOU 1025 CD LYS A 134 16980 16241 16444 -1712 -1149 -4765 C ATOM 1026 CE LYS A 134 -5.815 8.980 -30.718 1.00134.42 C ANISOU 1026 CE LYS A 134 17563 17011 16499 -1846 -1302 -4824 C ATOM 1027 NZ LYS A 134 -6.031 8.007 -31.832 1.00138.45 N ANISOU 1027 NZ LYS A 134 18172 17511 16921 -1961 -1374 -5232 N ATOM 1028 N SER A 135 -3.849 8.317 -23.952 1.00 89.31 N ANISOU 1028 N SER A 135 11246 10314 12372 -1232 -825 -3745 N ATOM 1029 CA SER A 135 -3.502 7.517 -22.779 1.00 82.12 C ANISOU 1029 CA SER A 135 10223 9137 11840 -1137 -759 -3641 C ATOM 1030 C SER A 135 -4.112 8.082 -21.501 1.00 82.26 C ANISOU 1030 C SER A 135 10142 9149 11963 -1105 -813 -3271 C ATOM 1031 O SER A 135 -4.333 7.353 -20.536 1.00 84.80 O ANISOU 1031 O SER A 135 10364 9254 12601 -1073 -820 -3148 O ATOM 1032 CB SER A 135 -1.986 7.418 -22.614 1.00 81.33 C ANISOU 1032 CB SER A 135 10121 9007 11775 -1000 -561 -3708 C ATOM 1033 OG SER A 135 -1.359 7.079 -23.833 1.00 89.51 O ANISOU 1033 OG SER A 135 11251 10097 12662 -1019 -481 -4046 O ATOM 1034 N ILE A 136 -4.374 9.385 -21.490 1.00 78.72 N ANISOU 1034 N ILE A 136 9723 8935 11250 -1112 -844 -3093 N ATOM 1035 CA ILE A 136 -4.911 10.039 -20.303 1.00 75.22 C ANISOU 1035 CA ILE A 136 9197 8509 10873 -1072 -877 -2762 C ATOM 1036 C ILE A 136 -6.398 9.740 -20.151 1.00 81.56 C ANISOU 1036 C ILE A 136 9934 9251 11802 -1173 -1037 -2675 C ATOM 1037 O ILE A 136 -7.218 10.206 -20.940 1.00 88.14 O ANISOU 1037 O ILE A 136 10807 10227 12457 -1270 -1158 -2713 O ATOM 1038 CB ILE A 136 -4.666 11.552 -20.344 1.00 68.67 C ANISOU 1038 CB ILE A 136 8419 7929 9743 -1039 -850 -2614 C ATOM 1039 CG1 ILE A 136 -3.305 11.831 -20.976 1.00 74.42 C ANISOU 1039 CG1 ILE A 136 9228 8754 10296 -988 -712 -2768 C ATOM 1040 CG2 ILE A 136 -4.747 12.141 -18.946 1.00 68.43 C ANISOU 1040 CG2 ILE A 136 8308 7886 9805 -955 -823 -2313 C ATOM 1041 CD1 ILE A 136 -2.857 13.260 -20.882 1.00 66.40 C ANISOU 1041 CD1 ILE A 136 8249 7943 9035 -948 -664 -2609 C ATOM 1042 N VAL A 137 -6.735 8.966 -19.124 1.00 80.82 N ANISOU 1042 N VAL A 137 9732 8952 12024 -1150 -1039 -2543 N ATOM 1043 CA VAL A 137 -8.064 8.374 -19.012 1.00 88.20 C ANISOU 1043 CA VAL A 137 10584 9779 13150 -1257 -1176 -2493 C ATOM 1044 C VAL A 137 -8.551 8.341 -17.564 1.00 84.63 C ANISOU 1044 C VAL A 137 10006 9238 12913 -1207 -1156 -2180 C ATOM 1045 O VAL A 137 -9.749 8.251 -17.307 1.00 79.09 O ANISOU 1045 O VAL A 137 9217 8515 12319 -1283 -1256 -2056 O ATOM 1046 CB VAL A 137 -8.083 6.935 -19.625 1.00 82.51 C ANISOU 1046 CB VAL A 137 9865 8828 12655 -1334 -1214 -2765 C ATOM 1047 CG1 VAL A 137 -9.247 6.123 -19.093 1.00 87.37 C ANISOU 1047 CG1 VAL A 137 10358 9256 13583 -1422 -1320 -2655 C ATOM 1048 CG2 VAL A 137 -8.125 6.994 -21.152 1.00 81.61 C ANISOU 1048 CG2 VAL A 137 9870 8839 12299 -1431 -1286 -3073 C ATOM 1049 N PHE A 138 -7.622 8.435 -16.618 1.00 86.67 N ANISOU 1049 N PHE A 138 10249 9461 13221 -1080 -1028 -2048 N ATOM 1050 CA PHE A 138 -7.979 8.343 -15.206 1.00 88.57 C ANISOU 1050 CA PHE A 138 10380 9628 13643 -1027 -997 -1755 C ATOM 1051 C PHE A 138 -9.120 9.299 -14.838 1.00 93.01 C ANISOU 1051 C PHE A 138 10895 10352 14093 -1058 -1059 -1548 C ATOM 1052 O PHE A 138 -10.043 8.929 -14.104 1.00 98.36 O ANISOU 1052 O PHE A 138 11462 10951 14960 -1090 -1090 -1369 O ATOM 1053 CB PHE A 138 -6.757 8.583 -14.310 1.00 79.92 C ANISOU 1053 CB PHE A 138 9293 8540 12533 -884 -865 -1642 C ATOM 1054 CG PHE A 138 -7.024 8.338 -12.854 1.00 73.15 C ANISOU 1054 CG PHE A 138 8334 7606 11856 -831 -830 -1353 C ATOM 1055 CD1 PHE A 138 -7.239 7.057 -12.387 1.00 71.89 C ANISOU 1055 CD1 PHE A 138 8089 7205 12021 -852 -837 -1301 C ATOM 1056 CD2 PHE A 138 -7.087 9.386 -11.958 1.00 68.69 C ANISOU 1056 CD2 PHE A 138 7760 7208 11132 -763 -790 -1133 C ATOM 1057 CE1 PHE A 138 -7.499 6.821 -11.048 1.00 69.23 C ANISOU 1057 CE1 PHE A 138 7659 6812 11831 -808 -801 -1014 C ATOM 1058 CE2 PHE A 138 -7.341 9.161 -10.619 1.00 65.43 C ANISOU 1058 CE2 PHE A 138 7261 6748 10852 -716 -752 -872 C ATOM 1059 CZ PHE A 138 -7.548 7.870 -10.165 1.00 72.83 C ANISOU 1059 CZ PHE A 138 8113 7461 12097 -739 -756 -802 C ATOM 1060 N HIS A 139 -9.059 10.517 -15.372 1.00 87.34 N ANISOU 1060 N HIS A 139 10253 9853 13078 -1046 -1072 -1569 N ATOM 1061 CA HIS A 139 -10.042 11.555 -15.075 1.00 89.95 C ANISOU 1061 CA HIS A 139 10543 10341 13295 -1054 -1122 -1383 C ATOM 1062 C HIS A 139 -11.419 11.288 -15.695 1.00106.62 C ANISOU 1062 C HIS A 139 12586 12446 15478 -1183 -1271 -1408 C ATOM 1063 O HIS A 139 -12.414 11.909 -15.295 1.00115.08 O ANISOU 1063 O HIS A 139 13578 13604 16544 -1190 -1313 -1228 O ATOM 1064 CB HIS A 139 -9.524 12.917 -15.539 1.00 79.76 C ANISOU 1064 CB HIS A 139 9354 9260 11689 -1006 -1099 -1401 C ATOM 1065 CG HIS A 139 -9.576 13.093 -17.034 1.00 78.99 C ANISOU 1065 CG HIS A 139 9346 9258 11408 -1094 -1188 -1615 C ATOM 1066 ND1 HIS A 139 -8.819 12.355 -17.882 1.00 82.14 N ANISOU 1066 ND1 HIS A 139 9818 9595 11794 -1127 -1172 -1862 N ATOM 1067 CD2 HIS A 139 -10.334 13.941 -17.785 1.00 81.20 C ANISOU 1067 CD2 HIS A 139 9648 9698 11506 -1151 -1295 -1602 C ATOM 1068 CE1 HIS A 139 -9.089 12.736 -19.145 1.00 89.78 C ANISOU 1068 CE1 HIS A 139 10864 10699 12549 -1210 -1264 -2008 C ATOM 1069 NE2 HIS A 139 -9.984 13.673 -19.098 1.00 89.71 N ANISOU 1069 NE2 HIS A 139 10823 10821 12440 -1226 -1345 -1844 N ATOM 1070 N ARG A 140 -11.478 10.390 -16.679 1.00113.16 N ANISOU 1070 N ARG A 140 13442 13178 16376 -1285 -1353 -1641 N ATOM 1071 CA ARG A 140 -12.764 9.990 -17.250 1.00119.47 C ANISOU 1071 CA ARG A 140 14166 13953 17274 -1424 -1512 -1679 C ATOM 1072 C ARG A 140 -13.747 9.724 -16.121 1.00118.52 C ANISOU 1072 C ARG A 140 13881 13747 17403 -1430 -1511 -1422 C ATOM 1073 O ARG A 140 -14.866 10.221 -16.131 1.00110.67 O ANISOU 1073 O ARG A 140 12798 12848 16402 -1478 -1599 -1300 O ATOM 1074 CB ARG A 140 -12.619 8.747 -18.134 1.00123.34 C ANISOU 1074 CB ARG A 140 14691 14277 17894 -1528 -1580 -1962 C ATOM 1075 CG ARG A 140 -12.615 9.034 -19.619 1.00126.52 C ANISOU 1075 CG ARG A 140 15209 14824 18040 -1613 -1688 -2215 C ATOM 1076 CD ARG A 140 -12.176 10.459 -19.883 1.00130.54 C ANISOU 1076 CD ARG A 140 15809 15587 18204 -1536 -1647 -2145 C ATOM 1077 NE ARG A 140 -11.161 10.516 -20.927 1.00138.21 N ANISOU 1077 NE ARG A 140 16933 16637 18943 -1534 -1607 -2398 N ATOM 1078 CZ ARG A 140 -11.421 10.447 -22.227 1.00143.61 C ANISOU 1078 CZ ARG A 140 17697 17422 19448 -1644 -1726 -2615 C ATOM 1079 NH1 ARG A 140 -12.674 10.320 -22.649 1.00145.06 N ANISOU 1079 NH1 ARG A 140 17815 17633 19669 -1768 -1913 -2609 N ATOM 1080 NH2 ARG A 140 -10.427 10.506 -23.103 1.00142.77 N ANISOU 1080 NH2 ARG A 140 17729 17398 19117 -1631 -1658 -2835 N ATOM 1081 N LYS A 141 -13.299 8.943 -15.145 1.00125.16 N ANISOU 1081 N LYS A 141 14676 14414 18465 -1377 -1406 -1331 N ATOM 1082 CA LYS A 141 -14.085 8.658 -13.967 1.00131.75 C ANISOU 1082 CA LYS A 141 15361 15174 19523 -1373 -1372 -1065 C ATOM 1083 C LYS A 141 -14.147 9.876 -13.053 1.00132.27 C ANISOU 1083 C LYS A 141 15412 15424 19420 -1256 -1280 -830 C ATOM 1084 O LYS A 141 -13.330 10.788 -13.121 1.00119.22 O ANISOU 1084 O LYS A 141 13868 13906 17523 -1163 -1220 -861 O ATOM 1085 CB LYS A 141 -13.497 7.476 -13.194 1.00135.25 C ANISOU 1085 CB LYS A 141 15771 15383 20236 -1344 -1285 -1019 C ATOM 1086 CG LYS A 141 -13.588 6.136 -13.916 1.00139.84 C ANISOU 1086 CG LYS A 141 16340 15727 21066 -1462 -1370 -1229 C ATOM 1087 CD LYS A 141 -12.239 5.680 -14.444 1.00138.50 C ANISOU 1087 CD LYS A 141 16297 15462 20863 -1407 -1315 -1470 C ATOM 1088 CE LYS A 141 -11.952 6.259 -15.812 1.00134.06 C ANISOU 1088 CE LYS A 141 15866 15056 20015 -1440 -1380 -1747 C ATOM 1089 NZ LYS A 141 -11.177 5.281 -16.624 1.00130.87 N ANISOU 1089 NZ LYS A 141 15542 14481 19703 -1466 -1377 -2054 N ATOM 1090 N LYS A 142 -15.149 9.893 -12.193 1.00145.73 N ANISOU 1090 N LYS A 142 16976 17133 21263 -1266 -1264 -599 N ATOM 1091 CA LYS A 142 -15.193 10.842 -11.066 1.00149.32 C ANISOU 1091 CA LYS A 142 17404 17726 21603 -1145 -1146 -367 C ATOM 1092 C LYS A 142 -15.410 12.314 -11.359 1.00142.90 C ANISOU 1092 C LYS A 142 16638 17132 20527 -1089 -1160 -355 C ATOM 1093 O LYS A 142 -16.291 12.678 -12.143 1.00150.20 O ANISOU 1093 O LYS A 142 17517 18128 21422 -1160 -1277 -394 O ATOM 1094 CB LYS A 142 -13.978 10.688 -10.140 1.00151.68 C ANISOU 1094 CB LYS A 142 17771 17982 21876 -1030 -1009 -304 C ATOM 1095 CG LYS A 142 -14.195 9.607 -9.061 1.00160.64 C ANISOU 1095 CG LYS A 142 18796 18958 23282 -1039 -944 -115 C ATOM 1096 CD LYS A 142 -12.996 9.277 -8.124 1.00188.62 C ANISOU 1096 CD LYS A 142 22394 22445 26830 -932 -831 -32 C ATOM 1097 CE LYS A 142 -13.455 8.064 -7.256 1.00127.40 C ANISOU 1097 CE LYS A 142 14512 14511 19382 -975 -797 167 C ATOM 1098 NZ LYS A 142 -12.464 7.466 -6.298 1.00122.41 N ANISOU 1098 NZ LYS A 142 13899 13787 18825 -890 -710 293 N ATOM 1099 N ASN A 143 -14.565 13.138 -10.747 1.00124.56 N ANISOU 1099 N ASN A 143 14402 14905 18021 -963 -1049 -302 N ATOM 1100 CA ASN A 143 -14.794 14.566 -10.615 1.00107.44 C ANISOU 1100 CA ASN A 143 12258 12917 15646 -886 -1026 -230 C ATOM 1101 C ASN A 143 -13.398 15.211 -10.804 1.00 98.63 C ANISOU 1101 C ASN A 143 11306 11861 14309 -807 -973 -341 C ATOM 1102 O ASN A 143 -12.841 15.947 -9.958 1.00 88.49 O ANISOU 1102 O ASN A 143 10065 10648 12907 -701 -871 -255 O ATOM 1103 CB ASN A 143 -15.351 14.823 -9.213 1.00104.28 C ANISOU 1103 CB ASN A 143 11757 12556 15308 -810 -910 8 C ATOM 1104 CG ASN A 143 -15.621 16.268 -8.954 1.00104.05 C ANISOU 1104 CG ASN A 143 11746 12690 15098 -718 -870 77 C ATOM 1105 OD1 ASN A 143 -16.072 17.005 -9.840 1.00103.60 O ANISOU 1105 OD1 ASN A 143 11699 12710 14955 -740 -962 16 O ATOM 1106 ND2 ASN A 143 -15.373 16.692 -7.725 1.00 97.32 N ANISOU 1106 ND2 ASN A 143 10897 11891 14188 -613 -735 207 N ATOM 1107 N LEU A 144 -12.828 14.841 -11.940 1.00 95.98 N ANISOU 1107 N LEU A 144 11054 11488 13925 -870 -1044 -546 N ATOM 1108 CA LEU A 144 -11.429 14.990 -12.239 1.00 87.01 C ANISOU 1108 CA LEU A 144 10049 10361 12649 -823 -992 -680 C ATOM 1109 C LEU A 144 -11.304 15.690 -13.572 1.00 86.90 C ANISOU 1109 C LEU A 144 10130 10458 12432 -868 -1072 -833 C ATOM 1110 O LEU A 144 -11.328 15.036 -14.623 1.00 97.28 O ANISOU 1110 O LEU A 144 11472 11730 13761 -959 -1154 -1007 O ATOM 1111 CB LEU A 144 -10.792 13.605 -12.369 1.00 72.48 C ANISOU 1111 CB LEU A 144 8212 8347 10982 -859 -981 -797 C ATOM 1112 CG LEU A 144 -10.245 12.922 -11.116 1.00 65.50 C ANISOU 1112 CG LEU A 144 7282 7351 10253 -788 -879 -669 C ATOM 1113 CD1 LEU A 144 -8.822 13.346 -10.867 1.00 71.63 C ANISOU 1113 CD1 LEU A 144 8151 8172 10892 -693 -794 -710 C ATOM 1114 CD2 LEU A 144 -11.097 13.213 -9.892 1.00 66.35 C ANISOU 1114 CD2 LEU A 144 7291 7501 10418 -750 -834 -418 C ATOM 1115 N GLN A 145 -11.185 17.014 -13.532 1.00 69.23 N ANISOU 1115 N GLN A 145 7943 8359 10003 -807 -1050 -768 N ATOM 1116 CA GLN A 145 -10.911 17.797 -14.730 1.00 61.54 C ANISOU 1116 CA GLN A 145 7070 7500 8814 -840 -1111 -880 C ATOM 1117 C GLN A 145 -9.423 17.659 -15.025 1.00 63.29 C ANISOU 1117 C GLN A 145 7400 7712 8935 -815 -1031 -1021 C ATOM 1118 O GLN A 145 -8.624 17.515 -14.103 1.00 62.00 O ANISOU 1118 O GLN A 145 7237 7498 8824 -739 -927 -977 O ATOM 1119 CB GLN A 145 -11.278 19.259 -14.489 1.00 56.93 C ANISOU 1119 CB GLN A 145 6493 7038 8099 -777 -1107 -740 C ATOM 1120 CG GLN A 145 -10.890 20.205 -15.600 1.00 67.44 C ANISOU 1120 CG GLN A 145 7932 8488 9204 -799 -1154 -810 C ATOM 1121 CD GLN A 145 -11.696 19.986 -16.857 1.00 80.46 C ANISOU 1121 CD GLN A 145 9575 10189 10808 -907 -1307 -884 C ATOM 1122 OE1 GLN A 145 -12.641 19.199 -16.869 1.00 83.40 O ANISOU 1122 OE1 GLN A 145 9848 10504 11335 -968 -1387 -880 O ATOM 1123 NE2 GLN A 145 -11.335 20.690 -17.927 1.00 86.94 N ANISOU 1123 NE2 GLN A 145 10496 11124 11413 -940 -1354 -943 N ATOM 1124 N TYR A 146 -9.046 17.674 -16.298 1.00 61.41 N ANISOU 1124 N TYR A 146 7248 7532 8552 -879 -1077 -1189 N ATOM 1125 CA TYR A 146 -7.647 17.491 -16.648 1.00 55.49 C ANISOU 1125 CA TYR A 146 6586 6779 7718 -857 -988 -1333 C ATOM 1126 C TYR A 146 -7.148 18.571 -17.596 1.00 48.04 C ANISOU 1126 C TYR A 146 5748 5993 6511 -871 -989 -1379 C ATOM 1127 O TYR A 146 -7.842 18.952 -18.532 1.00 60.03 O ANISOU 1127 O TYR A 146 7295 7607 7906 -942 -1093 -1397 O ATOM 1128 CB TYR A 146 -7.415 16.113 -17.270 1.00 62.50 C ANISOU 1128 CB TYR A 146 7477 7554 8715 -919 -1002 -1536 C ATOM 1129 CG TYR A 146 -6.059 16.019 -17.912 1.00 68.87 C ANISOU 1129 CG TYR A 146 8374 8387 9405 -902 -911 -1711 C ATOM 1130 CD1 TYR A 146 -4.940 15.710 -17.157 1.00 76.62 C ANISOU 1130 CD1 TYR A 146 9339 9289 10482 -815 -789 -1705 C ATOM 1131 CD2 TYR A 146 -5.889 16.279 -19.262 1.00 63.31 C ANISOU 1131 CD2 TYR A 146 7764 7804 8488 -971 -944 -1869 C ATOM 1132 CE1 TYR A 146 -3.702 15.641 -17.727 1.00 75.13 C ANISOU 1132 CE1 TYR A 146 9211 9128 10205 -794 -697 -1858 C ATOM 1133 CE2 TYR A 146 -4.651 16.216 -19.839 1.00 67.55 C ANISOU 1133 CE2 TYR A 146 8373 8379 8914 -953 -839 -2024 C ATOM 1134 CZ TYR A 146 -3.562 15.896 -19.065 1.00 75.14 C ANISOU 1134 CZ TYR A 146 9301 9249 9998 -863 -712 -2019 C ATOM 1135 OH TYR A 146 -2.316 15.832 -19.628 1.00 78.45 O ANISOU 1135 OH TYR A 146 9771 9709 10328 -840 -599 -2168 O ATOM 1136 N TYR A 147 -5.939 19.057 -17.355 1.00 44.02 N ANISOU 1136 N TYR A 147 5291 5515 5922 -810 -878 -1385 N ATOM 1137 CA TYR A 147 -5.308 20.024 -18.247 1.00 58.13 C ANISOU 1137 CA TYR A 147 7173 7440 7472 -830 -858 -1422 C ATOM 1138 C TYR A 147 -3.855 19.621 -18.503 1.00 65.67 C ANISOU 1138 C TYR A 147 8170 8385 8395 -811 -737 -1568 C ATOM 1139 O TYR A 147 -3.146 19.184 -17.592 1.00 51.52 O ANISOU 1139 O TYR A 147 6331 6499 6745 -741 -654 -1555 O ATOM 1140 CB TYR A 147 -5.340 21.448 -17.655 1.00 48.00 C ANISOU 1140 CB TYR A 147 5900 6224 6114 -774 -842 -1238 C ATOM 1141 CG TYR A 147 -6.710 21.967 -17.302 1.00 52.28 C ANISOU 1141 CG TYR A 147 6387 6774 6703 -769 -938 -1084 C ATOM 1142 CD1 TYR A 147 -7.587 22.398 -18.291 1.00 58.47 C ANISOU 1142 CD1 TYR A 147 7190 7648 7379 -835 -1057 -1065 C ATOM 1143 CD2 TYR A 147 -7.131 22.035 -15.981 1.00 51.95 C ANISOU 1143 CD2 TYR A 147 6267 6661 6810 -695 -909 -953 C ATOM 1144 CE1 TYR A 147 -8.841 22.866 -17.980 1.00 54.51 C ANISOU 1144 CE1 TYR A 147 6617 7152 6944 -821 -1144 -920 C ATOM 1145 CE2 TYR A 147 -8.394 22.503 -15.660 1.00 49.02 C ANISOU 1145 CE2 TYR A 147 5831 6301 6493 -681 -978 -818 C ATOM 1146 CZ TYR A 147 -9.242 22.917 -16.665 1.00 57.69 C ANISOU 1146 CZ TYR A 147 6935 7476 7509 -741 -1096 -802 C ATOM 1147 OH TYR A 147 -10.499 23.396 -16.356 1.00 68.36 O ANISOU 1147 OH TYR A 147 8202 8836 8935 -719 -1165 -661 O ATOM 1148 N ASP A 148 -3.424 19.752 -19.753 1.00 70.78 N ANISOU 1148 N ASP A 148 8900 9139 8854 -871 -726 -1702 N ATOM 1149 CA ASP A 148 -2.008 19.760 -20.058 1.00 63.84 C ANISOU 1149 CA ASP A 148 8059 8296 7904 -848 -593 -1807 C ATOM 1150 C ASP A 148 -1.472 21.040 -19.437 1.00 64.12 C ANISOU 1150 C ASP A 148 8098 8387 7879 -799 -543 -1638 C ATOM 1151 O ASP A 148 -2.146 22.068 -19.459 1.00 63.27 O ANISOU 1151 O ASP A 148 8013 8346 7679 -814 -612 -1497 O ATOM 1152 CB ASP A 148 -1.783 19.816 -21.570 1.00 64.83 C ANISOU 1152 CB ASP A 148 8277 8560 7796 -931 -588 -1961 C ATOM 1153 CG ASP A 148 -1.768 18.446 -22.224 1.00 70.45 C ANISOU 1153 CG ASP A 148 8998 9208 8564 -969 -583 -2204 C ATOM 1154 OD1 ASP A 148 -1.874 17.423 -21.508 1.00 69.22 O ANISOU 1154 OD1 ASP A 148 8769 8879 8654 -929 -581 -2246 O ATOM 1155 OD2 ASP A 148 -1.642 18.403 -23.469 1.00 71.37 O ANISOU 1155 OD2 ASP A 148 9198 9448 8473 -1040 -580 -2355 O ATOM 1156 N ILE A 149 -0.272 20.993 -18.875 1.00 60.43 N ANISOU 1156 N ILE A 149 7600 7884 7476 -739 -429 -1653 N ATOM 1157 CA ILE A 149 0.378 22.220 -18.435 1.00 62.63 C ANISOU 1157 CA ILE A 149 7890 8222 7686 -712 -382 -1525 C ATOM 1158 C ILE A 149 1.863 22.208 -18.758 1.00 65.59 C ANISOU 1158 C ILE A 149 8261 8638 8023 -703 -251 -1617 C ATOM 1159 O ILE A 149 2.448 21.157 -19.052 1.00 68.41 O ANISOU 1159 O ILE A 149 8591 8952 8450 -690 -184 -1774 O ATOM 1160 CB ILE A 149 0.203 22.478 -16.929 1.00 62.12 C ANISOU 1160 CB ILE A 149 7762 8071 7770 -636 -400 -1378 C ATOM 1161 CG1 ILE A 149 1.001 21.453 -16.124 1.00 67.26 C ANISOU 1161 CG1 ILE A 149 8337 8617 8600 -571 -336 -1430 C ATOM 1162 CG2 ILE A 149 -1.273 22.463 -16.547 1.00 57.63 C ANISOU 1162 CG2 ILE A 149 7177 7465 7256 -636 -508 -1281 C ATOM 1163 CD1 ILE A 149 1.326 21.890 -14.707 1.00 69.57 C ANISOU 1163 CD1 ILE A 149 8582 8873 8979 -500 -327 -1295 C ATOM 1164 N SER A 150 2.470 23.388 -18.708 1.00 58.10 N ANISOU 1164 N SER A 150 7333 7764 6979 -711 -212 -1521 N ATOM 1165 CA SER A 150 3.910 23.492 -18.841 1.00 51.92 C ANISOU 1165 CA SER A 150 6521 7018 6188 -702 -86 -1577 C ATOM 1166 C SER A 150 4.415 24.547 -17.890 1.00 56.94 C ANISOU 1166 C SER A 150 7128 7645 6863 -676 -82 -1432 C ATOM 1167 O SER A 150 4.443 25.725 -18.232 1.00 70.84 O ANISOU 1167 O SER A 150 8939 9477 8501 -723 -87 -1341 O ATOM 1168 CB SER A 150 4.298 23.852 -20.267 1.00 53.65 C ANISOU 1168 CB SER A 150 6808 7380 6194 -781 -20 -1650 C ATOM 1169 OG SER A 150 5.702 23.756 -20.428 1.00 63.02 O ANISOU 1169 OG SER A 150 7946 8603 7397 -769 122 -1723 O ATOM 1170 N ALA A 151 4.798 24.127 -16.689 1.00 52.55 N ANISOU 1170 N ALA A 151 6494 6996 6478 -603 -81 -1409 N ATOM 1171 CA ALA A 151 5.322 25.046 -15.684 1.00 53.55 C ANISOU 1171 CA ALA A 151 6591 7112 6643 -579 -88 -1294 C ATOM 1172 C ALA A 151 6.283 26.092 -16.259 1.00 59.37 C ANISOU 1172 C ALA A 151 7342 7937 7278 -638 -20 -1275 C ATOM 1173 O ALA A 151 6.111 27.288 -16.014 1.00 60.97 O ANISOU 1173 O ALA A 151 7584 8152 7430 -665 -58 -1167 O ATOM 1174 CB ALA A 151 5.995 24.271 -14.551 1.00 55.86 C ANISOU 1174 CB ALA A 151 6785 7326 7111 -501 -76 -1302 C ATOM 1175 N LYS A 152 7.278 25.638 -17.027 1.00 59.33 N ANISOU 1175 N LYS A 152 7300 7985 7256 -657 89 -1381 N ATOM 1176 CA LYS A 152 8.382 26.502 -17.485 1.00 62.10 C ANISOU 1176 CA LYS A 152 7633 8419 7543 -713 177 -1359 C ATOM 1177 C LYS A 152 7.989 27.504 -18.573 1.00 55.37 C ANISOU 1177 C LYS A 152 6881 7664 6494 -805 182 -1297 C ATOM 1178 O LYS A 152 8.799 28.326 -18.970 1.00 54.48 O ANISOU 1178 O LYS A 152 6759 7616 6324 -864 252 -1248 O ATOM 1179 CB LYS A 152 9.560 25.661 -18.000 1.00 69.27 C ANISOU 1179 CB LYS A 152 8457 9364 8499 -699 313 -1493 C ATOM 1180 CG LYS A 152 10.325 24.877 -16.945 1.00 72.30 C ANISOU 1180 CG LYS A 152 8714 9661 9096 -611 321 -1523 C ATOM 1181 CD LYS A 152 11.459 25.695 -16.365 1.00 81.34 C ANISOU 1181 CD LYS A 152 9773 10830 10302 -628 345 -1446 C ATOM 1182 CE LYS A 152 12.511 24.801 -15.716 1.00 88.80 C ANISOU 1182 CE LYS A 152 10568 11727 11443 -549 385 -1498 C ATOM 1183 NZ LYS A 152 13.214 23.920 -16.706 1.00 90.68 N ANISOU 1183 NZ LYS A 152 10746 12002 11706 -529 533 -1647 N ATOM 1184 N SER A 153 6.765 27.418 -19.079 1.00 52.44 N ANISOU 1184 N SER A 153 6596 7305 6024 -820 105 -1287 N ATOM 1185 CA SER A 153 6.326 28.344 -20.114 1.00 54.07 C ANISOU 1185 CA SER A 153 6895 7608 6041 -903 90 -1205 C ATOM 1186 C SER A 153 5.016 28.986 -19.706 1.00 56.79 C ANISOU 1186 C SER A 153 7296 7896 6387 -891 -51 -1079 C ATOM 1187 O SER A 153 4.425 29.753 -20.463 1.00 53.94 O ANISOU 1187 O SER A 153 7009 7595 5891 -946 -97 -984 O ATOM 1188 CB SER A 153 6.184 27.634 -21.462 1.00 52.22 C ANISOU 1188 CB SER A 153 6713 7487 5642 -948 138 -1326 C ATOM 1189 OG SER A 153 5.402 26.464 -21.342 1.00 53.33 O ANISOU 1189 OG SER A 153 6851 7569 5842 -904 78 -1439 O ATOM 1190 N ASN A 154 4.581 28.653 -18.494 1.00 56.63 N ANISOU 1190 N ASN A 154 7231 7763 6522 -815 -114 -1071 N ATOM 1191 CA ASN A 154 3.345 29.161 -17.916 1.00 49.17 C ANISOU 1191 CA ASN A 154 6316 6755 5611 -783 -229 -965 C ATOM 1192 C ASN A 154 2.059 28.675 -18.605 1.00 62.49 C ANISOU 1192 C ASN A 154 8043 8470 7229 -796 -313 -975 C ATOM 1193 O ASN A 154 0.953 29.098 -18.255 1.00 68.18 O ANISOU 1193 O ASN A 154 8776 9150 7979 -771 -406 -880 O ATOM 1194 CB ASN A 154 3.403 30.679 -17.835 1.00 39.16 C ANISOU 1194 CB ASN A 154 5088 5479 4313 -812 -248 -825 C ATOM 1195 CG ASN A 154 4.408 31.159 -16.809 1.00 53.03 C ANISOU 1195 CG ASN A 154 6795 7175 6178 -792 -206 -816 C ATOM 1196 OD1 ASN A 154 4.545 30.560 -15.737 1.00 55.37 O ANISOU 1196 OD1 ASN A 154 7035 7413 6589 -726 -213 -863 O ATOM 1197 ND2 ASN A 154 5.123 32.244 -17.128 1.00 53.00 N ANISOU 1197 ND2 ASN A 154 6810 7189 6140 -855 -169 -747 N ATOM 1198 N TYR A 155 2.204 27.767 -19.563 1.00 58.65 N ANISOU 1198 N TYR A 155 7570 8054 6660 -835 -279 -1099 N ATOM 1199 CA TYR A 155 1.075 27.322 -20.383 1.00 60.46 C ANISOU 1199 CA TYR A 155 7842 8330 6801 -870 -369 -1126 C ATOM 1200 C TYR A 155 -0.037 26.663 -19.564 1.00 62.65 C ANISOU 1200 C TYR A 155 8071 8505 7228 -815 -462 -1119 C ATOM 1201 O TYR A 155 0.179 25.629 -18.946 1.00 70.21 O ANISOU 1201 O TYR A 155 8972 9385 8321 -771 -431 -1210 O ATOM 1202 CB TYR A 155 1.597 26.371 -21.458 1.00 66.58 C ANISOU 1202 CB TYR A 155 8640 9190 7467 -918 -301 -1303 C ATOM 1203 CG TYR A 155 0.559 25.614 -22.255 1.00 68.89 C ANISOU 1203 CG TYR A 155 8970 9523 7684 -960 -396 -1388 C ATOM 1204 CD1 TYR A 155 -0.225 26.251 -23.210 1.00 66.16 C ANISOU 1204 CD1 TYR A 155 8695 9290 7153 -1029 -492 -1308 C ATOM 1205 CD2 TYR A 155 0.407 24.242 -22.090 1.00 76.27 C ANISOU 1205 CD2 TYR A 155 9864 10380 8736 -938 -396 -1551 C ATOM 1206 CE1 TYR A 155 -1.159 25.543 -23.957 1.00 75.34 C ANISOU 1206 CE1 TYR A 155 9886 10501 8239 -1078 -596 -1395 C ATOM 1207 CE2 TYR A 155 -0.518 23.523 -22.831 1.00 79.59 C ANISOU 1207 CE2 TYR A 155 10314 10828 9097 -990 -491 -1648 C ATOM 1208 CZ TYR A 155 -1.300 24.174 -23.763 1.00 82.73 C ANISOU 1208 CZ TYR A 155 10781 11352 9299 -1063 -596 -1576 C ATOM 1209 OH TYR A 155 -2.216 23.446 -24.496 1.00 84.48 O ANISOU 1209 OH TYR A 155 11028 11611 9460 -1124 -709 -1680 O ATOM 1210 N ASN A 156 -1.223 27.268 -19.562 1.00 57.23 N ANISOU 1210 N ASN A 156 7398 7818 6528 -816 -573 -998 N ATOM 1211 CA ASN A 156 -2.372 26.750 -18.807 1.00 52.59 C ANISOU 1211 CA ASN A 156 6752 7147 6084 -769 -655 -968 C ATOM 1212 C ASN A 156 -2.196 26.832 -17.310 1.00 49.21 C ANISOU 1212 C ASN A 156 6264 6614 5818 -683 -614 -915 C ATOM 1213 O ASN A 156 -2.955 26.207 -16.570 1.00 53.97 O ANISOU 1213 O ASN A 156 6808 7149 6549 -641 -649 -900 O ATOM 1214 CB ASN A 156 -2.677 25.291 -19.155 1.00 52.35 C ANISOU 1214 CB ASN A 156 6693 7097 6099 -795 -677 -1115 C ATOM 1215 CG ASN A 156 -3.395 25.149 -20.454 1.00 57.47 C ANISOU 1215 CG ASN A 156 7390 7843 6602 -878 -770 -1156 C ATOM 1216 OD1 ASN A 156 -4.123 26.041 -20.865 1.00 69.51 O ANISOU 1216 OD1 ASN A 156 8940 9430 8040 -900 -858 -1032 O ATOM 1217 ND2 ASN A 156 -3.197 24.022 -21.119 1.00 59.57 N ANISOU 1217 ND2 ASN A 156 7669 8123 6844 -924 -758 -1336 N ATOM 1218 N PHE A 157 -1.194 27.580 -16.867 1.00 42.84 N ANISOU 1218 N PHE A 157 5472 5803 5003 -663 -541 -885 N ATOM 1219 CA PHE A 157 -0.988 27.812 -15.445 1.00 45.55 C ANISOU 1219 CA PHE A 157 5773 6068 5467 -588 -514 -836 C ATOM 1220 C PHE A 157 -2.295 28.087 -14.667 1.00 55.32 C ANISOU 1220 C PHE A 157 6981 7256 6783 -532 -580 -736 C ATOM 1221 O PHE A 157 -2.545 27.482 -13.622 1.00 60.07 O ANISOU 1221 O PHE A 157 7527 7804 7493 -476 -568 -731 O ATOM 1222 CB PHE A 157 0.028 28.950 -15.191 1.00 46.71 C ANISOU 1222 CB PHE A 157 5950 6222 5577 -592 -462 -797 C ATOM 1223 CG PHE A 157 0.169 29.283 -13.738 1.00 46.95 C ANISOU 1223 CG PHE A 157 5948 6185 5705 -522 -451 -758 C ATOM 1224 CD1 PHE A 157 0.889 28.439 -12.891 1.00 41.03 C ANISOU 1224 CD1 PHE A 157 5144 5410 5036 -484 -411 -814 C ATOM 1225 CD2 PHE A 157 -0.487 30.384 -13.199 1.00 41.32 C ANISOU 1225 CD2 PHE A 157 5259 5436 5006 -488 -487 -666 C ATOM 1226 CE1 PHE A 157 0.973 28.694 -11.541 1.00 38.78 C ANISOU 1226 CE1 PHE A 157 4836 5085 4812 -423 -411 -777 C ATOM 1227 CE2 PHE A 157 -0.409 30.655 -11.849 1.00 44.25 C ANISOU 1227 CE2 PHE A 157 5610 5758 5444 -423 -474 -651 C ATOM 1228 CZ PHE A 157 0.322 29.807 -11.013 1.00 47.90 C ANISOU 1228 CZ PHE A 157 6027 6218 5957 -395 -440 -705 C ATOM 1229 N GLU A 158 -3.127 28.991 -15.176 1.00 56.32 N ANISOU 1229 N GLU A 158 7136 7405 6857 -545 -643 -647 N ATOM 1230 CA GLU A 158 -4.325 29.412 -14.452 1.00 56.12 C ANISOU 1230 CA GLU A 158 7071 7335 6916 -482 -689 -548 C ATOM 1231 C GLU A 158 -5.463 28.380 -14.472 1.00 57.52 C ANISOU 1231 C GLU A 158 7180 7506 7170 -480 -746 -551 C ATOM 1232 O GLU A 158 -6.310 28.372 -13.568 1.00 55.52 O ANISOU 1232 O GLU A 158 6865 7211 7019 -417 -750 -486 O ATOM 1233 CB GLU A 158 -4.834 30.759 -14.988 1.00 48.71 C ANISOU 1233 CB GLU A 158 6173 6406 5928 -485 -741 -440 C ATOM 1234 CG GLU A 158 -5.692 30.661 -16.247 1.00 49.46 C ANISOU 1234 CG GLU A 158 6272 6567 5953 -542 -841 -400 C ATOM 1235 CD GLU A 158 -4.901 30.339 -17.517 1.00 63.06 C ANISOU 1235 CD GLU A 158 8058 8381 7520 -639 -838 -472 C ATOM 1236 OE1 GLU A 158 -3.644 30.425 -17.504 1.00 48.88 O ANISOU 1236 OE1 GLU A 158 6302 6594 5677 -660 -749 -532 O ATOM 1237 OE2 GLU A 158 -5.549 30.006 -18.541 1.00 63.42 O ANISOU 1237 OE2 GLU A 158 8111 8500 7485 -696 -925 -471 O ATOM 1238 N LYS A 159 -5.477 27.518 -15.492 1.00 56.78 N ANISOU 1238 N LYS A 159 7093 7455 7028 -553 -785 -631 N ATOM 1239 CA LYS A 159 -6.619 26.621 -15.730 1.00 58.83 C ANISOU 1239 CA LYS A 159 7288 7707 7359 -576 -865 -636 C ATOM 1240 C LYS A 159 -7.015 25.805 -14.499 1.00 55.44 C ANISOU 1240 C LYS A 159 6771 7198 7096 -520 -829 -620 C ATOM 1241 O LYS A 159 -8.160 25.860 -14.068 1.00 66.13 O ANISOU 1241 O LYS A 159 8053 8534 8540 -490 -869 -530 O ATOM 1242 CB LYS A 159 -6.376 25.685 -16.922 1.00 61.51 C ANISOU 1242 CB LYS A 159 7657 8092 7622 -667 -901 -770 C ATOM 1243 CG LYS A 159 -6.020 26.373 -18.233 1.00 60.19 C ANISOU 1243 CG LYS A 159 7579 8032 7258 -735 -932 -783 C ATOM 1244 CD LYS A 159 -7.240 26.939 -18.934 1.00 46.33 C ANISOU 1244 CD LYS A 159 5815 6337 5452 -766 -1067 -680 C ATOM 1245 CE LYS A 159 -6.979 27.216 -20.425 1.00 49.54 C ANISOU 1245 CE LYS A 159 6310 6873 5639 -857 -1119 -712 C ATOM 1246 NZ LYS A 159 -6.122 28.418 -20.674 1.00 70.68 N ANISOU 1246 NZ LYS A 159 9065 9594 8197 -853 -1056 -633 N ATOM 1247 N PRO A 160 -6.065 25.045 -13.932 1.00 59.63 N ANISOU 1247 N PRO A 160 7301 7685 7672 -504 -751 -692 N ATOM 1248 CA PRO A 160 -6.346 24.202 -12.761 1.00 56.04 C ANISOU 1248 CA PRO A 160 6768 7159 7367 -455 -716 -657 C ATOM 1249 C PRO A 160 -7.049 24.967 -11.644 1.00 50.24 C ANISOU 1249 C PRO A 160 5995 6422 6673 -377 -693 -527 C ATOM 1250 O PRO A 160 -7.851 24.379 -10.915 1.00 57.76 O ANISOU 1250 O PRO A 160 6866 7341 7741 -351 -687 -461 O ATOM 1251 CB PRO A 160 -4.939 23.787 -12.288 1.00 47.67 C ANISOU 1251 CB PRO A 160 5730 6071 6310 -432 -634 -724 C ATOM 1252 CG PRO A 160 -4.102 23.847 -13.500 1.00 41.16 C ANISOU 1252 CG PRO A 160 4973 5291 5377 -493 -632 -840 C ATOM 1253 CD PRO A 160 -4.643 24.979 -14.327 1.00 51.82 C ANISOU 1253 CD PRO A 160 6373 6714 6602 -526 -688 -794 C ATOM 1254 N PHE A 161 -6.743 26.256 -11.517 1.00 43.10 N ANISOU 1254 N PHE A 161 5147 5550 5680 -342 -674 -494 N ATOM 1255 CA PHE A 161 -7.177 27.056 -10.379 1.00 43.90 C ANISOU 1255 CA PHE A 161 5228 5643 5807 -257 -631 -407 C ATOM 1256 C PHE A 161 -8.569 27.601 -10.610 1.00 52.30 C ANISOU 1256 C PHE A 161 6240 6716 6914 -237 -682 -319 C ATOM 1257 O PHE A 161 -9.392 27.641 -9.696 1.00 57.28 O ANISOU 1257 O PHE A 161 6802 7337 7624 -173 -646 -246 O ATOM 1258 CB PHE A 161 -6.212 28.226 -10.153 1.00 46.62 C ANISOU 1258 CB PHE A 161 5657 5997 6061 -233 -593 -427 C ATOM 1259 CG PHE A 161 -4.796 27.805 -9.900 1.00 44.34 C ANISOU 1259 CG PHE A 161 5402 5708 5738 -250 -547 -504 C ATOM 1260 CD1 PHE A 161 -4.395 27.394 -8.637 1.00 43.97 C ANISOU 1260 CD1 PHE A 161 5330 5652 5726 -198 -496 -495 C ATOM 1261 CD2 PHE A 161 -3.861 27.816 -10.926 1.00 50.23 C ANISOU 1261 CD2 PHE A 161 6197 6474 6416 -316 -555 -577 C ATOM 1262 CE1 PHE A 161 -3.084 26.994 -8.401 1.00 40.58 C ANISOU 1262 CE1 PHE A 161 4914 5224 5281 -210 -469 -553 C ATOM 1263 CE2 PHE A 161 -2.554 27.420 -10.699 1.00 46.20 C ANISOU 1263 CE2 PHE A 161 5695 5964 5896 -326 -509 -644 C ATOM 1264 CZ PHE A 161 -2.164 27.010 -9.434 1.00 41.77 C ANISOU 1264 CZ PHE A 161 5100 5385 5388 -271 -473 -630 C ATOM 1265 N LEU A 162 -8.809 28.047 -11.841 1.00 59.00 N ANISOU 1265 N LEU A 162 7118 7591 7707 -290 -763 -320 N ATOM 1266 CA LEU A 162 -10.104 28.565 -12.260 1.00 54.57 C ANISOU 1266 CA LEU A 162 6498 7043 7191 -278 -838 -228 C ATOM 1267 C LEU A 162 -11.145 27.488 -12.057 1.00 64.57 C ANISOU 1267 C LEU A 162 7647 8302 8583 -293 -868 -199 C ATOM 1268 O LEU A 162 -12.203 27.717 -11.465 1.00 70.61 O ANISOU 1268 O LEU A 162 8319 9061 9451 -234 -857 -106 O ATOM 1269 CB LEU A 162 -10.053 28.935 -13.737 1.00 42.92 C ANISOU 1269 CB LEU A 162 5077 5617 5613 -355 -938 -235 C ATOM 1270 CG LEU A 162 -11.290 29.612 -14.314 1.00 49.95 C ANISOU 1270 CG LEU A 162 5911 6529 6538 -344 -1040 -122 C ATOM 1271 CD1 LEU A 162 -11.645 30.843 -13.500 1.00 52.01 C ANISOU 1271 CD1 LEU A 162 6156 6741 6864 -233 -988 -31 C ATOM 1272 CD2 LEU A 162 -11.077 29.970 -15.777 1.00 47.11 C ANISOU 1272 CD2 LEU A 162 5623 6237 6038 -428 -1142 -119 C ATOM 1273 N TRP A 163 -10.822 26.298 -12.547 1.00 63.69 N ANISOU 1273 N TRP A 163 7536 8187 8478 -373 -897 -282 N ATOM 1274 CA TRP A 163 -11.721 25.170 -12.443 1.00 54.24 C ANISOU 1274 CA TRP A 163 6229 6963 7416 -409 -935 -266 C ATOM 1275 C TRP A 163 -11.983 24.787 -10.985 1.00 55.82 C ANISOU 1275 C TRP A 163 6353 7123 7733 -338 -832 -193 C ATOM 1276 O TRP A 163 -13.111 24.425 -10.627 1.00 56.45 O ANISOU 1276 O TRP A 163 6313 7194 7942 -332 -842 -108 O ATOM 1277 CB TRP A 163 -11.170 23.990 -13.231 1.00 49.06 C ANISOU 1277 CB TRP A 163 5605 6287 6750 -506 -977 -396 C ATOM 1278 CG TRP A 163 -12.151 22.898 -13.367 1.00 55.26 C ANISOU 1278 CG TRP A 163 6282 7033 7683 -567 -1044 -390 C ATOM 1279 CD1 TRP A 163 -13.007 22.693 -14.405 1.00 65.04 C ANISOU 1279 CD1 TRP A 163 7480 8303 8931 -651 -1180 -409 C ATOM 1280 CD2 TRP A 163 -12.405 21.846 -12.413 1.00 55.14 C ANISOU 1280 CD2 TRP A 163 6178 6937 7838 -559 -988 -354 C ATOM 1281 NE1 TRP A 163 -13.778 21.582 -14.163 1.00 74.71 N ANISOU 1281 NE1 TRP A 163 8591 9462 10335 -700 -1213 -400 N ATOM 1282 CE2 TRP A 163 -13.428 21.052 -12.972 1.00 68.35 C ANISOU 1282 CE2 TRP A 163 7755 8583 9633 -646 -1093 -359 C ATOM 1283 CE3 TRP A 163 -11.862 21.520 -11.175 1.00 51.82 C ANISOU 1283 CE3 TRP A 163 5749 6470 7471 -493 -869 -309 C ATOM 1284 CZ2 TRP A 163 -13.913 19.923 -12.295 1.00 61.24 C ANISOU 1284 CZ2 TRP A 163 6746 7592 8929 -670 -1069 -314 C ATOM 1285 CZ3 TRP A 163 -12.348 20.395 -10.521 1.00 54.30 C ANISOU 1285 CZ3 TRP A 163 5962 6708 7962 -512 -847 -253 C ATOM 1286 CH2 TRP A 163 -13.364 19.614 -11.083 1.00 56.91 C ANISOU 1286 CH2 TRP A 163 6194 6996 8433 -601 -941 -253 C ATOM 1287 N LEU A 164 -10.958 24.870 -10.140 1.00 50.87 N ANISOU 1287 N LEU A 164 5789 6484 7056 -287 -733 -218 N ATOM 1288 CA LEU A 164 -11.148 24.599 -8.713 1.00 53.93 C ANISOU 1288 CA LEU A 164 6120 6859 7513 -217 -634 -140 C ATOM 1289 C LEU A 164 -11.954 25.696 -8.006 1.00 55.07 C ANISOU 1289 C LEU A 164 6228 7039 7657 -125 -583 -50 C ATOM 1290 O LEU A 164 -12.670 25.429 -7.033 1.00 52.23 O ANISOU 1290 O LEU A 164 5780 6688 7376 -77 -513 38 O ATOM 1291 CB LEU A 164 -9.808 24.413 -8.002 1.00 56.46 C ANISOU 1291 CB LEU A 164 6517 7170 7766 -189 -562 -188 C ATOM 1292 CG LEU A 164 -9.020 23.127 -8.251 1.00 54.06 C ANISOU 1292 CG LEU A 164 6217 6811 7511 -247 -573 -255 C ATOM 1293 CD1 LEU A 164 -7.589 23.282 -7.782 1.00 35.51 C ANISOU 1293 CD1 LEU A 164 3947 4469 5078 -215 -523 -307 C ATOM 1294 CD2 LEU A 164 -9.719 21.918 -7.587 1.00 60.40 C ANISOU 1294 CD2 LEU A 164 6913 7563 8474 -256 -553 -168 C ATOM 1295 N ALA A 165 -11.838 26.929 -8.492 1.00 47.99 N ANISOU 1295 N ALA A 165 5395 6159 6679 -99 -610 -69 N ATOM 1296 CA ALA A 165 -12.526 28.048 -7.852 1.00 45.01 C ANISOU 1296 CA ALA A 165 4991 5794 6315 0 -556 -4 C ATOM 1297 C ALA A 165 -14.035 27.954 -8.086 1.00 48.93 C ANISOU 1297 C ALA A 165 5345 6300 6945 9 -596 93 C ATOM 1298 O ALA A 165 -14.842 28.172 -7.176 1.00 47.05 O ANISOU 1298 O ALA A 165 5021 6077 6780 90 -511 165 O ATOM 1299 CB ALA A 165 -11.971 29.387 -8.342 1.00 41.50 C ANISOU 1299 CB ALA A 165 4651 5338 5778 22 -581 -44 C ATOM 1300 N ARG A 166 -14.407 27.608 -9.312 1.00 53.92 N ANISOU 1300 N ARG A 166 5948 6934 7606 -77 -724 91 N ATOM 1301 CA ARG A 166 -15.806 27.416 -9.662 1.00 56.01 C ANISOU 1301 CA ARG A 166 6064 7212 8007 -89 -792 182 C ATOM 1302 C ARG A 166 -16.507 26.344 -8.817 1.00 61.76 C ANISOU 1302 C ARG A 166 6658 7935 8874 -95 -728 244 C ATOM 1303 O ARG A 166 -17.704 26.446 -8.556 1.00 68.34 O ANISOU 1303 O ARG A 166 7345 8784 9836 -59 -718 345 O ATOM 1304 CB ARG A 166 -15.919 27.093 -11.145 1.00 47.35 C ANISOU 1304 CB ARG A 166 4977 6130 6884 -201 -958 147 C ATOM 1305 CG ARG A 166 -15.505 28.246 -12.012 1.00 52.03 C ANISOU 1305 CG ARG A 166 5673 6743 7354 -194 -1023 136 C ATOM 1306 CD ARG A 166 -15.639 27.921 -13.469 1.00 55.91 C ANISOU 1306 CD ARG A 166 6180 7277 7786 -307 -1186 107 C ATOM 1307 NE ARG A 166 -15.280 29.072 -14.276 1.00 52.69 N ANISOU 1307 NE ARG A 166 5868 6897 7255 -299 -1244 131 N ATOM 1308 CZ ARG A 166 -15.303 29.093 -15.600 1.00 71.95 C ANISOU 1308 CZ ARG A 166 8348 9398 9592 -388 -1383 123 C ATOM 1309 NH1 ARG A 166 -15.676 28.018 -16.272 1.00 82.83 N ANISOU 1309 NH1 ARG A 166 9682 10814 10975 -493 -1485 66 N ATOM 1310 NH2 ARG A 166 -14.958 30.193 -16.250 1.00 79.93 N ANISOU 1310 NH2 ARG A 166 9445 10433 10494 -377 -1422 173 N ATOM 1311 N LYS A 167 -15.771 25.325 -8.381 1.00 51.40 N ANISOU 1311 N LYS A 167 5384 6596 7548 -138 -681 199 N ATOM 1312 CA LYS A 167 -16.372 24.271 -7.566 1.00 59.32 C ANISOU 1312 CA LYS A 167 6266 7585 8689 -151 -617 280 C ATOM 1313 C LYS A 167 -16.526 24.681 -6.107 1.00 60.08 C ANISOU 1313 C LYS A 167 6336 7721 8772 -38 -453 358 C ATOM 1314 O LYS A 167 -17.523 24.372 -5.462 1.00 68.34 O ANISOU 1314 O LYS A 167 7241 8788 9937 -14 -386 470 O ATOM 1315 CB LYS A 167 -15.549 22.986 -7.633 1.00 69.38 C ANISOU 1315 CB LYS A 167 7584 8801 9977 -235 -632 219 C ATOM 1316 CG LYS A 167 -15.165 22.561 -9.032 1.00 71.42 C ANISOU 1316 CG LYS A 167 7899 9024 10212 -342 -772 99 C ATOM 1317 CD LYS A 167 -16.370 22.128 -9.829 1.00 70.22 C ANISOU 1317 CD LYS A 167 7621 8866 10193 -425 -893 129 C ATOM 1318 CE LYS A 167 -16.699 20.671 -9.564 1.00 73.42 C ANISOU 1318 CE LYS A 167 7929 9190 10776 -505 -895 151 C ATOM 1319 NZ LYS A 167 -17.631 20.117 -10.597 1.00 77.21 N ANISOU 1319 NZ LYS A 167 8312 9650 11373 -622 -1050 127 N ATOM 1320 N LEU A 168 -15.524 25.360 -5.578 1.00 59.79 N ANISOU 1320 N LEU A 168 6432 7701 8584 27 -386 297 N ATOM 1321 CA LEU A 168 -15.518 25.706 -4.164 1.00 63.41 C ANISOU 1321 CA LEU A 168 6893 8210 8991 128 -234 343 C ATOM 1322 C LEU A 168 -16.435 26.887 -3.897 1.00 57.94 C ANISOU 1322 C LEU A 168 6144 7552 8319 231 -176 377 C ATOM 1323 O LEU A 168 -16.883 27.096 -2.768 1.00 60.83 O ANISOU 1323 O LEU A 168 6462 7971 8678 316 -38 430 O ATOM 1324 CB LEU A 168 -14.091 26.033 -3.716 1.00 71.87 C ANISOU 1324 CB LEU A 168 8124 9288 9894 152 -203 250 C ATOM 1325 CG LEU A 168 -13.046 24.977 -4.069 1.00 62.56 C ANISOU 1325 CG LEU A 168 7001 8065 8702 65 -262 203 C ATOM 1326 CD1 LEU A 168 -11.657 25.591 -4.128 1.00 46.70 C ANISOU 1326 CD1 LEU A 168 5141 6057 6546 76 -275 91 C ATOM 1327 CD2 LEU A 168 -13.109 23.824 -3.077 1.00 66.96 C ANISOU 1327 CD2 LEU A 168 7495 8631 9317 58 -190 301 C ATOM 1328 N ILE A 169 -16.692 27.670 -4.940 1.00 54.79 N ANISOU 1328 N ILE A 169 5753 7124 7942 227 -277 347 N ATOM 1329 CA ILE A 169 -17.626 28.787 -4.840 1.00 66.53 C ANISOU 1329 CA ILE A 169 7169 8619 9490 329 -240 388 C ATOM 1330 C ILE A 169 -19.012 28.336 -5.302 1.00 69.79 C ANISOU 1330 C ILE A 169 7386 9042 10089 302 -293 500 C ATOM 1331 O ILE A 169 -20.031 28.785 -4.788 1.00 63.64 O ANISOU 1331 O ILE A 169 6480 8289 9411 392 -209 574 O ATOM 1332 CB ILE A 169 -17.165 30.004 -5.677 1.00 64.39 C ANISOU 1332 CB ILE A 169 7007 8302 9155 350 -324 321 C ATOM 1333 CG1 ILE A 169 -15.709 30.371 -5.351 1.00 57.44 C ANISOU 1333 CG1 ILE A 169 6311 7406 8106 349 -293 208 C ATOM 1334 CG2 ILE A 169 -18.075 31.195 -5.441 1.00 56.52 C ANISOU 1334 CG2 ILE A 169 5941 7292 8244 476 -272 363 C ATOM 1335 CD1 ILE A 169 -15.454 30.612 -3.878 1.00 55.76 C ANISOU 1335 CD1 ILE A 169 6135 7229 7823 440 -135 176 C ATOM 1336 N GLY A 170 -19.036 27.417 -6.257 1.00 70.20 N ANISOU 1336 N GLY A 170 7409 9073 10190 174 -431 503 N ATOM 1337 CA GLY A 170 -20.281 27.004 -6.865 1.00 67.21 C ANISOU 1337 CA GLY A 170 6848 8701 9986 125 -522 595 C ATOM 1338 C GLY A 170 -20.765 28.118 -7.767 1.00 70.71 C ANISOU 1338 C GLY A 170 7274 9142 10451 165 -630 612 C ATOM 1339 O GLY A 170 -21.941 28.495 -7.751 1.00 78.62 O ANISOU 1339 O GLY A 170 8109 10162 11600 221 -632 710 O ATOM 1340 N ASP A 171 -19.839 28.664 -8.545 1.00 58.48 N ANISOU 1340 N ASP A 171 5889 7572 8761 139 -716 527 N ATOM 1341 CA ASP A 171 -20.188 29.645 -9.545 1.00 48.97 C ANISOU 1341 CA ASP A 171 4683 6363 7562 157 -842 560 C ATOM 1342 C ASP A 171 -19.560 29.322 -10.886 1.00 51.49 C ANISOU 1342 C ASP A 171 5106 6690 7766 27 -1011 499 C ATOM 1343 O ASP A 171 -18.440 29.714 -11.162 1.00 53.66 O ANISOU 1343 O ASP A 171 5551 6951 7888 13 -1009 418 O ATOM 1344 CB ASP A 171 -19.794 31.046 -9.098 1.00 51.88 C ANISOU 1344 CB ASP A 171 5145 6693 7874 286 -753 542 C ATOM 1345 CG ASP A 171 -20.307 32.120 -10.046 1.00 61.14 C ANISOU 1345 CG ASP A 171 6292 7845 9094 323 -877 615 C ATOM 1346 OD1 ASP A 171 -20.796 31.762 -11.146 1.00 54.59 O ANISOU 1346 OD1 ASP A 171 5399 7051 8293 233 -1048 670 O ATOM 1347 OD2 ASP A 171 -20.218 33.319 -9.690 1.00 66.10 O ANISOU 1347 OD2 ASP A 171 6964 8418 9732 439 -809 619 O ATOM 1348 N PRO A 172 -20.310 28.630 -11.741 1.00 60.19 N ANISOU 1348 N PRO A 172 6102 7824 8944 -72 -1160 536 N ATOM 1349 CA PRO A 172 -19.842 28.213 -13.067 1.00 65.32 C ANISOU 1349 CA PRO A 172 6841 8502 9474 -205 -1327 465 C ATOM 1350 C PRO A 172 -19.416 29.403 -13.929 1.00 64.71 C ANISOU 1350 C PRO A 172 6881 8444 9263 -183 -1406 480 C ATOM 1351 O PRO A 172 -18.813 29.212 -14.984 1.00 62.25 O ANISOU 1351 O PRO A 172 6679 8171 8803 -283 -1513 414 O ATOM 1352 CB PRO A 172 -21.091 27.571 -13.689 1.00 63.56 C ANISOU 1352 CB PRO A 172 6440 8317 9393 -286 -1480 531 C ATOM 1353 CG PRO A 172 -22.024 27.335 -12.559 1.00 61.82 C ANISOU 1353 CG PRO A 172 6037 8076 9376 -214 -1363 625 C ATOM 1354 CD PRO A 172 -21.751 28.384 -11.559 1.00 54.40 C ANISOU 1354 CD PRO A 172 5142 7111 8417 -56 -1189 653 C ATOM 1355 N ASN A 173 -19.754 30.614 -13.499 1.00 61.38 N ANISOU 1355 N ASN A 173 6431 7992 8899 -53 -1350 569 N ATOM 1356 CA ASN A 173 -19.518 31.803 -14.317 1.00 63.79 C ANISOU 1356 CA ASN A 173 6822 8296 9120 -28 -1435 623 C ATOM 1357 C ASN A 173 -18.484 32.735 -13.721 1.00 65.50 C ANISOU 1357 C ASN A 173 7186 8444 9256 52 -1300 574 C ATOM 1358 O ASN A 173 -18.358 33.886 -14.132 1.00 69.99 O ANISOU 1358 O ASN A 173 7811 8979 9804 100 -1336 638 O ATOM 1359 CB ASN A 173 -20.820 32.551 -14.555 1.00 68.29 C ANISOU 1359 CB ASN A 173 7229 8867 9853 50 -1523 781 C ATOM 1360 CG ASN A 173 -21.748 31.805 -15.481 1.00 79.53 C ANISOU 1360 CG ASN A 173 8520 10371 11324 -55 -1716 837 C ATOM 1361 OD1 ASN A 173 -21.305 31.165 -16.439 1.00 85.63 O ANISOU 1361 OD1 ASN A 173 9379 11208 11950 -193 -1837 769 O ATOM 1362 ND2 ASN A 173 -23.045 31.882 -15.205 1.00 78.00 N ANISOU 1362 ND2 ASN A 173 8113 10181 11342 8 -1744 954 N ATOM 1363 N LEU A 174 -17.760 32.219 -12.737 1.00 64.15 N ANISOU 1363 N LEU A 174 7073 8251 9051 62 -1153 469 N ATOM 1364 CA LEU A 174 -16.656 32.924 -12.134 1.00 56.41 C ANISOU 1364 CA LEU A 174 6236 7216 7981 114 -1035 398 C ATOM 1365 C LEU A 174 -15.577 33.079 -13.202 1.00 64.42 C ANISOU 1365 C LEU A 174 7402 8251 8825 15 -1114 352 C ATOM 1366 O LEU A 174 -15.296 32.141 -13.950 1.00 62.79 O ANISOU 1366 O LEU A 174 7218 8106 8533 -100 -1189 300 O ATOM 1367 CB LEU A 174 -16.134 32.119 -10.942 1.00 57.29 C ANISOU 1367 CB LEU A 174 6364 7326 8079 125 -891 305 C ATOM 1368 CG LEU A 174 -15.096 32.744 -10.005 1.00 58.71 C ANISOU 1368 CG LEU A 174 6666 7460 8183 187 -760 224 C ATOM 1369 CD1 LEU A 174 -15.694 33.931 -9.272 1.00 67.49 C ANISOU 1369 CD1 LEU A 174 7741 8515 9389 327 -681 264 C ATOM 1370 CD2 LEU A 174 -14.616 31.727 -9.004 1.00 53.31 C ANISOU 1370 CD2 LEU A 174 5986 6800 7468 175 -658 155 C ATOM 1371 N GLU A 175 -14.999 34.273 -13.298 1.00 68.84 N ANISOU 1371 N GLU A 175 8059 8756 9341 56 -1094 369 N ATOM 1372 CA GLU A 175 -13.903 34.522 -14.231 1.00 61.42 C ANISOU 1372 CA GLU A 175 7261 7838 8240 -36 -1142 339 C ATOM 1373 C GLU A 175 -12.774 35.186 -13.469 1.00 53.30 C ANISOU 1373 C GLU A 175 6342 6737 7172 1 -1019 264 C ATOM 1374 O GLU A 175 -13.019 35.830 -12.456 1.00 62.71 O ANISOU 1374 O GLU A 175 7512 7853 8464 109 -932 262 O ATOM 1375 CB GLU A 175 -14.354 35.414 -15.387 1.00 64.85 C ANISOU 1375 CB GLU A 175 7698 8282 8660 -50 -1276 476 C ATOM 1376 CG GLU A 175 -15.603 34.929 -16.117 1.00 77.13 C ANISOU 1376 CG GLU A 175 9126 9911 10268 -78 -1423 568 C ATOM 1377 CD GLU A 175 -15.392 33.621 -16.871 1.00 92.50 C ANISOU 1377 CD GLU A 175 11089 11968 12089 -216 -1498 481 C ATOM 1378 OE1 GLU A 175 -14.262 33.369 -17.345 1.00 94.60 O ANISOU 1378 OE1 GLU A 175 11484 12270 12188 -299 -1475 390 O ATOM 1379 OE2 GLU A 175 -16.367 32.844 -16.995 1.00100.30 O ANISOU 1379 OE2 GLU A 175 11953 13000 13156 -241 -1578 497 O ATOM 1380 N PHE A 176 -11.536 34.991 -13.919 1.00 48.90 N ANISOU 1380 N PHE A 176 5898 6209 6474 -89 -1008 190 N ATOM 1381 CA PHE A 176 -10.407 35.762 -13.382 1.00 48.31 C ANISOU 1381 CA PHE A 176 5924 6066 6366 -73 -919 134 C ATOM 1382 C PHE A 176 -10.353 37.009 -14.213 1.00 51.05 C ANISOU 1382 C PHE A 176 6325 6367 6706 -82 -981 242 C ATOM 1383 O PHE A 176 -10.285 36.930 -15.442 1.00 57.46 O ANISOU 1383 O PHE A 176 7164 7248 7419 -168 -1072 304 O ATOM 1384 CB PHE A 176 -9.066 35.027 -13.520 1.00 51.18 C ANISOU 1384 CB PHE A 176 6364 6481 6601 -165 -876 20 C ATOM 1385 CG PHE A 176 -8.918 33.830 -12.609 1.00 55.26 C ANISOU 1385 CG PHE A 176 6838 7023 7134 -153 -809 -78 C ATOM 1386 CD1 PHE A 176 -9.526 33.807 -11.363 1.00 61.25 C ANISOU 1386 CD1 PHE A 176 7535 7745 7992 -56 -744 -80 C ATOM 1387 CD2 PHE A 176 -8.160 32.738 -12.997 1.00 44.14 C ANISOU 1387 CD2 PHE A 176 5450 5674 5645 -235 -805 -163 C ATOM 1388 CE1 PHE A 176 -9.390 32.720 -10.531 1.00 56.09 C ANISOU 1388 CE1 PHE A 176 6843 7119 7349 -50 -685 -140 C ATOM 1389 CE2 PHE A 176 -8.009 31.659 -12.163 1.00 55.66 C ANISOU 1389 CE2 PHE A 176 6868 7140 7141 -221 -749 -231 C ATOM 1390 CZ PHE A 176 -8.626 31.645 -10.928 1.00 59.85 C ANISOU 1390 CZ PHE A 176 7339 7638 7763 -132 -693 -208 C ATOM 1391 N VAL A 177 -10.398 38.163 -13.559 1.00 50.82 N ANISOU 1391 N VAL A 177 6312 6218 6780 5 -933 265 N ATOM 1392 CA VAL A 177 -10.328 39.429 -14.281 1.00 58.52 C ANISOU 1392 CA VAL A 177 7337 7115 7782 2 -989 384 C ATOM 1393 C VAL A 177 -8.914 39.663 -14.850 1.00 55.55 C ANISOU 1393 C VAL A 177 7077 6752 7276 -112 -972 358 C ATOM 1394 O VAL A 177 -8.762 40.125 -15.982 1.00 53.87 O ANISOU 1394 O VAL A 177 6906 6565 6999 -180 -1044 475 O ATOM 1395 CB VAL A 177 -10.824 40.614 -13.411 1.00 48.22 C ANISOU 1395 CB VAL A 177 6013 5650 6657 134 -939 405 C ATOM 1396 CG1 VAL A 177 -12.035 40.197 -12.639 1.00 49.15 C ANISOU 1396 CG1 VAL A 177 6009 5778 6888 245 -910 394 C ATOM 1397 CG2 VAL A 177 -9.782 41.042 -12.429 1.00 52.94 C ANISOU 1397 CG2 VAL A 177 6694 6166 7255 142 -832 269 C ATOM 1398 N ALA A 178 -7.884 39.317 -14.082 1.00 43.86 N ANISOU 1398 N ALA A 178 5641 5270 5754 -135 -877 215 N ATOM 1399 CA ALA A 178 -6.511 39.475 -14.564 1.00 58.15 C ANISOU 1399 CA ALA A 178 7537 7100 7459 -242 -850 186 C ATOM 1400 C ALA A 178 -5.612 38.301 -14.205 1.00 61.65 C ANISOU 1400 C ALA A 178 7983 7634 7807 -294 -787 41 C ATOM 1401 O ALA A 178 -5.670 37.769 -13.094 1.00 61.97 O ANISOU 1401 O ALA A 178 7989 7665 7891 -235 -734 -57 O ATOM 1402 CB ALA A 178 -5.888 40.801 -14.064 1.00 48.11 C ANISOU 1402 CB ALA A 178 6323 5677 6278 -225 -808 188 C ATOM 1403 N MET A 179 -4.774 37.907 -15.154 1.00 58.72 N ANISOU 1403 N MET A 179 7650 7353 7307 -401 -789 35 N ATOM 1404 CA MET A 179 -3.784 36.867 -14.904 1.00 59.70 C ANISOU 1404 CA MET A 179 7773 7548 7362 -448 -725 -98 C ATOM 1405 C MET A 179 -2.719 37.357 -13.903 1.00 61.09 C ANISOU 1405 C MET A 179 7972 7650 7589 -441 -652 -176 C ATOM 1406 O MET A 179 -2.124 38.443 -14.079 1.00 60.42 O ANISOU 1406 O MET A 179 7934 7497 7525 -478 -643 -130 O ATOM 1407 CB MET A 179 -3.150 36.418 -16.219 1.00 59.62 C ANISOU 1407 CB MET A 179 7795 7653 7203 -558 -730 -93 C ATOM 1408 CG MET A 179 -2.099 35.336 -16.059 1.00 73.25 C ANISOU 1408 CG MET A 179 9509 9445 8877 -597 -656 -233 C ATOM 1409 SD MET A 179 -2.843 33.703 -15.903 1.00116.09 S ANISOU 1409 SD MET A 179 14872 14928 14309 -566 -679 -324 S ATOM 1410 CE MET A 179 -3.703 33.623 -17.466 1.00 58.93 C ANISOU 1410 CE MET A 179 7655 7787 6949 -631 -777 -248 C ATOM 1411 N PRO A 180 -2.477 36.559 -12.844 1.00 51.19 N ANISOU 1411 N PRO A 180 6683 6408 6359 -398 -608 -285 N ATOM 1412 CA PRO A 180 -1.540 36.929 -11.774 1.00 51.59 C ANISOU 1412 CA PRO A 180 6747 6406 6447 -388 -559 -367 C ATOM 1413 C PRO A 180 -0.169 37.197 -12.341 1.00 46.99 C ANISOU 1413 C PRO A 180 6192 5843 5820 -489 -531 -382 C ATOM 1414 O PRO A 180 0.094 36.848 -13.494 1.00 50.37 O ANISOU 1414 O PRO A 180 6624 6346 6167 -560 -529 -348 O ATOM 1415 CB PRO A 180 -1.481 35.676 -10.904 1.00 44.18 C ANISOU 1415 CB PRO A 180 5758 5525 5504 -347 -530 -453 C ATOM 1416 CG PRO A 180 -2.747 34.952 -11.212 1.00 55.17 C ANISOU 1416 CG PRO A 180 7108 6952 6904 -307 -562 -407 C ATOM 1417 CD PRO A 180 -3.005 35.201 -12.660 1.00 45.44 C ANISOU 1417 CD PRO A 180 5897 5749 5619 -371 -611 -331 C ATOM 1418 N ALA A 181 0.697 37.796 -11.533 1.00 46.70 N ANISOU 1418 N ALA A 181 6168 5746 5829 -500 -508 -439 N ATOM 1419 CA ALA A 181 2.052 38.110 -11.969 1.00 49.28 C ANISOU 1419 CA ALA A 181 6500 6087 6139 -601 -478 -450 C ATOM 1420 C ALA A 181 2.910 36.842 -11.985 1.00 49.53 C ANISOU 1420 C ALA A 181 6474 6226 6118 -627 -437 -530 C ATOM 1421 O ALA A 181 3.109 36.192 -10.958 1.00 40.10 O ANISOU 1421 O ALA A 181 5243 5046 4947 -577 -434 -608 O ATOM 1422 CB ALA A 181 2.658 39.180 -11.084 1.00 49.82 C ANISOU 1422 CB ALA A 181 6590 6047 6291 -612 -482 -490 C ATOM 1423 N LEU A 182 3.397 36.498 -13.174 1.00 53.52 N ANISOU 1423 N LEU A 182 6972 6810 6552 -701 -403 -504 N ATOM 1424 CA LEU A 182 4.116 35.248 -13.401 1.00 52.29 C ANISOU 1424 CA LEU A 182 6760 6750 6358 -717 -354 -584 C ATOM 1425 C LEU A 182 5.574 35.439 -13.842 1.00 51.29 C ANISOU 1425 C LEU A 182 6598 6664 6225 -806 -288 -603 C ATOM 1426 O LEU A 182 5.895 36.355 -14.615 1.00 43.78 O ANISOU 1426 O LEU A 182 5679 5708 5247 -884 -268 -526 O ATOM 1427 CB LEU A 182 3.376 34.385 -14.437 1.00 51.61 C ANISOU 1427 CB LEU A 182 6683 6741 6184 -718 -356 -577 C ATOM 1428 CG LEU A 182 1.951 33.936 -14.114 1.00 42.38 C ANISOU 1428 CG LEU A 182 5519 5550 5032 -640 -418 -561 C ATOM 1429 CD1 LEU A 182 1.552 32.783 -15.014 1.00 41.37 C ANISOU 1429 CD1 LEU A 182 5379 5504 4835 -656 -420 -600 C ATOM 1430 CD2 LEU A 182 1.862 33.536 -12.661 1.00 40.21 C ANISOU 1430 CD2 LEU A 182 5205 5228 4846 -560 -424 -612 C ATOM 1431 N ALA A 183 6.443 34.556 -13.344 1.00 57.09 N ANISOU 1431 N ALA A 183 7258 7438 6997 -791 -253 -692 N ATOM 1432 CA ALA A 183 7.854 34.501 -13.753 1.00 49.34 C ANISOU 1432 CA ALA A 183 6212 6510 6026 -864 -179 -721 C ATOM 1433 C ALA A 183 7.957 34.289 -15.261 1.00 52.60 C ANISOU 1433 C ALA A 183 6642 7015 6330 -926 -104 -699 C ATOM 1434 O ALA A 183 7.218 33.497 -15.831 1.00 59.76 O ANISOU 1434 O ALA A 183 7576 7968 7161 -896 -105 -725 O ATOM 1435 CB ALA A 183 8.578 33.398 -13.007 1.00 38.76 C ANISOU 1435 CB ALA A 183 4777 5197 4754 -814 -163 -813 C ATOM 1436 N PRO A 184 8.864 35.014 -15.919 1.00 60.86 N ANISOU 1436 N PRO A 184 7673 8093 7358 -1021 -40 -650 N ATOM 1437 CA PRO A 184 8.956 34.927 -17.384 1.00 73.05 C ANISOU 1437 CA PRO A 184 9245 9746 8764 -1088 41 -616 C ATOM 1438 C PRO A 184 9.228 33.494 -17.869 1.00 71.92 C ANISOU 1438 C PRO A 184 9055 9702 8568 -1055 116 -743 C ATOM 1439 O PRO A 184 10.081 32.805 -17.301 1.00 67.42 O ANISOU 1439 O PRO A 184 8388 9132 8097 -1021 158 -833 O ATOM 1440 CB PRO A 184 10.139 35.853 -17.715 1.00 74.28 C ANISOU 1440 CB PRO A 184 9359 9916 8950 -1194 115 -548 C ATOM 1441 CG PRO A 184 10.243 36.776 -16.531 1.00 69.52 C ANISOU 1441 CG PRO A 184 8748 9175 8492 -1191 31 -518 C ATOM 1442 CD PRO A 184 9.859 35.940 -15.350 1.00 64.31 C ANISOU 1442 CD PRO A 184 8062 8474 7898 -1080 -37 -623 C ATOM 1443 N PRO A 185 8.508 33.050 -18.914 1.00 66.97 N ANISOU 1443 N PRO A 185 8496 9156 7795 -1064 126 -753 N ATOM 1444 CA PRO A 185 8.639 31.673 -19.411 1.00 65.96 C ANISOU 1444 CA PRO A 185 8338 9103 7621 -1031 191 -898 C ATOM 1445 C PRO A 185 10.076 31.360 -19.787 1.00 70.84 C ANISOU 1445 C PRO A 185 8864 9797 8255 -1064 338 -969 C ATOM 1446 O PRO A 185 10.591 31.923 -20.751 1.00 73.65 O ANISOU 1446 O PRO A 185 9236 10252 8497 -1150 428 -917 O ATOM 1447 CB PRO A 185 7.750 31.659 -20.660 1.00 61.44 C ANISOU 1447 CB PRO A 185 7868 8625 6853 -1074 173 -873 C ATOM 1448 CG PRO A 185 6.752 32.764 -20.427 1.00 54.72 C ANISOU 1448 CG PRO A 185 7088 7705 5997 -1082 52 -715 C ATOM 1449 CD PRO A 185 7.535 33.833 -19.698 1.00 58.83 C ANISOU 1449 CD PRO A 185 7569 8145 6637 -1107 66 -629 C ATOM 1450 N GLU A 186 10.707 30.474 -19.023 1.00 70.49 N ANISOU 1450 N GLU A 186 8717 9709 8358 -995 364 -1074 N ATOM 1451 CA GLU A 186 12.111 30.125 -19.207 1.00 67.44 C ANISOU 1451 CA GLU A 186 8211 9379 8034 -1006 499 -1143 C ATOM 1452 C GLU A 186 12.353 29.256 -20.448 1.00 70.77 C ANISOU 1452 C GLU A 186 8637 9917 8336 -1014 634 -1268 C ATOM 1453 O GLU A 186 13.466 29.207 -20.969 1.00 72.41 O ANISOU 1453 O GLU A 186 8761 10210 8543 -1045 780 -1307 O ATOM 1454 CB GLU A 186 12.636 29.467 -17.932 1.00 72.56 C ANISOU 1454 CB GLU A 186 8744 9937 8889 -919 461 -1196 C ATOM 1455 CG GLU A 186 12.175 30.215 -16.680 1.00 80.48 C ANISOU 1455 CG GLU A 186 9771 10837 9972 -904 316 -1098 C ATOM 1456 CD GLU A 186 12.712 29.631 -15.380 1.00 89.33 C ANISOU 1456 CD GLU A 186 10783 11890 11266 -826 264 -1131 C ATOM 1457 OE1 GLU A 186 13.369 28.564 -15.424 1.00 92.82 O ANISOU 1457 OE1 GLU A 186 11126 12348 11795 -772 331 -1220 O ATOM 1458 OE2 GLU A 186 12.470 30.249 -14.314 1.00 83.33 O ANISOU 1458 OE2 GLU A 186 10039 11065 10556 -817 156 -1067 O ATOM 1459 N VAL A 187 11.305 28.574 -20.908 1.00 77.62 N ANISOU 1459 N VAL A 187 9596 10792 9105 -987 587 -1339 N ATOM 1460 CA VAL A 187 11.289 27.934 -22.225 1.00 85.59 C ANISOU 1460 CA VAL A 187 10652 11924 9942 -1014 692 -1461 C ATOM 1461 C VAL A 187 10.020 28.349 -22.987 1.00 91.34 C ANISOU 1461 C VAL A 187 11530 12710 10464 -1070 597 -1396 C ATOM 1462 O VAL A 187 9.031 28.782 -22.388 1.00 90.70 O ANISOU 1462 O VAL A 187 11500 12544 10420 -1055 447 -1294 O ATOM 1463 CB VAL A 187 11.376 26.373 -22.159 1.00 64.47 C ANISOU 1463 CB VAL A 187 7925 9202 7368 -924 735 -1667 C ATOM 1464 CG1 VAL A 187 12.586 25.920 -21.342 1.00 66.61 C ANISOU 1464 CG1 VAL A 187 8034 9407 7868 -854 810 -1711 C ATOM 1465 CG2 VAL A 187 10.100 25.778 -21.598 1.00 59.88 C ANISOU 1465 CG2 VAL A 187 7400 8507 6844 -871 579 -1684 C ATOM 1466 N VAL A 188 10.064 28.213 -24.309 1.00 88.86 N ANISOU 1466 N VAL A 188 11281 12551 9931 -1131 685 -1457 N ATOM 1467 CA VAL A 188 8.949 28.570 -25.172 1.00 86.07 C ANISOU 1467 CA VAL A 188 11063 12283 9355 -1192 592 -1395 C ATOM 1468 C VAL A 188 7.977 27.404 -25.312 1.00 97.33 C ANISOU 1468 C VAL A 188 12535 13678 10768 -1148 507 -1554 C ATOM 1469 O VAL A 188 8.385 26.241 -25.291 1.00106.52 O ANISOU 1469 O VAL A 188 13647 14812 12012 -1095 583 -1752 O ATOM 1470 CB VAL A 188 9.455 28.937 -26.575 1.00 81.22 C ANISOU 1470 CB VAL A 188 10505 11877 8476 -1288 725 -1385 C ATOM 1471 CG1 VAL A 188 8.293 29.262 -27.513 1.00 69.43 C ANISOU 1471 CG1 VAL A 188 9154 10492 6734 -1354 610 -1313 C ATOM 1472 CG2 VAL A 188 10.448 30.090 -26.489 1.00 89.11 C ANISOU 1472 CG2 VAL A 188 11449 12904 9505 -1347 819 -1215 C ATOM 1473 N MET A 189 6.692 27.715 -25.454 1.00 86.54 N ANISOU 1473 N MET A 189 11255 12307 9320 -1171 345 -1465 N ATOM 1474 CA MET A 189 5.702 26.699 -25.754 1.00 78.38 C ANISOU 1474 CA MET A 189 10268 11263 8252 -1157 252 -1605 C ATOM 1475 C MET A 189 5.208 26.893 -27.183 1.00 84.68 C ANISOU 1475 C MET A 189 11182 12251 8741 -1251 228 -1611 C ATOM 1476 O MET A 189 4.365 27.745 -27.442 1.00 96.77 O ANISOU 1476 O MET A 189 12777 13826 10167 -1296 101 -1436 O ATOM 1477 CB MET A 189 4.539 26.778 -24.765 1.00 81.43 C ANISOU 1477 CB MET A 189 10641 11501 8798 -1108 75 -1506 C ATOM 1478 CG MET A 189 3.473 25.705 -24.970 1.00 80.38 C ANISOU 1478 CG MET A 189 10534 11337 8672 -1100 -32 -1638 C ATOM 1479 SD MET A 189 4.058 24.055 -24.536 1.00 77.69 S ANISOU 1479 SD MET A 189 10113 10877 8530 -1026 59 -1891 S ATOM 1480 CE MET A 189 3.413 23.093 -25.904 1.00 98.66 C ANISOU 1480 CE MET A 189 12858 13636 10991 -1095 23 -2109 C ATOM 1481 N ASP A 190 5.748 26.109 -28.111 1.00 82.58 N ANISOU 1481 N ASP A 190 10943 12105 8329 -1277 351 -1813 N ATOM 1482 CA ASP A 190 5.379 26.210 -29.521 1.00 86.42 C ANISOU 1482 CA ASP A 190 11548 12804 8482 -1372 340 -1845 C ATOM 1483 C ASP A 190 3.861 26.268 -29.697 1.00 97.29 C ANISOU 1483 C ASP A 190 12996 14180 9791 -1403 109 -1777 C ATOM 1484 O ASP A 190 3.140 25.435 -29.155 1.00102.08 O ANISOU 1484 O ASP A 190 13572 14653 10562 -1358 5 -1881 O ATOM 1485 CB ASP A 190 5.953 25.021 -30.297 1.00 83.45 C ANISOU 1485 CB ASP A 190 11188 12514 8005 -1372 483 -2145 C ATOM 1486 CG ASP A 190 5.758 25.149 -31.804 1.00 93.75 C ANISOU 1486 CG ASP A 190 12623 14076 8920 -1477 501 -2195 C ATOM 1487 OD1 ASP A 190 5.598 26.288 -32.299 1.00 95.13 O ANISOU 1487 OD1 ASP A 190 12858 14386 8899 -1551 464 -1964 O ATOM 1488 OD2 ASP A 190 5.773 24.105 -32.497 1.00 96.02 O ANISOU 1488 OD2 ASP A 190 12956 14431 9095 -1485 553 -2466 O ATOM 1489 N PRO A 191 3.366 27.267 -30.442 1.00101.27 N ANISOU 1489 N PRO A 191 13583 14828 10065 -1482 26 -1584 N ATOM 1490 CA PRO A 191 1.930 27.327 -30.743 1.00103.11 C ANISOU 1490 CA PRO A 191 13873 15086 10218 -1516 -200 -1514 C ATOM 1491 C PRO A 191 1.440 26.125 -31.555 1.00105.83 C ANISOU 1491 C PRO A 191 14276 15520 10414 -1557 -251 -1774 C ATOM 1492 O PRO A 191 0.247 25.817 -31.527 1.00102.88 O ANISOU 1492 O PRO A 191 13910 15109 10071 -1569 -444 -1777 O ATOM 1493 CB PRO A 191 1.801 28.611 -31.562 1.00107.10 C ANISOU 1493 CB PRO A 191 14456 15759 10477 -1597 -240 -1262 C ATOM 1494 CG PRO A 191 2.940 29.456 -31.109 1.00107.94 C ANISOU 1494 CG PRO A 191 14513 15822 10678 -1580 -78 -1128 C ATOM 1495 CD PRO A 191 4.066 28.502 -30.834 1.00103.87 C ANISOU 1495 CD PRO A 191 13935 15269 10263 -1536 119 -1373 C ATOM 1496 N ALA A 192 2.343 25.463 -32.274 1.00111.45 N ANISOU 1496 N ALA A 192 15024 16347 10977 -1580 -78 -1996 N ATOM 1497 CA ALA A 192 1.989 24.261 -33.027 1.00110.02 C ANISOU 1497 CA ALA A 192 14903 16233 10667 -1617 -107 -2289 C ATOM 1498 C ALA A 192 1.645 23.121 -32.073 1.00106.84 C ANISOU 1498 C ALA A 192 14414 15584 10597 -1539 -156 -2462 C ATOM 1499 O ALA A 192 0.522 22.612 -32.086 1.00110.60 O ANISOU 1499 O ALA A 192 14901 16009 11112 -1564 -342 -2516 O ATOM 1500 CB ALA A 192 3.117 23.856 -33.959 1.00107.46 C ANISOU 1500 CB ALA A 192 14630 16080 10119 -1645 120 -2498 C ATOM 1501 N LEU A 193 2.614 22.733 -31.246 1.00 99.39 N ANISOU 1501 N LEU A 193 13375 14489 9901 -1447 7 -2533 N ATOM 1502 CA LEU A 193 2.393 21.721 -30.217 1.00100.12 C ANISOU 1502 CA LEU A 193 13374 14334 10334 -1365 -28 -2649 C ATOM 1503 C LEU A 193 1.136 22.005 -29.395 1.00 93.71 C ANISOU 1503 C LEU A 193 12522 13393 9689 -1354 -242 -2463 C ATOM 1504 O LEU A 193 0.282 21.134 -29.237 1.00 99.05 O ANISOU 1504 O LEU A 193 13183 13966 10484 -1359 -364 -2574 O ATOM 1505 CB LEU A 193 3.603 21.617 -29.288 1.00101.40 C ANISOU 1505 CB LEU A 193 13426 14363 10740 -1264 150 -2648 C ATOM 1506 CG LEU A 193 4.853 20.976 -29.883 1.00107.79 C ANISOU 1506 CG LEU A 193 14228 15236 11492 -1243 377 -2883 C ATOM 1507 CD1 LEU A 193 5.957 20.879 -28.833 1.00112.30 C ANISOU 1507 CD1 LEU A 193 14663 15660 12348 -1138 517 -2850 C ATOM 1508 CD2 LEU A 193 4.521 19.607 -30.461 1.00105.34 C ANISOU 1508 CD2 LEU A 193 13959 14887 11177 -1252 367 -3201 C ATOM 1509 N ALA A 194 1.028 23.223 -28.872 1.00 82.35 N ANISOU 1509 N ALA A 194 11061 11956 8271 -1339 -281 -2185 N ATOM 1510 CA ALA A 194 -0.140 23.618 -28.091 1.00 77.57 C ANISOU 1510 CA ALA A 194 10413 11242 7817 -1319 -463 -1999 C ATOM 1511 C ALA A 194 -1.431 23.372 -28.862 1.00 77.49 C ANISOU 1511 C ALA A 194 10458 11316 7671 -1398 -658 -2026 C ATOM 1512 O ALA A 194 -2.423 22.930 -28.286 1.00 81.31 O ANISOU 1512 O ALA A 194 10883 11675 8337 -1382 -794 -2013 O ATOM 1513 CB ALA A 194 -0.042 25.076 -27.676 1.00 73.04 C ANISOU 1513 CB ALA A 194 9831 10685 7235 -1303 -469 -1716 C ATOM 1514 N ALA A 195 -1.410 23.648 -30.164 1.00 75.07 N ANISOU 1514 N ALA A 195 10257 11228 7039 -1489 -673 -2059 N ATOM 1515 CA ALA A 195 -2.591 23.465 -31.004 1.00 79.70 C ANISOU 1515 CA ALA A 195 10900 11926 7456 -1578 -875 -2083 C ATOM 1516 C ALA A 195 -2.882 21.987 -31.301 1.00 84.18 C ANISOU 1516 C ALA A 195 11473 12441 8070 -1610 -911 -2396 C ATOM 1517 O ALA A 195 -4.026 21.537 -31.219 1.00 82.86 O ANISOU 1517 O ALA A 195 11274 12215 7994 -1643 -1097 -2413 O ATOM 1518 CB ALA A 195 -2.454 24.256 -32.289 1.00 74.53 C ANISOU 1518 CB ALA A 195 10362 11538 6417 -1669 -887 -2002 C ATOM 1519 N GLN A 196 -1.848 21.233 -31.647 1.00 88.92 N ANISOU 1519 N GLN A 196 12107 13052 8626 -1600 -729 -2645 N ATOM 1520 CA GLN A 196 -2.014 19.802 -31.843 1.00 97.87 C ANISOU 1520 CA GLN A 196 13242 14093 9850 -1618 -742 -2960 C ATOM 1521 C GLN A 196 -2.466 19.140 -30.542 1.00 92.67 C ANISOU 1521 C GLN A 196 12456 13152 9601 -1543 -793 -2940 C ATOM 1522 O GLN A 196 -3.390 18.337 -30.547 1.00 94.56 O ANISOU 1522 O GLN A 196 12675 13303 9951 -1586 -940 -3048 O ATOM 1523 CB GLN A 196 -0.719 19.167 -32.371 1.00106.47 C ANISOU 1523 CB GLN A 196 14377 15228 10851 -1597 -508 -3227 C ATOM 1524 CG GLN A 196 -0.775 17.647 -32.569 1.00116.58 C ANISOU 1524 CG GLN A 196 15660 16379 12255 -1602 -497 -3582 C ATOM 1525 CD GLN A 196 -1.745 17.206 -33.663 1.00129.82 C ANISOU 1525 CD GLN A 196 17439 18190 13698 -1730 -679 -3756 C ATOM 1526 OE1 GLN A 196 -2.511 18.009 -34.199 1.00131.23 O ANISOU 1526 OE1 GLN A 196 17672 18551 13640 -1812 -842 -3585 O ATOM 1527 NE2 GLN A 196 -1.716 15.915 -33.992 1.00134.94 N ANISOU 1527 NE2 GLN A 196 18110 18740 14422 -1749 -659 -4100 N ATOM 1528 N TYR A 197 -1.826 19.495 -29.430 1.00 89.36 N ANISOU 1528 N TYR A 197 11952 12601 9401 -1439 -678 -2793 N ATOM 1529 CA TYR A 197 -2.122 18.882 -28.133 1.00 89.61 C ANISOU 1529 CA TYR A 197 11865 12380 9804 -1361 -702 -2757 C ATOM 1530 C TYR A 197 -3.509 19.236 -27.613 1.00 89.47 C ANISOU 1530 C TYR A 197 11793 12312 9890 -1381 -905 -2558 C ATOM 1531 O TYR A 197 -4.164 18.411 -26.974 1.00 88.75 O ANISOU 1531 O TYR A 197 11624 12050 10048 -1370 -979 -2594 O ATOM 1532 CB TYR A 197 -1.083 19.274 -27.077 1.00 92.11 C ANISOU 1532 CB TYR A 197 12108 12598 10290 -1250 -542 -2635 C ATOM 1533 CG TYR A 197 0.256 18.577 -27.200 1.00104.13 C ANISOU 1533 CG TYR A 197 13623 14085 11858 -1199 -339 -2841 C ATOM 1534 CD1 TYR A 197 0.337 17.198 -27.348 1.00114.46 C ANISOU 1534 CD1 TYR A 197 14918 15266 13307 -1191 -310 -3104 C ATOM 1535 CD2 TYR A 197 1.444 19.298 -27.136 1.00107.62 C ANISOU 1535 CD2 TYR A 197 14058 14604 12230 -1157 -175 -2768 C ATOM 1536 CE1 TYR A 197 1.564 16.558 -27.451 1.00113.57 C ANISOU 1536 CE1 TYR A 197 14783 15106 13261 -1128 -117 -3292 C ATOM 1537 CE2 TYR A 197 2.674 18.666 -27.238 1.00110.33 C ANISOU 1537 CE2 TYR A 197 14370 14916 12634 -1103 15 -2949 C ATOM 1538 CZ TYR A 197 2.726 17.296 -27.395 1.00109.75 C ANISOU 1538 CZ TYR A 197 14283 14718 12701 -1082 46 -3211 C ATOM 1539 OH TYR A 197 3.942 16.664 -27.494 1.00110.44 O ANISOU 1539 OH TYR A 197 14327 14763 12872 -1014 240 -3391 O ATOM 1540 N GLU A 198 -3.944 20.468 -27.862 1.00 90.33 N ANISOU 1540 N GLU A 198 11931 12562 9828 -1407 -986 -2336 N ATOM 1541 CA GLU A 198 -5.280 20.889 -27.457 1.00 98.88 C ANISOU 1541 CA GLU A 198 12954 13615 11003 -1419 -1174 -2142 C ATOM 1542 C GLU A 198 -6.320 20.163 -28.301 1.00103.81 C ANISOU 1542 C GLU A 198 13597 14291 11554 -1526 -1356 -2280 C ATOM 1543 O GLU A 198 -7.386 19.778 -27.817 1.00109.39 O ANISOU 1543 O GLU A 198 14215 14892 12456 -1537 -1493 -2232 O ATOM 1544 CB GLU A 198 -5.448 22.398 -27.619 1.00108.22 C ANISOU 1544 CB GLU A 198 14165 14928 12025 -1415 -1216 -1878 C ATOM 1545 CG GLU A 198 -4.793 23.234 -26.534 1.00121.39 C ANISOU 1545 CG GLU A 198 15786 16506 13832 -1313 -1093 -1699 C ATOM 1546 CD GLU A 198 -5.180 24.706 -26.630 1.00132.68 C ANISOU 1546 CD GLU A 198 17233 18022 15157 -1310 -1161 -1433 C ATOM 1547 OE1 GLU A 198 -6.346 24.987 -26.991 1.00136.64 O ANISOU 1547 OE1 GLU A 198 17722 18578 15619 -1349 -1338 -1330 O ATOM 1548 OE2 GLU A 198 -4.326 25.579 -26.346 1.00131.11 O ANISOU 1548 OE2 GLU A 198 17053 17828 14933 -1269 -1044 -1325 O ATOM 1549 N HIS A 199 -5.990 19.982 -29.573 1.00 99.85 N ANISOU 1549 N HIS A 199 13211 13963 10764 -1610 -1354 -2455 N ATOM 1550 CA HIS A 199 -6.845 19.271 -30.509 1.00 95.39 C ANISOU 1550 CA HIS A 199 12686 13474 10084 -1726 -1527 -2629 C ATOM 1551 C HIS A 199 -6.892 17.780 -30.199 1.00 89.47 C ANISOU 1551 C HIS A 199 11890 12524 9579 -1733 -1512 -2893 C ATOM 1552 O HIS A 199 -7.917 17.138 -30.365 1.00 91.59 O ANISOU 1552 O HIS A 199 12121 12746 9934 -1810 -1688 -2968 O ATOM 1553 CB HIS A 199 -6.337 19.496 -31.931 1.00102.72 C ANISOU 1553 CB HIS A 199 13764 14659 10605 -1809 -1501 -2758 C ATOM 1554 CG HIS A 199 -7.166 18.836 -32.981 1.00109.60 C ANISOU 1554 CG HIS A 199 14695 15643 11303 -1939 -1691 -2952 C ATOM 1555 ND1 HIS A 199 -6.749 17.706 -33.656 1.00115.48 N ANISOU 1555 ND1 HIS A 199 15516 16392 11970 -1993 -1634 -3312 N ATOM 1556 CD2 HIS A 199 -8.387 19.140 -33.479 1.00117.25 C ANISOU 1556 CD2 HIS A 199 15655 16726 12166 -2029 -1944 -2845 C ATOM 1557 CE1 HIS A 199 -7.676 17.347 -34.521 1.00125.36 C ANISOU 1557 CE1 HIS A 199 16812 17757 13061 -2119 -1848 -3429 C ATOM 1558 NE2 HIS A 199 -8.685 18.201 -34.433 1.00126.67 N ANISOU 1558 NE2 HIS A 199 16923 17998 13208 -2145 -2046 -3141 N ATOM 1559 N ASP A 200 -5.770 17.234 -29.746 1.00 88.59 N ANISOU 1559 N ASP A 200 11774 12288 9598 -1653 -1305 -3024 N ATOM 1560 CA ASP A 200 -5.681 15.820 -29.403 1.00 85.69 C ANISOU 1560 CA ASP A 200 11361 11702 9496 -1644 -1270 -3262 C ATOM 1561 C ASP A 200 -6.423 15.533 -28.107 1.00 85.30 C ANISOU 1561 C ASP A 200 11167 11429 9814 -1596 -1339 -3094 C ATOM 1562 O ASP A 200 -6.614 14.380 -27.734 1.00 81.55 O ANISOU 1562 O ASP A 200 10634 10751 9598 -1601 -1350 -3237 O ATOM 1563 CB ASP A 200 -4.218 15.390 -29.266 1.00 85.44 C ANISOU 1563 CB ASP A 200 11351 11603 9511 -1556 -1023 -3421 C ATOM 1564 CG ASP A 200 -3.511 15.271 -30.607 1.00101.23 C ANISOU 1564 CG ASP A 200 13485 13795 11183 -1611 -933 -3673 C ATOM 1565 OD1 ASP A 200 -4.200 15.285 -31.653 1.00108.79 O ANISOU 1565 OD1 ASP A 200 14530 14919 11888 -1728 -1077 -3770 O ATOM 1566 OD2 ASP A 200 -2.263 15.156 -30.613 1.00104.07 O ANISOU 1566 OD2 ASP A 200 13859 14150 11534 -1537 -717 -3774 O ATOM 1567 N LEU A 201 -6.825 16.593 -27.416 1.00 88.91 N ANISOU 1567 N LEU A 201 11566 11920 10296 -1549 -1377 -2789 N ATOM 1568 CA LEU A 201 -7.573 16.456 -26.174 1.00 85.58 C ANISOU 1568 CA LEU A 201 11008 11321 10187 -1501 -1431 -2607 C ATOM 1569 C LEU A 201 -9.069 16.425 -26.446 1.00 89.02 C ANISOU 1569 C LEU A 201 11388 11787 10649 -1595 -1659 -2541 C ATOM 1570 O LEU A 201 -9.808 15.665 -25.822 1.00 93.95 O ANISOU 1570 O LEU A 201 11905 12246 11546 -1611 -1727 -2533 O ATOM 1571 CB LEU A 201 -7.236 17.600 -25.219 1.00 80.89 C ANISOU 1571 CB LEU A 201 10375 10739 9620 -1393 -1343 -2333 C ATOM 1572 CG LEU A 201 -6.222 17.296 -24.118 1.00 78.30 C ANISOU 1572 CG LEU A 201 10001 10256 9495 -1279 -1163 -2317 C ATOM 1573 CD1 LEU A 201 -6.066 18.515 -23.215 1.00 75.48 C ANISOU 1573 CD1 LEU A 201 9609 9927 9141 -1191 -1113 -2053 C ATOM 1574 CD2 LEU A 201 -6.670 16.084 -23.314 1.00 73.86 C ANISOU 1574 CD2 LEU A 201 9337 9472 9256 -1268 -1185 -2362 C ATOM 1575 N GLU A 202 -9.503 17.261 -27.383 1.00 89.14 N ANISOU 1575 N GLU A 202 11467 12018 10384 -1661 -1778 -2481 N ATOM 1576 CA GLU A 202 -10.901 17.310 -27.793 1.00 98.12 C ANISOU 1576 CA GLU A 202 12548 13218 11515 -1756 -2015 -2415 C ATOM 1577 C GLU A 202 -11.308 16.043 -28.536 1.00101.54 C ANISOU 1577 C GLU A 202 12999 13610 11970 -1881 -2130 -2702 C ATOM 1578 O GLU A 202 -12.293 15.393 -28.180 1.00105.66 O ANISOU 1578 O GLU A 202 13407 14007 12732 -1934 -2259 -2697 O ATOM 1579 CB GLU A 202 -11.150 18.536 -28.668 1.00105.77 C ANISOU 1579 CB GLU A 202 13588 14436 12163 -1790 -2115 -2269 C ATOM 1580 CG GLU A 202 -11.356 19.806 -27.871 1.00115.42 C ANISOU 1580 CG GLU A 202 14745 15665 13446 -1688 -2089 -1944 C ATOM 1581 CD GLU A 202 -10.803 21.031 -28.570 1.00124.97 C ANISOU 1581 CD GLU A 202 16065 17072 14347 -1678 -2058 -1826 C ATOM 1582 OE1 GLU A 202 -11.199 21.291 -29.730 1.00129.00 O ANISOU 1582 OE1 GLU A 202 16645 17775 14596 -1773 -2204 -1840 O ATOM 1583 OE2 GLU A 202 -9.970 21.733 -27.952 1.00122.39 O ANISOU 1583 OE2 GLU A 202 15754 16709 14041 -1580 -1892 -1711 O ATOM 1584 N VAL A 203 -10.536 15.698 -29.563 1.00100.66 N ANISOU 1584 N VAL A 203 13030 13602 11614 -1931 -2075 -2959 N ATOM 1585 CA VAL A 203 -10.776 14.498 -30.362 1.00104.31 C ANISOU 1585 CA VAL A 203 13538 14030 12067 -2049 -2168 -3284 C ATOM 1586 C VAL A 203 -10.611 13.224 -29.531 1.00108.48 C ANISOU 1586 C VAL A 203 13984 14255 12980 -2019 -2085 -3426 C ATOM 1587 O VAL A 203 -10.552 12.115 -30.063 1.00120.06 O ANISOU 1587 O VAL A 203 15491 15632 14492 -2094 -2110 -3730 O ATOM 1588 CB VAL A 203 -9.886 14.479 -31.625 1.00101.10 C ANISOU 1588 CB VAL A 203 13310 13818 11286 -2094 -2092 -3534 C ATOM 1589 CG1 VAL A 203 -9.965 13.145 -32.345 1.00 97.73 C ANISOU 1589 CG1 VAL A 203 12939 13319 10874 -2198 -2147 -3920 C ATOM 1590 CG2 VAL A 203 -10.303 15.600 -32.561 1.00104.78 C ANISOU 1590 CG2 VAL A 203 13852 14587 11372 -2158 -2229 -3387 C ATOM 1591 N ALA A 204 -10.550 13.390 -28.215 1.00 99.26 N ANISOU 1591 N ALA A 204 12700 12925 12089 -1908 -1990 -3201 N ATOM 1592 CA ALA A 204 -10.563 12.249 -27.314 1.00 96.47 C ANISOU 1592 CA ALA A 204 12248 12285 12123 -1881 -1936 -3263 C ATOM 1593 C ALA A 204 -11.798 12.261 -26.424 1.00102.26 C ANISOU 1593 C ALA A 204 12815 12914 13125 -1899 -2062 -3023 C ATOM 1594 O ALA A 204 -12.366 11.212 -26.127 1.00 99.93 O ANISOU 1594 O ALA A 204 12433 12424 13111 -1960 -2129 -3101 O ATOM 1595 CB ALA A 204 -9.307 12.217 -26.473 1.00 84.22 C ANISOU 1595 CB ALA A 204 10698 10617 10683 -1735 -1696 -3227 C ATOM 1596 N GLN A 205 -12.209 13.450 -25.997 1.00109.59 N ANISOU 1596 N GLN A 205 13695 13967 13977 -1844 -2086 -2731 N ATOM 1597 CA GLN A 205 -13.361 13.581 -25.110 1.00115.88 C ANISOU 1597 CA GLN A 205 14324 14687 15016 -1842 -2178 -2487 C ATOM 1598 C GLN A 205 -14.672 13.214 -25.799 1.00116.59 C ANISOU 1598 C GLN A 205 14347 14817 15136 -1994 -2425 -2538 C ATOM 1599 O GLN A 205 -15.659 12.904 -25.131 1.00117.08 O ANISOU 1599 O GLN A 205 14249 14768 15467 -2021 -2503 -2402 O ATOM 1600 CB GLN A 205 -13.450 14.997 -24.530 1.00120.55 C ANISOU 1600 CB GLN A 205 14887 15403 15515 -1737 -2134 -2185 C ATOM 1601 CG GLN A 205 -12.834 15.151 -23.142 1.00122.88 C ANISOU 1601 CG GLN A 205 15131 15568 15990 -1595 -1940 -2026 C ATOM 1602 CD GLN A 205 -13.657 14.484 -22.042 1.00125.20 C ANISOU 1602 CD GLN A 205 15259 15681 16630 -1590 -1952 -1900 C ATOM 1603 OE1 GLN A 205 -13.414 14.709 -20.855 1.00121.39 O ANISOU 1603 OE1 GLN A 205 14719 15123 16279 -1482 -1823 -1728 O ATOM 1604 NE2 GLN A 205 -14.634 13.661 -22.433 1.00122.42 N ANISOU 1604 NE2 GLN A 205 14828 15265 16421 -1715 -2109 -1981 N ATOM 1605 N THR A 206 -14.669 13.246 -27.132 1.00118.53 N ANISOU 1605 N THR A 206 14709 15229 15099 -2096 -2545 -2732 N ATOM 1606 CA THR A 206 -15.857 12.951 -27.936 1.00124.43 C ANISOU 1606 CA THR A 206 15405 16049 15822 -2254 -2807 -2802 C ATOM 1607 C THR A 206 -15.822 11.572 -28.595 1.00130.01 C ANISOU 1607 C THR A 206 16160 16635 16601 -2383 -2876 -3157 C ATOM 1608 O THR A 206 -16.552 11.322 -29.557 1.00130.96 O ANISOU 1608 O THR A 206 16294 16859 16606 -2531 -3095 -3297 O ATOM 1609 CB THR A 206 -16.050 14.012 -29.044 1.00123.47 C ANISOU 1609 CB THR A 206 15378 16231 15305 -2296 -2942 -2753 C ATOM 1610 OG1 THR A 206 -15.042 13.848 -30.050 1.00125.90 O ANISOU 1610 OG1 THR A 206 15882 16652 15303 -2324 -2872 -3016 O ATOM 1611 CG2 THR A 206 -15.968 15.399 -28.459 1.00117.34 C ANISOU 1611 CG2 THR A 206 14571 15551 14460 -2163 -2861 -2424 C ATOM 1612 N THR A 207 -14.991 10.683 -28.056 1.00134.71 N ANISOU 1612 N THR A 207 16777 17007 17400 -2327 -2697 -3301 N ATOM 1613 CA THR A 207 -14.652 9.433 -28.729 1.00138.41 C ANISOU 1613 CA THR A 207 17326 17349 17914 -2420 -2711 -3677 C ATOM 1614 C THR A 207 -14.930 8.105 -27.969 1.00168.34 C ANISOU 1614 C THR A 207 20997 20800 22162 -2453 -2698 -3751 C ATOM 1615 O THR A 207 -15.798 7.329 -28.383 1.00166.45 O ANISOU 1615 O THR A 207 20703 20477 22062 -2605 -2886 -3896 O ATOM 1616 CB THR A 207 -13.199 9.516 -29.286 1.00125.42 C ANISOU 1616 CB THR A 207 15866 15782 16006 -2341 -2513 -3887 C ATOM 1617 OG1 THR A 207 -13.234 10.098 -30.599 1.00127.29 O ANISOU 1617 OG1 THR A 207 16239 16312 15813 -2422 -2621 -4007 O ATOM 1618 CG2 THR A 207 -12.555 8.138 -29.341 1.00124.53 C ANISOU 1618 CG2 THR A 207 15792 15420 16102 -2352 -2414 -4213 C ATOM 1619 N ALA A 208 -14.219 7.862 -26.866 1.00167.20 N ANISOU 1619 N ALA A 208 20809 20464 22254 -2318 -2490 -3638 N ATOM 1620 CA ALA A 208 -14.253 6.560 -26.177 1.00164.74 C ANISOU 1620 CA ALA A 208 20408 19820 22368 -2335 -2448 -3711 C ATOM 1621 C ALA A 208 -14.750 6.643 -24.728 1.00157.00 C ANISOU 1621 C ALA A 208 19248 18703 21702 -2266 -2396 -3355 C ATOM 1622 O ALA A 208 -14.536 5.713 -23.937 1.00151.43 O ANISOU 1622 O ALA A 208 18472 17728 21337 -2237 -2307 -3341 O ATOM 1623 CB ALA A 208 -12.872 5.852 -26.239 1.00 90.03 C ANISOU 1623 CB ALA A 208 11056 10205 12945 -2245 -2247 -3955 C TER 1624 ALA A 208 ATOM 1625 N SER B 661 -13.492 32.038 13.002 1.00227.69 N ANISOU 1625 N SER B 661 23635 42367 20511 9078 712 2349 N ATOM 1626 CA SER B 661 -12.317 31.215 12.744 1.00228.33 C ANISOU 1626 CA SER B 661 23672 42344 20740 8945 518 2338 C ATOM 1627 C SER B 661 -11.066 32.069 12.573 1.00228.28 C ANISOU 1627 C SER B 661 23763 42123 20850 8910 597 2134 C ATOM 1628 O SER B 661 -11.066 33.045 11.824 1.00230.66 O ANISOU 1628 O SER B 661 24151 42280 21209 9012 769 2056 O ATOM 1629 CB SER B 661 -12.530 30.353 11.497 1.00228.08 C ANISOU 1629 CB SER B 661 23563 42267 20830 9000 425 2501 C ATOM 1630 OG SER B 661 -12.668 31.157 10.339 1.00227.69 O ANISOU 1630 OG SER B 661 23568 42037 20905 9135 619 2466 O ATOM 1631 N TRP B 662 -10.001 31.694 13.272 1.00225.94 N ANISOU 1631 N TRP B 662 23462 41809 20574 8752 455 2048 N ATOM 1632 CA TRP B 662 -8.724 32.388 13.175 1.00224.40 C ANISOU 1632 CA TRP B 662 23358 41440 20463 8693 503 1868 C ATOM 1633 C TRP B 662 -7.810 31.646 12.207 1.00222.12 C ANISOU 1633 C TRP B 662 22994 41064 20338 8646 350 1856 C ATOM 1634 O TRP B 662 -8.148 30.561 11.735 1.00221.54 O ANISOU 1634 O TRP B 662 22807 41057 20311 8659 189 1990 O ATOM 1635 CB TRP B 662 -8.070 32.472 14.553 1.00224.41 C ANISOU 1635 CB TRP B 662 23410 41467 20389 8548 455 1774 C ATOM 1636 CG TRP B 662 -8.075 31.160 15.266 1.00223.32 C ANISOU 1636 CG TRP B 662 23165 41459 20227 8410 211 1849 C ATOM 1637 CD1 TRP B 662 -9.138 30.571 15.883 1.00224.04 C ANISOU 1637 CD1 TRP B 662 23187 41745 20193 8393 134 1979 C ATOM 1638 CD2 TRP B 662 -6.968 30.260 15.423 1.00221.37 C ANISOU 1638 CD2 TRP B 662 22878 41169 20065 8256 -19 1788 C ATOM 1639 NE1 TRP B 662 -8.762 29.364 16.420 1.00223.26 N ANISOU 1639 NE1 TRP B 662 23020 41716 20093 8222 -144 2007 N ATOM 1640 CE2 TRP B 662 -7.439 29.150 16.151 1.00221.01 C ANISOU 1640 CE2 TRP B 662 22754 41278 19942 8145 -244 1884 C ATOM 1641 CE3 TRP B 662 -5.630 30.289 15.021 1.00219.49 C ANISOU 1641 CE3 TRP B 662 22663 40792 19940 8196 -71 1650 C ATOM 1642 CZ2 TRP B 662 -6.614 28.076 16.486 1.00218.66 C ANISOU 1642 CZ2 TRP B 662 22418 40973 19689 7982 -532 1837 C ATOM 1643 CZ3 TRP B 662 -4.814 29.221 15.356 1.00217.08 C ANISOU 1643 CZ3 TRP B 662 22304 40496 19681 8052 -338 1601 C ATOM 1644 CH2 TRP B 662 -5.310 28.130 16.081 1.00216.79 C ANISOU 1644 CH2 TRP B 662 22206 40589 19577 7949 -571 1690 C ATOM 1645 N GLN B 663 -6.650 32.229 11.919 1.00220.54 N ANISOU 1645 N GLN B 663 22859 40731 20204 8591 385 1697 N ATOM 1646 CA GLN B 663 -5.718 31.645 10.960 1.00217.92 C ANISOU 1646 CA GLN B 663 22447 40339 20014 8551 247 1653 C ATOM 1647 C GLN B 663 -4.319 31.466 11.550 1.00218.42 C ANISOU 1647 C GLN B 663 22527 40382 20081 8398 124 1499 C ATOM 1648 O GLN B 663 -3.787 32.370 12.195 1.00214.59 O ANISOU 1648 O GLN B 663 22169 39842 19524 8339 240 1386 O ATOM 1649 CB GLN B 663 -5.655 32.511 9.699 1.00215.72 C ANISOU 1649 CB GLN B 663 22211 39935 19816 8628 399 1601 C ATOM 1650 CG GLN B 663 -4.677 32.026 8.645 1.00212.78 C ANISOU 1650 CG GLN B 663 21744 39519 19584 8583 270 1538 C ATOM 1651 CD GLN B 663 -4.376 33.090 7.606 1.00209.99 C ANISOU 1651 CD GLN B 663 21461 39043 19282 8593 415 1435 C ATOM 1652 OE1 GLN B 663 -3.376 33.012 6.892 1.00208.43 O ANISOU 1652 OE1 GLN B 663 21212 38825 19158 8521 335 1329 O ATOM 1653 NE2 GLN B 663 -5.238 34.096 7.523 1.00210.01 N ANISOU 1653 NE2 GLN B 663 21588 38977 19231 8673 611 1452 N ATOM 1654 N CYS B 664 -3.732 30.292 11.326 1.00223.70 N ANISOU 1654 N CYS B 664 23077 41094 20823 8342 -122 1497 N ATOM 1655 CA CYS B 664 -2.378 29.994 11.795 1.00229.89 C ANISOU 1655 CA CYS B 664 23866 41866 21617 8202 -267 1336 C ATOM 1656 C CYS B 664 -1.337 30.672 10.903 1.00231.87 C ANISOU 1656 C CYS B 664 24136 42047 21919 8189 -197 1187 C ATOM 1657 O CYS B 664 -1.229 30.361 9.720 1.00231.89 O ANISOU 1657 O CYS B 664 24037 42053 22017 8248 -258 1196 O ATOM 1658 CB CYS B 664 -2.144 28.479 11.833 1.00231.19 C ANISOU 1658 CB CYS B 664 23906 42113 21823 8158 -595 1367 C ATOM 1659 SG CYS B 664 -0.457 27.967 12.271 1.00191.61 S ANISOU 1659 SG CYS B 664 18884 37088 16829 8003 -816 1142 S ATOM 1660 N ASP B 665 -0.571 31.596 11.475 1.00232.77 N ANISOU 1660 N ASP B 665 24381 42105 21957 8101 -78 1059 N ATOM 1661 CA ASP B 665 0.366 32.398 10.692 1.00231.88 C ANISOU 1661 CA ASP B 665 24313 41949 21840 8063 -4 924 C ATOM 1662 C ASP B 665 1.655 31.657 10.331 1.00230.71 C ANISOU 1662 C ASP B 665 24056 41863 21739 7977 -212 785 C ATOM 1663 O ASP B 665 2.661 32.282 10.000 1.00231.79 O ANISOU 1663 O ASP B 665 24241 42002 21828 7898 -175 646 O ATOM 1664 CB ASP B 665 0.690 33.714 11.408 1.00233.15 C ANISOU 1664 CB ASP B 665 24683 42037 21865 8003 186 860 C ATOM 1665 CG ASP B 665 -0.453 34.719 11.344 1.00234.92 C ANISOU 1665 CG ASP B 665 25025 42203 22031 8114 391 949 C ATOM 1666 OD1 ASP B 665 -1.619 34.297 11.177 1.00236.11 O ANISOU 1666 OD1 ASP B 665 25098 42381 22231 8227 402 1077 O ATOM 1667 OD2 ASP B 665 -0.182 35.934 11.466 1.00234.97 O ANISOU 1667 OD2 ASP B 665 25211 42142 21923 8090 527 890 O ATOM 1668 N THR B 666 1.626 30.329 10.403 1.00228.38 N ANISOU 1668 N THR B 666 23624 41636 21514 7990 -450 815 N ATOM 1669 CA THR B 666 2.740 29.514 9.918 1.00223.81 C ANISOU 1669 CA THR B 666 22922 41135 20982 7946 -687 676 C ATOM 1670 C THR B 666 2.398 28.785 8.619 1.00220.44 C ANISOU 1670 C THR B 666 22326 40761 20670 8062 -819 744 C ATOM 1671 O THR B 666 3.224 28.705 7.707 1.00219.10 O ANISOU 1671 O THR B 666 22059 40651 20539 8056 -901 624 O ATOM 1672 CB THR B 666 3.197 28.481 10.962 1.00221.95 C ANISOU 1672 CB THR B 666 22670 40931 20729 7862 -928 618 C ATOM 1673 OG1 THR B 666 3.960 29.135 11.982 1.00220.83 O ANISOU 1673 OG1 THR B 666 22670 40735 20501 7728 -826 504 O ATOM 1674 CG2 THR B 666 4.061 27.419 10.305 1.00220.90 C ANISOU 1674 CG2 THR B 666 22386 40896 20649 7871 -1228 495 C ATOM 1675 N CYS B 667 1.180 28.250 8.540 1.00219.06 N ANISOU 1675 N CYS B 667 22116 40576 20541 8166 -845 944 N ATOM 1676 CA CYS B 667 0.755 27.492 7.362 1.00217.31 C ANISOU 1676 CA CYS B 667 21750 40385 20431 8285 -974 1053 C ATOM 1677 C CYS B 667 -0.499 28.061 6.688 1.00219.76 C ANISOU 1677 C CYS B 667 22085 40618 20795 8394 -750 1237 C ATOM 1678 O CYS B 667 -0.862 27.639 5.592 1.00221.09 O ANISOU 1678 O CYS B 667 22151 40778 21074 8490 -801 1337 O ATOM 1679 CB CYS B 667 0.547 26.014 7.708 1.00214.63 C ANISOU 1679 CB CYS B 667 21336 40122 20093 8314 -1303 1138 C ATOM 1680 SG CYS B 667 -1.086 25.611 8.339 1.00202.51 S ANISOU 1680 SG CYS B 667 19855 38587 18502 8369 -1287 1415 S ATOM 1681 N LEU B 668 -1.147 29.021 7.345 1.00219.91 N ANISOU 1681 N LEU B 668 22244 40576 20735 8384 -509 1275 N ATOM 1682 CA LEU B 668 -2.331 29.701 6.804 1.00216.06 C ANISOU 1682 CA LEU B 668 21805 40010 20277 8487 -284 1415 C ATOM 1683 C LEU B 668 -3.629 28.884 6.876 1.00216.07 C ANISOU 1683 C LEU B 668 21762 40049 20285 8593 -342 1654 C ATOM 1684 O LEU B 668 -4.637 29.269 6.283 1.00216.14 O ANISOU 1684 O LEU B 668 21791 39999 20333 8693 -179 1782 O ATOM 1685 CB LEU B 668 -2.095 30.174 5.361 1.00209.64 C ANISOU 1685 CB LEU B 668 20945 39125 19585 8514 -205 1369 C ATOM 1686 CG LEU B 668 -0.773 30.870 5.011 1.00204.76 C ANISOU 1686 CG LEU B 668 20343 38510 18948 8393 -192 1141 C ATOM 1687 CD1 LEU B 668 -0.843 31.447 3.608 1.00202.73 C ANISOU 1687 CD1 LEU B 668 20055 38174 18799 8403 -93 1120 C ATOM 1688 CD2 LEU B 668 -0.422 31.951 6.018 1.00204.20 C ANISOU 1688 CD2 LEU B 668 20454 38413 18718 8301 -44 1030 C ATOM 1689 N LEU B 669 -3.611 27.771 7.605 1.00215.15 N ANISOU 1689 N LEU B 669 21598 40034 20115 8560 -584 1712 N ATOM 1690 CA LEU B 669 -4.804 26.935 7.740 1.00212.90 C ANISOU 1690 CA LEU B 669 21284 39820 19791 8633 -681 1950 C ATOM 1691 C LEU B 669 -5.839 27.579 8.662 1.00218.23 C ANISOU 1691 C LEU B 669 22057 40525 20334 8637 -484 2025 C ATOM 1692 O LEU B 669 -5.491 28.151 9.696 1.00218.89 O ANISOU 1692 O LEU B 669 22223 40616 20330 8545 -410 1899 O ATOM 1693 CB LEU B 669 -4.443 25.537 8.253 1.00205.68 C ANISOU 1693 CB LEU B 669 20308 39012 18827 8571 -1051 1977 C ATOM 1694 CG LEU B 669 -5.592 24.528 8.306 1.00201.05 C ANISOU 1694 CG LEU B 669 19760 38468 18160 8563 -1118 2197 C ATOM 1695 CD1 LEU B 669 -6.010 24.119 6.905 1.00199.85 C ANISOU 1695 CD1 LEU B 669 19634 38196 18105 8611 -996 2302 C ATOM 1696 CD2 LEU B 669 -5.205 23.311 9.118 1.00200.38 C ANISOU 1696 CD2 LEU B 669 19723 38424 17989 8389 -1375 2130 C ATOM 1697 N GLN B 670 -7.109 27.476 8.280 1.00221.63 N ANISOU 1697 N GLN B 670 22479 40982 20748 8748 -403 2231 N ATOM 1698 CA GLN B 670 -8.204 28.061 9.053 1.00224.03 C ANISOU 1698 CA GLN B 670 22857 41352 20911 8775 -223 2303 C ATOM 1699 C GLN B 670 -8.721 27.114 10.136 1.00226.18 C ANISOU 1699 C GLN B 670 23107 41806 21023 8696 -431 2420 C ATOM 1700 O GLN B 670 -9.536 26.232 9.866 1.00227.84 O ANISOU 1700 O GLN B 670 23268 42115 21186 8740 -568 2634 O ATOM 1701 CB GLN B 670 -9.357 28.473 8.132 1.00220.15 C ANISOU 1701 CB GLN B 670 22375 40813 20459 8929 -24 2454 C ATOM 1702 CG GLN B 670 -9.064 29.672 7.244 1.00215.20 C ANISOU 1702 CG GLN B 670 21810 40003 19954 8982 213 2319 C ATOM 1703 CD GLN B 670 -10.230 30.020 6.338 1.00209.65 C ANISOU 1703 CD GLN B 670 21124 39229 19302 9123 393 2460 C ATOM 1704 OE1 GLN B 670 -10.882 29.138 5.779 1.00206.46 O ANISOU 1704 OE1 GLN B 670 20649 38857 18939 9189 306 2675 O ATOM 1705 NE2 GLN B 670 -10.496 31.311 6.185 1.00208.04 N ANISOU 1705 NE2 GLN B 670 21034 38922 19091 9168 632 2342 N ATOM 1706 N ASN B 671 -8.252 27.311 11.364 1.00224.42 N ANISOU 1706 N ASN B 671 22931 41627 20710 8565 -460 2287 N ATOM 1707 CA ASN B 671 -8.663 26.473 12.484 1.00220.57 C ANISOU 1707 CA ASN B 671 22429 41310 20068 8444 -671 2365 C ATOM 1708 C ASN B 671 -9.894 27.030 13.194 1.00220.22 C ANISOU 1708 C ASN B 671 22415 41400 19858 8473 -493 2450 C ATOM 1709 O ASN B 671 -10.437 28.060 12.799 1.00217.58 O ANISOU 1709 O ASN B 671 22122 41017 19532 8607 -212 2443 O ATOM 1710 CB ASN B 671 -7.512 26.316 13.477 1.00217.23 C ANISOU 1710 CB ASN B 671 22037 40856 19645 8264 -814 2174 C ATOM 1711 CG ASN B 671 -6.183 26.069 12.792 1.00209.79 C ANISOU 1711 CG ASN B 671 21071 39785 18854 8251 -932 2032 C ATOM 1712 OD1 ASN B 671 -5.987 25.042 12.140 1.00205.83 O ANISOU 1712 OD1 ASN B 671 20499 39306 18401 8272 -1186 2097 O ATOM 1713 ND2 ASN B 671 -5.260 27.011 12.939 1.00207.37 N ANISOU 1713 ND2 ASN B 671 20827 39361 18605 8219 -761 1839 N ATOM 1714 N LYS B 672 -10.320 26.345 14.250 1.00223.23 N ANISOU 1714 N LYS B 672 22778 41961 20079 8338 -677 2515 N ATOM 1715 CA LYS B 672 -11.511 26.733 14.999 1.00225.60 C ANISOU 1715 CA LYS B 672 23081 42448 20189 8347 -552 2595 C ATOM 1716 C LYS B 672 -11.160 27.332 16.361 1.00231.94 C ANISOU 1716 C LYS B 672 23931 43271 20924 8214 -486 2432 C ATOM 1717 O LYS B 672 -10.071 27.101 16.886 1.00234.51 O ANISOU 1717 O LYS B 672 24283 43496 21323 8067 -615 2296 O ATOM 1718 CB LYS B 672 -12.424 25.520 15.182 1.00222.63 C ANISOU 1718 CB LYS B 672 22643 42307 19640 8276 -816 2816 C ATOM 1719 CG LYS B 672 -11.670 24.251 15.546 1.00220.23 C ANISOU 1719 CG LYS B 672 22327 42018 19334 8085 -1216 2811 C ATOM 1720 CD LYS B 672 -12.605 23.153 16.013 1.00218.99 C ANISOU 1720 CD LYS B 672 22148 42053 19006 7916 -1379 2956 C ATOM 1721 CE LYS B 672 -13.495 22.656 14.892 1.00216.11 C ANISOU 1721 CE LYS B 672 21769 41668 18673 8011 -1249 3142 C ATOM 1722 NZ LYS B 672 -14.360 21.545 15.370 1.00215.60 N ANISOU 1722 NZ LYS B 672 21686 41754 18476 7798 -1356 3255 N ATOM 1723 N VAL B 673 -12.088 28.098 16.931 1.00235.29 N ANISOU 1723 N VAL B 673 24367 43827 21206 8271 -289 2444 N ATOM 1724 CA VAL B 673 -11.888 28.699 18.250 1.00237.84 C ANISOU 1724 CA VAL B 673 24731 44185 21454 8159 -219 2311 C ATOM 1725 C VAL B 673 -11.664 27.634 19.322 1.00236.95 C ANISOU 1725 C VAL B 673 24575 44192 21262 7895 -522 2321 C ATOM 1726 O VAL B 673 -10.878 27.829 20.253 1.00235.33 O ANISOU 1726 O VAL B 673 24417 43899 21099 7744 -543 2181 O ATOM 1727 CB VAL B 673 -13.082 29.594 18.666 1.00240.05 C ANISOU 1727 CB VAL B 673 25009 44638 21560 8283 6 2334 C ATOM 1728 CG1 VAL B 673 -13.098 30.880 17.854 1.00240.81 C ANISOU 1728 CG1 VAL B 673 25195 44567 21735 8514 299 2255 C ATOM 1729 CG2 VAL B 673 -14.401 28.842 18.522 1.00238.62 C ANISOU 1729 CG2 VAL B 673 24729 44740 21195 8301 -98 2534 C ATOM 1730 N THR B 674 -12.363 26.511 19.183 1.00236.48 N ANISOU 1730 N THR B 674 24442 44327 21083 7829 -767 2492 N ATOM 1731 CA THR B 674 -12.237 25.402 20.121 1.00233.27 C ANISOU 1731 CA THR B 674 24008 44049 20574 7557 -1114 2510 C ATOM 1732 C THR B 674 -10.831 24.822 20.038 1.00230.66 C ANISOU 1732 C THR B 674 23725 43493 20424 7439 -1325 2383 C ATOM 1733 O THR B 674 -10.286 24.339 21.032 1.00231.37 O ANISOU 1733 O THR B 674 23836 43572 20501 7200 -1532 2287 O ATOM 1734 CB THR B 674 -13.272 24.296 19.834 1.00231.35 C ANISOU 1734 CB THR B 674 23702 44064 20136 7518 -1369 2742 C ATOM 1735 OG1 THR B 674 -12.680 23.273 19.024 1.00227.95 O ANISOU 1735 OG1 THR B 674 23285 43516 19810 7502 -1629 2797 O ATOM 1736 CG2 THR B 674 -14.490 24.875 19.122 1.00231.81 C ANISOU 1736 CG2 THR B 674 23724 44257 20096 7754 -1114 2889 C ATOM 1737 N ASP B 675 -10.253 24.868 18.841 1.00227.48 N ANISOU 1737 N ASP B 675 23334 42914 20186 7601 -1277 2375 N ATOM 1738 CA ASP B 675 -8.843 24.551 18.660 1.00222.69 C ANISOU 1738 CA ASP B 675 22764 42094 19754 7534 -1418 2219 C ATOM 1739 C ASP B 675 -8.011 25.628 19.350 1.00221.10 C ANISOU 1739 C ASP B 675 22636 41728 19644 7493 -1181 2018 C ATOM 1740 O ASP B 675 -8.331 26.815 19.284 1.00221.96 O ANISOU 1740 O ASP B 675 22778 41806 19752 7631 -853 2000 O ATOM 1741 CB ASP B 675 -8.479 24.473 17.171 1.00218.82 C ANISOU 1741 CB ASP B 675 22251 41483 19406 7729 -1393 2254 C ATOM 1742 CG ASP B 675 -8.586 23.061 16.608 1.00213.47 C ANISOU 1742 CG ASP B 675 21531 40885 18694 7704 -1773 2390 C ATOM 1743 OD1 ASP B 675 -8.662 22.101 17.403 1.00213.20 O ANISOU 1743 OD1 ASP B 675 21522 40888 18597 7461 -1970 2358 O ATOM 1744 OD2 ASP B 675 -8.582 22.911 15.367 1.00210.52 O ANISOU 1744 OD2 ASP B 675 21136 40415 18436 7848 -1692 2444 O ATOM 1745 N ASN B 676 -6.951 25.204 20.026 1.00218.74 N ANISOU 1745 N ASN B 676 22378 41319 19413 7302 -1365 1870 N ATOM 1746 CA ASN B 676 -6.048 26.125 20.700 1.00217.68 C ANISOU 1746 CA ASN B 676 22331 41011 19366 7244 -1166 1696 C ATOM 1747 C ASN B 676 -4.681 26.076 20.038 1.00218.48 C ANISOU 1747 C ASN B 676 22466 40920 19627 7267 -1210 1551 C ATOM 1748 O ASN B 676 -3.797 26.878 20.340 1.00218.68 O ANISOU 1748 O ASN B 676 22575 40788 19725 7245 -1036 1416 O ATOM 1749 CB ASN B 676 -5.948 25.781 22.185 1.00215.19 C ANISOU 1749 CB ASN B 676 22047 40721 18996 6977 -1310 1633 C ATOM 1750 CG ASN B 676 -5.810 24.293 22.423 1.00212.37 C ANISOU 1750 CG ASN B 676 21659 40430 18603 6776 -1753 1638 C ATOM 1751 OD1 ASN B 676 -5.596 23.522 21.487 1.00212.06 O ANISOU 1751 OD1 ASN B 676 21585 40394 18592 6849 -1963 1671 O ATOM 1752 ND2 ASN B 676 -5.934 23.880 23.677 1.00210.59 N ANISOU 1752 ND2 ASN B 676 21452 40257 18306 6517 -1920 1602 N ATOM 1753 N LYS B 677 -4.521 25.111 19.139 1.00217.89 N ANISOU 1753 N LYS B 677 22327 40874 19587 7312 -1459 1588 N ATOM 1754 CA LYS B 677 -3.347 25.026 18.283 1.00215.62 C ANISOU 1754 CA LYS B 677 22036 40456 19433 7373 -1510 1460 C ATOM 1755 C LYS B 677 -3.811 24.636 16.887 1.00216.39 C ANISOU 1755 C LYS B 677 22047 40617 19555 7564 -1562 1591 C ATOM 1756 O LYS B 677 -4.988 24.782 16.556 1.00218.47 O ANISOU 1756 O LYS B 677 22277 40984 19748 7673 -1454 1771 O ATOM 1757 CB LYS B 677 -2.348 24.001 18.816 1.00212.15 C ANISOU 1757 CB LYS B 677 21613 39966 19027 7184 -1863 1313 C ATOM 1758 CG LYS B 677 -2.849 22.578 18.798 1.00209.11 C ANISOU 1758 CG LYS B 677 21180 39712 18560 7112 -2278 1410 C ATOM 1759 CD LYS B 677 -1.703 21.600 18.904 1.00207.61 C ANISOU 1759 CD LYS B 677 21008 39451 18422 6993 -2650 1232 C ATOM 1760 CE LYS B 677 -2.175 20.210 18.547 1.00208.08 C ANISOU 1760 CE LYS B 677 21082 39484 18493 6899 -2830 1254 C ATOM 1761 NZ LYS B 677 -1.069 19.224 18.559 1.00208.29 N ANISOU 1761 NZ LYS B 677 21169 39349 18623 6765 -3073 1013 N ATOM 1762 N CYS B 678 -2.898 24.132 16.067 1.00213.63 N ANISOU 1762 N CYS B 678 21656 40211 19302 7606 -1730 1501 N ATOM 1763 CA CYS B 678 -3.242 23.800 14.691 1.00209.82 C ANISOU 1763 CA CYS B 678 21090 39765 18868 7788 -1770 1621 C ATOM 1764 C CYS B 678 -3.518 22.309 14.489 1.00210.95 C ANISOU 1764 C CYS B 678 21208 39965 18977 7732 -2110 1698 C ATOM 1765 O CYS B 678 -2.764 21.457 14.957 1.00213.42 O ANISOU 1765 O CYS B 678 21568 40211 19311 7563 -2328 1534 O ATOM 1766 CB CYS B 678 -2.136 24.276 13.755 1.00206.96 C ANISOU 1766 CB CYS B 678 20700 39299 18636 7870 -1674 1465 C ATOM 1767 SG CYS B 678 -2.646 24.429 12.038 1.00212.19 S ANISOU 1767 SG CYS B 678 21271 39962 19390 8096 -1560 1605 S ATOM 1768 N ILE B 679 -4.607 22.004 13.792 1.00212.80 N ANISOU 1768 N ILE B 679 21432 40228 19193 7812 -2007 1889 N ATOM 1769 CA ILE B 679 -5.010 20.624 13.562 1.00217.20 C ANISOU 1769 CA ILE B 679 22037 40748 19742 7698 -2149 1937 C ATOM 1770 C ILE B 679 -4.257 20.029 12.375 1.00221.94 C ANISOU 1770 C ILE B 679 22635 41215 20477 7759 -2197 1841 C ATOM 1771 O ILE B 679 -4.543 18.910 11.935 1.00225.46 O ANISOU 1771 O ILE B 679 23130 41600 20934 7704 -2299 1889 O ATOM 1772 CB ILE B 679 -6.545 20.518 13.354 1.00208.52 C ANISOU 1772 CB ILE B 679 20935 39745 18547 7744 -2009 2200 C ATOM 1773 CG1 ILE B 679 -6.981 19.057 13.216 1.00210.72 C ANISOU 1773 CG1 ILE B 679 21274 39984 18806 7600 -2171 2264 C ATOM 1774 CG2 ILE B 679 -6.976 21.354 12.160 1.00206.49 C ANISOU 1774 CG2 ILE B 679 20632 39467 18359 7982 -1743 2325 C ATOM 1775 CD1 ILE B 679 -8.483 18.882 13.148 1.00212.54 C ANISOU 1775 CD1 ILE B 679 21500 40333 18922 7608 -2048 2522 C ATOM 1776 N ALA B 680 -3.276 20.772 11.869 1.00222.68 N ANISOU 1776 N ALA B 680 22675 41269 20663 7864 -2132 1702 N ATOM 1777 CA ALA B 680 -2.499 20.299 10.721 1.00222.56 C ANISOU 1777 CA ALA B 680 22643 41157 20761 7920 -2172 1589 C ATOM 1778 C ALA B 680 -1.008 20.116 10.969 1.00221.64 C ANISOU 1778 C ALA B 680 22519 41006 20689 7849 -2354 1301 C ATOM 1779 O ALA B 680 -0.429 19.127 10.527 1.00222.71 O ANISOU 1779 O ALA B 680 22684 41070 20867 7812 -2521 1171 O ATOM 1780 CB ALA B 680 -2.695 21.214 9.547 1.00221.88 C ANISOU 1780 CB ALA B 680 22489 41059 20756 8102 -1922 1676 C ATOM 1781 N CYS B 681 -0.387 21.068 11.658 1.00220.76 N ANISOU 1781 N CYS B 681 22373 40944 20561 7838 -2322 1199 N ATOM 1782 CA CYS B 681 1.037 20.970 11.954 1.00221.87 C ANISOU 1782 CA CYS B 681 22509 41062 20730 7764 -2478 927 C ATOM 1783 C CYS B 681 1.347 21.024 13.449 1.00222.26 C ANISOU 1783 C CYS B 681 22623 41113 20712 7597 -2601 840 C ATOM 1784 O CYS B 681 2.511 21.099 13.839 1.00220.25 O ANISOU 1784 O CYS B 681 22377 40838 20472 7527 -2704 623 O ATOM 1785 CB CYS B 681 1.806 22.079 11.241 1.00221.13 C ANISOU 1785 CB CYS B 681 22318 41012 20689 7885 -2328 848 C ATOM 1786 SG CYS B 681 1.647 23.726 11.991 1.00188.97 S ANISOU 1786 SG CYS B 681 18273 36949 16576 7887 -2034 900 S ATOM 1787 N GLN B 682 0.305 21.014 14.277 1.00222.60 N ANISOU 1787 N GLN B 682 22715 41187 20676 7526 -2581 1007 N ATOM 1788 CA GLN B 682 0.462 21.042 15.734 1.00220.73 C ANISOU 1788 CA GLN B 682 22549 40945 20373 7340 -2690 942 C ATOM 1789 C GLN B 682 1.148 22.310 16.251 1.00215.99 C ANISOU 1789 C GLN B 682 21963 40326 19777 7340 -2496 857 C ATOM 1790 O GLN B 682 1.928 22.255 17.202 1.00217.26 O ANISOU 1790 O GLN B 682 22200 40407 19943 7170 -2569 689 O ATOM 1791 CB GLN B 682 1.214 19.797 16.225 1.00223.83 C ANISOU 1791 CB GLN B 682 23021 41223 20801 7142 -2977 722 C ATOM 1792 CG GLN B 682 0.519 18.472 15.928 1.00225.38 C ANISOU 1792 CG GLN B 682 23267 41371 20996 7077 -3128 782 C ATOM 1793 CD GLN B 682 1.346 17.264 16.344 1.00225.27 C ANISOU 1793 CD GLN B 682 23348 41215 21030 6900 -3433 535 C ATOM 1794 OE1 GLN B 682 2.518 17.390 16.700 1.00223.74 O ANISOU 1794 OE1 GLN B 682 23170 40961 20881 6849 -3519 301 O ATOM 1795 NE2 GLN B 682 0.736 16.083 16.297 1.00225.92 N ANISOU 1795 NE2 GLN B 682 23504 41235 21100 6806 -3601 586 N ATOM 1796 N ALA B 683 0.842 23.448 15.634 1.00211.76 N ANISOU 1796 N ALA B 683 21416 39771 19272 7473 -2118 928 N ATOM 1797 CA ALA B 683 1.450 24.720 16.021 1.00211.38 C ANISOU 1797 CA ALA B 683 21453 39618 19243 7433 -1784 818 C ATOM 1798 C ALA B 683 0.535 25.565 16.907 1.00221.09 C ANISOU 1798 C ALA B 683 22770 40825 20411 7395 -1513 936 C ATOM 1799 O ALA B 683 -0.656 25.714 16.630 1.00211.53 O ANISOU 1799 O ALA B 683 21526 39688 19156 7497 -1412 1117 O ATOM 1800 CB ALA B 683 1.871 25.506 14.790 1.00206.51 C ANISOU 1800 CB ALA B 683 20793 38992 18678 7578 -1579 781 C ATOM 1801 N ALA B 684 1.113 26.124 17.967 1.00237.66 N ANISOU 1801 N ALA B 684 24978 42823 22500 7254 -1398 831 N ATOM 1802 CA ALA B 684 0.373 26.926 18.946 1.00235.61 C ANISOU 1802 CA ALA B 684 24805 42539 22178 7208 -1162 920 C ATOM 1803 C ALA B 684 -0.346 28.135 18.355 1.00230.57 C ANISOU 1803 C ALA B 684 24190 41913 21503 7387 -825 1026 C ATOM 1804 O ALA B 684 0.172 28.809 17.465 1.00224.77 O ANISOU 1804 O ALA B 684 23472 41134 20799 7487 -684 974 O ATOM 1805 CB ALA B 684 1.301 27.390 20.075 1.00233.35 C ANISOU 1805 CB ALA B 684 24645 42109 21907 7037 -1083 786 C ATOM 1806 N LYS B 685 -1.537 28.413 18.880 1.00227.60 N ANISOU 1806 N LYS B 685 23821 41608 21047 7414 -715 1161 N ATOM 1807 CA LYS B 685 -2.224 29.664 18.590 1.00221.88 C ANISOU 1807 CA LYS B 685 23153 40883 20269 7569 -400 1233 C ATOM 1808 C LYS B 685 -1.575 30.774 19.403 1.00217.38 C ANISOU 1808 C LYS B 685 22739 40184 19672 7509 -193 1146 C ATOM 1809 O LYS B 685 -1.308 30.608 20.592 1.00213.40 O ANISOU 1809 O LYS B 685 22284 39638 19160 7349 -241 1110 O ATOM 1810 CB LYS B 685 -3.709 29.579 18.943 1.00223.78 C ANISOU 1810 CB LYS B 685 23346 41272 20410 7624 -365 1390 C ATOM 1811 CG LYS B 685 -4.477 30.854 18.616 1.00226.49 C ANISOU 1811 CG LYS B 685 23750 41619 20685 7805 -64 1443 C ATOM 1812 CD LYS B 685 -5.650 31.073 19.553 1.00225.89 C ANISOU 1812 CD LYS B 685 23670 41680 20479 7809 10 1532 C ATOM 1813 CE LYS B 685 -6.611 29.903 19.519 1.00223.82 C ANISOU 1813 CE LYS B 685 23270 41611 20159 7778 -198 1666 C ATOM 1814 NZ LYS B 685 -7.839 30.190 20.307 1.00223.89 N ANISOU 1814 NZ LYS B 685 23257 41801 20011 7796 -113 1751 N ATOM 1815 N LEU B 686 -1.320 31.904 18.753 1.00215.71 N ANISOU 1815 N LEU B 686 22616 39902 19441 7626 23 1119 N ATOM 1816 CA LEU B 686 -0.668 33.039 19.394 1.00211.68 C ANISOU 1816 CA LEU B 686 22282 39267 18878 7585 209 1057 C ATOM 1817 C LEU B 686 -1.630 33.727 20.360 1.00210.93 C ANISOU 1817 C LEU B 686 22260 39198 18684 7624 363 1141 C ATOM 1818 O LEU B 686 -1.757 33.337 21.520 1.00211.29 O ANISOU 1818 O LEU B 686 22301 39254 18727 7495 303 1155 O ATOM 1819 CB LEU B 686 -0.204 34.049 18.336 1.00227.13 C ANISOU 1819 CB LEU B 686 24327 41166 20806 7691 354 1012 C ATOM 1820 CG LEU B 686 0.958 33.738 17.374 1.00234.75 C ANISOU 1820 CG LEU B 686 25249 42111 21835 7647 249 900 C ATOM 1821 CD1 LEU B 686 1.577 35.164 16.944 1.00162.07 C ANISOU 1821 CD1 LEU B 686 16226 32824 12528 7674 435 848 C ATOM 1822 CD2 LEU B 686 2.078 32.831 17.977 1.00158.57 C ANISOU 1822 CD2 LEU B 686 15568 32432 12249 7471 60 793 C TER 1823 LEU B 686 HETATM 1824 MG MG A 301 9.637 19.977 -4.775 1.00 56.04 MG ANISOU 1824 MG MG A 301 6164 7068 8060 49 -412 -666 MG HETATM 1825 PB GDP A 302 9.066 18.184 -8.176 1.00 50.54 P ANISOU 1825 PB GDP A 302 5483 6149 7569 16 -190 -1020 P HETATM 1826 O1B GDP A 302 8.896 19.296 -7.181 1.00 52.78 O ANISOU 1826 O1B GDP A 302 5810 6538 7705 -4 -264 -899 O HETATM 1827 O2B GDP A 302 9.937 17.121 -7.549 1.00 50.91 O ANISOU 1827 O2B GDP A 302 5399 6111 7833 105 -200 -967 O HETATM 1828 O3B GDP A 302 7.701 17.660 -8.538 1.00 47.76 O ANISOU 1828 O3B GDP A 302 5204 5722 7219 -9 -198 -1036 O HETATM 1829 O3A GDP A 302 9.776 18.646 -9.552 1.00 52.06 O ANISOU 1829 O3A GDP A 302 5685 6399 7697 -34 -90 -1191 O HETATM 1830 PA GDP A 302 10.676 19.983 -9.736 1.00 52.23 P ANISOU 1830 PA GDP A 302 5704 6555 7585 -87 -66 -1201 P HETATM 1831 O1A GDP A 302 9.824 21.230 -9.672 1.00 62.61 O ANISOU 1831 O1A GDP A 302 7140 7946 8703 -159 -113 -1150 O HETATM 1832 O2A GDP A 302 11.812 20.070 -8.752 1.00 48.07 O ANISOU 1832 O2A GDP A 302 5060 6054 7149 -42 -108 -1117 O HETATM 1833 O5' GDP A 302 11.227 19.735 -11.219 1.00 76.97 O ANISOU 1833 O5' GDP A 302 8824 9701 10720 -114 64 -1375 O HETATM 1834 C5' GDP A 302 12.100 18.629 -11.428 1.00 72.68 C ANISOU 1834 C5' GDP A 302 8161 9082 10371 -41 134 -1454 C HETATM 1835 C4' GDP A 302 12.760 18.809 -12.779 1.00 69.38 C ANISOU 1835 C4' GDP A 302 7737 8732 9893 -80 274 -1615 C HETATM 1836 O4' GDP A 302 11.724 18.954 -13.750 1.00 70.04 O ANISOU 1836 O4' GDP A 302 7959 8838 9814 -149 292 -1700 O HETATM 1837 C3' GDP A 302 13.580 20.094 -12.775 1.00 72.42 C ANISOU 1837 C3' GDP A 302 8097 9251 10170 -140 293 -1564 C HETATM 1838 O3' GDP A 302 14.918 19.869 -13.271 1.00 64.01 O ANISOU 1838 O3' GDP A 302 6897 8218 9206 -114 414 -1647 O HETATM 1839 C2' GDP A 302 12.774 21.058 -13.641 1.00 70.73 C ANISOU 1839 C2' GDP A 302 8033 9123 9718 -245 307 -1587 C HETATM 1840 O2' GDP A 302 13.579 21.986 -14.390 1.00 72.55 O ANISOU 1840 O2' GDP A 302 8250 9472 9843 -316 399 -1612 O HETATM 1841 C1' GDP A 302 11.953 20.132 -14.531 1.00 68.97 C ANISOU 1841 C1' GDP A 302 7883 8845 9479 -239 347 -1717 C HETATM 1842 N9 GDP A 302 10.679 20.775 -14.932 1.00 64.95 N ANISOU 1842 N9 GDP A 302 7524 8376 8779 -315 284 -1688 N HETATM 1843 C8 GDP A 302 9.704 21.188 -14.101 1.00 59.12 C ANISOU 1843 C8 GDP A 302 6845 7610 8009 -321 163 -1560 C HETATM 1844 N7 GDP A 302 8.677 21.733 -14.801 1.00 61.60 N ANISOU 1844 N7 GDP A 302 7278 7973 8155 -390 134 -1563 N HETATM 1845 C5 GDP A 302 8.994 21.669 -16.106 1.00 62.18 C ANISOU 1845 C5 GDP A 302 7381 8116 8129 -437 230 -1690 C HETATM 1846 C6 GDP A 302 8.356 22.068 -17.383 1.00 61.85 C ANISOU 1846 C6 GDP A 302 7452 8167 7882 -521 247 -1750 C HETATM 1847 O6 GDP A 302 7.237 22.622 -17.404 1.00 55.20 O ANISOU 1847 O6 GDP A 302 6696 7339 6938 -561 151 -1669 O HETATM 1848 N1 GDP A 302 9.018 21.825 -18.523 1.00 66.39 N ANISOU 1848 N1 GDP A 302 8029 8820 8377 -550 370 -1889 N HETATM 1849 C2 GDP A 302 10.234 21.248 -18.547 1.00 65.72 C ANISOU 1849 C2 GDP A 302 7837 8722 8412 -499 487 -1980 C HETATM 1850 N2 GDP A 302 10.827 21.050 -19.750 1.00 65.55 N ANISOU 1850 N2 GDP A 302 7823 8795 8288 -528 628 -2129 N HETATM 1851 N3 GDP A 302 10.878 20.856 -17.412 1.00 67.12 N ANISOU 1851 N3 GDP A 302 7894 8803 8805 -416 471 -1926 N HETATM 1852 C4 GDP A 302 10.317 21.037 -16.189 1.00 64.21 C ANISOU 1852 C4 GDP A 302 7521 8360 8515 -386 341 -1781 C HETATM 1853 ZN ZN B 300 -0.576 25.534 10.864 1.00189.05 ZN ANISOU 1853 ZN ZN B 300 18310 36903 16618 8120 -1381 1264 ZN HETATM 1854 O HOH A 217 11.334 19.354 -6.434 1.00 59.35 O ANISOU 1854 O HOH A 217 6444 7432 8673 57 -283 -864 O HETATM 1855 O HOH A 218 9.774 17.507 -4.706 1.00 50.92 O ANISOU 1855 O HOH A 218 5374 6208 7768 166 -394 -606 O HETATM 1856 O HOH A 219 10.506 19.930 -2.516 1.00 83.11 O ANISOU 1856 O HOH A 219 9501 10592 11483 121 -568 -445 O HETATM 1857 O HOH A 220 7.575 18.914 -4.419 1.00 60.83 O ANISOU 1857 O HOH A 220 6844 7565 8704 74 -420 -559 O HETATM 1858 O HOH A 221 4.419 19.391 -3.424 1.00 60.53 O ANISOU 1858 O HOH A 221 6965 7562 8471 45 -445 -383 O HETATM 1859 O HOH A 222 8.103 16.466 12.435 1.00 58.22 O ANISOU 1859 O HOH A 222 6446 8649 7026 496 -1336 1745 O HETATM 1860 O HOH A 223 -2.092 29.530 -20.933 1.00 61.84 O ANISOU 1860 O HOH A 223 8091 8538 6866 -894 -695 -730 O HETATM 1861 O HOH A 224 3.816 33.914 -19.444 1.00 51.76 O ANISOU 1861 O HOH A 224 6818 7140 5708 -982 -243 -504 O HETATM 1862 O HOH A 225 -0.395 31.569 -18.316 1.00 53.18 O ANISOU 1862 O HOH A 225 6949 7219 6038 -772 -538 -584 O HETATM 1863 O HOH A 226 13.897 21.980 -9.488 1.00 75.87 O ANISOU 1863 O HOH A 226 8490 9767 10569 -152 -22 -1185 O HETATM 1864 O HOH A 227 4.445 30.569 -5.142 1.00 51.51 O ANISOU 1864 O HOH A 227 6393 6716 6464 -273 -465 -788 O HETATM 1865 O HOH A 228 -5.057 37.115 -10.584 1.00 65.79 O ANISOU 1865 O HOH A 228 8451 8123 8423 -138 -603 -263 O HETATM 1866 O HOH A 229 2.222 37.269 -8.650 1.00 50.29 O ANISOU 1866 O HOH A 229 6578 6205 6325 -444 -478 -669 O HETATM 1867 O HOH A 230 0.131 38.783 -8.668 1.00 38.41 O ANISOU 1867 O HOH A 230 5144 4546 4905 -336 -505 -578 O HETATM 1868 O HOH A 231 2.592 11.315 -10.343 1.00 53.45 O ANISOU 1868 O HOH A 231 5913 5584 8811 -108 -278 -1258 O HETATM 1869 O HOH A 232 4.799 14.038 5.043 1.00 60.77 O ANISOU 1869 O HOH A 232 6632 7692 8765 398 -733 1091 O HETATM 1870 O HOH A 233 17.018 22.043 -14.854 1.00 77.96 O ANISOU 1870 O HOH A 233 8565 10282 10774 -288 653 -1691 O HETATM 1871 O HOH A 234 0.000 40.153 -15.416 0.50 49.44 O ANISOU 1871 O HOH A 234 6635 6063 6087 -681 0 0 O HETATM 1872 O HOH A 235 0.671 9.751 0.322 1.00 53.84 O ANISOU 1872 O HOH A 235 5611 5764 9080 184 -480 794 O HETATM 1873 O HOH A 236 -8.405 26.277 4.602 1.00 72.18 O ANISOU 1873 O HOH A 236 8688 9864 8872 431 200 203 O HETATM 1874 O HOH A 237 -16.572 25.296 -1.005 1.00 54.23 O ANISOU 1874 O HOH A 237 5581 7207 7816 287 120 562 O HETATM 1875 O HOH A 238 -16.472 18.295 0.167 1.00 72.45 O ANISOU 1875 O HOH A 238 7559 9256 10713 -113 104 1102 O HETATM 1876 O HOH A 240 -3.218 5.176 -14.044 1.00 90.07 O ANISOU 1876 O HOH A 240 10525 9154 14545 -647 -616 -1989 O HETATM 1877 O HOH A 241 -12.647 20.784 3.957 1.00 67.82 O ANISOU 1877 O HOH A 241 7499 9109 9161 231 339 985 O HETATM 1878 O HOH A 242 -0.655 35.854 -3.448 1.00 60.53 O ANISOU 1878 O HOH A 242 7850 7614 7536 -49 -416 -803 O HETATM 1879 O HOH A 243 8.095 34.899 3.528 1.00 73.96 O ANISOU 1879 O HOH A 243 9441 9895 8764 -312 -944 -1215 O HETATM 1880 O HOH A 244 5.564 40.173 -1.987 1.00 49.85 O ANISOU 1880 O HOH A 244 6643 6042 6256 -467 -668 -1252 O HETATM 1881 O HOH A 245 -12.421 36.692 -17.841 1.00 62.64 O ANISOU 1881 O HOH A 245 7699 8076 8024 -242 -1396 567 O HETATM 1882 O HOH A 246 8.043 25.065 -2.541 1.00 59.90 O ANISOU 1882 O HOH A 246 7014 7881 7863 -99 -567 -619 O HETATM 1883 O HOH A 247 -16.770 35.267 -3.711 1.00 66.53 O ANISOU 1883 O HOH A 247 7535 8395 9350 801 -29 96 O HETATM 1884 O HOH A 248 -8.853 36.132 -1.007 1.00 63.71 O ANISOU 1884 O HOH A 248 7996 8052 8160 538 -36 -566 O HETATM 1885 O HOH A 249 -12.032 17.727 3.288 1.00 94.24 O ANISOU 1885 O HOH A 249 10721 12172 12915 57 194 1191 O HETATM 1886 O HOH A 250 10.800 15.087 11.434 1.00 63.20 O ANISOU 1886 O HOH A 250 6753 9013 8246 577 -1558 1811 O HETATM 1887 O HOH B 7 -3.340 26.462 4.531 1.00110.28 O ANISOU 1887 O HOH B 7 8086 26674 7141 8710 -787 1833 O CONECT 137 1824 CONECT 1659 1853 CONECT 1680 1853 CONECT 1767 1853 CONECT 1824 137 1854 1855 1856 CONECT 1824 1857 CONECT 1825 1826 1827 1828 1829 CONECT 1826 1825 CONECT 1827 1825 CONECT 1828 1825 CONECT 1829 1825 1830 CONECT 1830 1829 1831 1832 1833 CONECT 1831 1830 CONECT 1832 1830 CONECT 1833 1830 1834 CONECT 1834 1833 1835 CONECT 1835 1834 1836 1837 CONECT 1836 1835 1841 CONECT 1837 1835 1838 1839 CONECT 1838 1837 CONECT 1839 1837 1840 1841 CONECT 1840 1839 CONECT 1841 1836 1839 1842 CONECT 1842 1841 1843 1852 CONECT 1843 1842 1844 CONECT 1844 1843 1845 CONECT 1845 1844 1846 1852 CONECT 1846 1845 1847 1848 CONECT 1847 1846 CONECT 1848 1846 1849 CONECT 1849 1848 1850 1851 CONECT 1850 1849 CONECT 1851 1849 1852 CONECT 1852 1842 1845 1851 CONECT 1853 1659 1680 1767 CONECT 1854 1824 CONECT 1855 1824 CONECT 1856 1824 CONECT 1857 1824 MASTER 338 0 3 11 10 0 8 6 1885 2 39 20 END
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Related entries of code: 3gj6
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
3ch5
RCSB PDB
PDBbind
52aa, >3CH5_2|Chain... at 92%
3gj7
RCSB PDB
PDBbind
98aa, >3GJ7_2|Chains... *
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3gj5
RCSB PDB
PDBbind
34-mer
3qbr
RCSB PDB
PDBbind
34-mer
Entry Information
PDB ID
3gj6
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
GTP-binding nuclear protein Ran
Ligand Name
34-mer
EC.Number
E.C.-.-.-.-
Resolution
2.7(Å)
Affinity (Kd/Ki/IC50)
Kd=6.5uM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) J.Mol.Biol. Vol. 391: pp. 375-389
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P49791
P62826
Entrez Gene ID
NCBI Entrez Gene ID:
5901
ASD
Information of known allosteric effects of PDB entries
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