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*** STRUCTURAL PROTEIN 17-JUL-23 8PUZ ***elNémo ID: 2406271123311174200Job options:ID = 2406271123311174200 JOBID = STRUCTURAL PROTEIN 17-JUL-23 8PUZ USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER STRUCTURAL PROTEIN 17-JUL-23 8PUZ TITLE CRYSTAL STRUCTURE OF TROPOMYOSIN (CDC8) CABLES, CONFORMER 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TROPOMYOSIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE; SOURCE 3 ORGANISM_COMMON: FISSION YEAST; SOURCE 4 ORGANISM_TAXID: 4896; SOURCE 5 GENE: CDC8, SPAC27F1.02C; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS TROPOMYOSIN, CDC8, YEAST, OVERLAP COMPLEX, STRUCTURAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.Y.A.REINKE,M.ZAHN,R.FEDOROV,D.J.MANSTEIN JRNL AUTH P.Y.A.REINKE,D.J.MANSTEIN JRNL TITL ATOMIC STRUCTURE OF CDC8 TROPOMYOSIN CABLES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.63 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 16951 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.235 REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 861 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 24.6300 - 3.9900 0.99 2676 122 0.2362 0.2652 REMARK 3 2 3.9900 - 3.1700 1.00 2677 165 0.2205 0.2704 REMARK 3 3 3.1700 - 2.7700 1.00 2667 155 0.2195 0.2906 REMARK 3 4 2.7700 - 2.5200 1.00 2671 137 0.2407 0.3013 REMARK 3 5 2.5200 - 2.3400 1.00 2694 126 0.2355 0.2813 REMARK 3 6 2.3400 - 2.2000 1.00 2705 156 0.2748 0.3383 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.184 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.76 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.08 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 : 0.002 2660 REMARK 3 ANGLE : 0.320 3550 REMARK 3 CHIRALITY : 0.021 400 REMARK 3 PLANARITY : 0.002 478 REMARK 3 DIHEDRAL : 14.960 1102 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -0.0004 -16.3960 21.7802 REMARK 3 T TENSOR REMARK 3 T11: 0.3116 T22: 0.3577 REMARK 3 T33: 0.3752 T12: -0.0248 REMARK 3 T13: 0.0289 T23: 0.0424 REMARK 3 L TENSOR REMARK 3 L11: 3.4093 L22: 5.4189 REMARK 3 L33: 1.9045 L12: -4.2159 REMARK 3 L13: 2.5032 L23: -3.1221 REMARK 3 S TENSOR REMARK 3 S11: -0.0880 S12: -0.0883 S13: 0.1534 REMARK 3 S21: 0.1045 S22: -0.0074 S23: -0.2696 REMARK 3 S31: 0.0207 S32: -0.0016 S33: 0.0948 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 8PUZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-23. REMARK 100 THE DEPOSITION ID IS D_1292131846. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-FEB-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : BM30A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : 1.00 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SADABS REMARK 200 DATA SCALING SOFTWARE : SADABS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16997 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 26.600 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 2.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M TRIS HCL PH 8.2, AND 45% MPD, REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: HEXAMERIC 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 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -124.34256 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 158.93182 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -98.52082 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 124.34256 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 -158.93182 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 98.52082 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP B 2 -130.17 54.20 REMARK 500 REMARK 500 REMARK: NULL DBREF 8PUZ A 1 161 UNP Q02088 TPM_SCHPO 1 161 DBREF 8PUZ B 1 161 UNP Q02088 TPM_SCHPO 1 161 SEQRES 1 A 161 MET ASP LYS LEU ARG GLU LYS ILE ASN ALA ALA ARG ALA SEQRES 2 A 161 GLU THR ASP GLU ALA VAL ALA ARG ALA GLU ALA ALA GLU SEQRES 3 A 161 ALA LYS LEU LYS GLU VAL GLU LEU GLN LEU SER LEU LYS SEQRES 4 A 161 GLU GLN GLU TYR GLU SER LEU SER ARG LYS SER GLU ALA SEQRES 5 A 161 ALA GLU SER GLN LEU GLU GLU LEU GLU GLU GLU THR LYS SEQRES 6 A 161 GLN LEU ARG LEU LYS ALA ASP ASN GLU ASP ILE GLN LYS SEQRES 7 A 161 THR GLU ALA GLU GLN LEU SER ARG LYS VAL GLU LEU LEU SEQRES 8 A 161 GLU GLU GLU LEU GLU THR ASN ASP LYS LEU LEU ARG GLU SEQRES 9 A 161 THR THR GLU LYS MET ARG GLN THR ASP VAL LYS ALA GLU SEQRES 10 A 161 HIS PHE GLU ARG ARG VAL GLN SER LEU GLU ARG GLU ARG SEQRES 11 A 161 ASP ASP MET GLU GLN LYS LEU GLU GLU MET THR ASP LYS SEQRES 12 A 161 TYR THR LYS VAL LYS ALA GLU LEU ASP GLU VAL HIS GLN SEQRES 13 A 161 ALA LEU GLU ASP LEU SEQRES 1 B 161 MET ASP LYS LEU ARG GLU LYS ILE ASN ALA ALA ARG ALA SEQRES 2 B 161 GLU THR ASP GLU ALA VAL ALA ARG ALA GLU ALA ALA GLU SEQRES 3 B 161 ALA LYS LEU LYS GLU VAL GLU LEU GLN LEU SER LEU LYS SEQRES 4 B 161 GLU GLN GLU TYR GLU SER LEU SER ARG LYS SER GLU ALA SEQRES 5 B 161 ALA GLU SER GLN LEU GLU GLU LEU GLU GLU GLU THR LYS SEQRES 6 B 161 GLN LEU ARG LEU LYS ALA ASP ASN GLU ASP ILE GLN LYS SEQRES 7 B 161 THR GLU ALA GLU GLN LEU SER ARG LYS VAL GLU LEU LEU SEQRES 8 B 161 GLU GLU GLU LEU GLU THR ASN ASP LYS LEU LEU ARG GLU SEQRES 9 B 161 THR THR GLU LYS MET ARG GLN THR ASP VAL LYS ALA GLU SEQRES 10 B 161 HIS PHE GLU ARG ARG VAL GLN SER LEU GLU ARG GLU ARG SEQRES 11 B 161 ASP ASP MET GLU GLN LYS LEU GLU GLU MET THR ASP LYS SEQRES 12 B 161 TYR THR LYS VAL LYS ALA GLU LEU ASP GLU VAL HIS GLN SEQRES 13 B 161 ALA LEU GLU ASP LEU SEQRES 1 C 161 MET ASP LYS LEU ARG GLU LYS ILE ASN ALA ALA ARG ALA SEQRES 2 C 161 GLU THR ASP GLU ALA VAL ALA ARG ALA GLU ALA ALA GLU SEQRES 3 C 161 ALA LYS LEU LYS GLU VAL GLU LEU GLN LEU SER LEU LYS SEQRES 4 C 161 GLU GLN GLU TYR GLU SER LEU SER ARG LYS SER GLU ALA SEQRES 5 C 161 ALA GLU SER GLN LEU GLU GLU LEU GLU GLU GLU THR LYS SEQRES 6 C 161 GLN LEU ARG LEU LYS ALA ASP ASN GLU ASP ILE GLN LYS SEQRES 7 C 161 THR GLU ALA GLU GLN LEU SER ARG LYS VAL GLU LEU LEU SEQRES 8 C 161 GLU GLU GLU LEU GLU THR ASN ASP LYS LEU LEU ARG GLU SEQRES 9 C 161 THR THR GLU LYS MET ARG GLN THR ASP VAL LYS ALA GLU SEQRES 10 C 161 HIS PHE GLU ARG ARG VAL GLN SER LEU GLU ARG GLU ARG SEQRES 11 C 161 ASP ASP MET GLU GLN LYS LEU GLU GLU MET THR ASP LYS SEQRES 12 C 161 TYR THR LYS VAL LYS ALA GLU LEU ASP GLU VAL HIS GLN SEQRES 13 C 161 ALA LEU GLU ASP LEU SEQRES 1 D 161 MET ASP LYS LEU ARG GLU LYS ILE ASN ALA ALA ARG ALA SEQRES 2 D 161 GLU THR ASP GLU ALA VAL ALA ARG ALA GLU ALA ALA GLU SEQRES 3 D 161 ALA LYS LEU LYS GLU VAL GLU LEU GLN LEU SER LEU LYS SEQRES 4 D 161 GLU GLN GLU TYR GLU SER LEU SER ARG LYS SER GLU ALA SEQRES 5 D 161 ALA GLU SER GLN LEU GLU GLU LEU GLU GLU GLU THR LYS SEQRES 6 D 161 GLN LEU ARG LEU LYS ALA ASP ASN GLU ASP ILE GLN LYS SEQRES 7 D 161 THR GLU ALA GLU GLN LEU SER ARG LYS VAL GLU LEU LEU SEQRES 8 D 161 GLU GLU GLU LEU GLU THR ASN ASP LYS LEU LEU ARG GLU SEQRES 9 D 161 THR THR GLU LYS MET ARG GLN THR ASP VAL LYS ALA GLU SEQRES 10 D 161 HIS PHE GLU ARG ARG VAL GLN SER LEU GLU ARG GLU ARG SEQRES 11 D 161 ASP ASP MET GLU GLN LYS LEU GLU GLU MET THR ASP LYS SEQRES 12 D 161 TYR THR LYS VAL LYS ALA GLU LEU ASP GLU VAL HIS GLN SEQRES 13 D 161 ALA LEU GLU ASP LEU SEQRES 1 E 161 MET ASP LYS LEU ARG GLU LYS ILE ASN ALA ALA ARG ALA SEQRES 2 E 161 GLU THR ASP GLU ALA VAL ALA ARG ALA GLU ALA ALA GLU SEQRES 3 E 161 ALA LYS LEU LYS GLU VAL GLU LEU GLN LEU SER LEU LYS SEQRES 4 E 161 GLU GLN GLU TYR GLU SER LEU SER ARG LYS SER GLU ALA SEQRES 5 E 161 ALA GLU SER GLN LEU GLU GLU LEU GLU GLU GLU THR LYS SEQRES 6 E 161 GLN LEU ARG LEU LYS ALA ASP ASN GLU ASP ILE GLN LYS SEQRES 7 E 161 THR GLU ALA GLU GLN LEU SER ARG LYS VAL GLU LEU LEU SEQRES 8 E 161 GLU GLU GLU LEU GLU THR ASN ASP LYS LEU LEU ARG GLU SEQRES 9 E 161 THR THR GLU LYS MET ARG GLN THR ASP VAL LYS ALA GLU SEQRES 10 E 161 HIS PHE GLU ARG ARG VAL GLN SER LEU GLU ARG GLU ARG SEQRES 11 E 161 ASP ASP MET GLU GLN LYS LEU GLU GLU MET THR ASP LYS SEQRES 12 E 161 TYR THR LYS VAL LYS ALA GLU LEU ASP GLU VAL HIS GLN SEQRES 13 E 161 ALA LEU GLU ASP LEU SEQRES 1 F 161 MET ASP LYS LEU ARG GLU LYS ILE ASN ALA ALA ARG ALA SEQRES 2 F 161 GLU THR ASP GLU ALA VAL ALA ARG ALA GLU ALA ALA GLU SEQRES 3 F 161 ALA LYS LEU LYS GLU VAL GLU LEU GLN LEU SER LEU LYS SEQRES 4 F 161 GLU GLN GLU TYR GLU SER LEU SER ARG LYS SER GLU ALA SEQRES 5 F 161 ALA GLU SER GLN LEU GLU GLU LEU GLU GLU GLU THR LYS SEQRES 6 F 161 GLN LEU ARG LEU LYS ALA ASP ASN GLU ASP ILE GLN LYS SEQRES 7 F 161 THR GLU ALA GLU GLN LEU SER ARG LYS VAL GLU LEU LEU SEQRES 8 F 161 GLU GLU GLU LEU GLU THR ASN ASP LYS LEU LEU ARG GLU SEQRES 9 F 161 THR THR GLU LYS MET ARG GLN THR ASP VAL LYS ALA GLU SEQRES 10 F 161 HIS PHE GLU ARG ARG VAL GLN SER LEU GLU ARG GLU ARG SEQRES 11 F 161 ASP ASP MET GLU GLN LYS LEU GLU GLU MET THR ASP LYS SEQRES 12 F 161 TYR THR LYS VAL LYS ALA GLU LEU ASP GLU VAL HIS GLN SEQRES 13 F 161 ALA LEU GLU ASP LEU FORMUL 3 HOH *35(H2 O) HELIX 1 1 MET A 1 LEU A 161 1 161 HELIX 2 2 ASP B 2 ASP B 72 1 71 HELIX 3 3 ASN B 73 ASP B 160 1 88 CRYST1 23.267 38.616 98.933 94.31 91.92 102.94 P 1 2 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 0.042979 0.009875 0.002287 0.00000 SCALE2 0.000000 0.026571 0.002263 0.00000 SCALE3 0.000000 0.000000 0.010150 0.00000 ATOM 1 N ALA A 149 -55.799 53.961 -12.458 1.00 42.36 N ANISOU 1 N ALA A 149 5139 5187 5770 381 -341 -584 N ATOM 2 CA ALA A 149 -56.305 55.248 -11.993 1.00 51.07 C ANISOU 2 CA ALA A 149 6393 6250 6762 609 -476 -685 C ATOM 3 C ALA A 149 -56.376 56.252 -13.138 1.00 50.58 C ANISOU 3 C ALA A 149 6270 6071 6876 432 -573 -709 C ATOM 4 O ALA A 149 -57.363 56.990 -13.269 1.00 54.64 O ANISOU 4 O ALA A 149 6816 6626 7318 537 -548 -708 O ATOM 5 CB ALA A 149 -55.427 55.781 -10.861 1.00 47.26 C ANISOU 5 CB ALA A 149 6132 5629 6193 834 -758 -861 C ATOM 6 N GLU A 150 -55.344 56.282 -13.987 1.00 47.83 N ANISOU 6 N GLU A 150 5821 5591 6759 186 -658 -694 N ATOM 7 CA GLU A 150 -55.346 57.198 -15.125 1.00 51.62 C ANISOU 7 CA GLU A 150 6220 5976 7418 39 -716 -664 C ATOM 8 C GLU A 150 -56.496 56.897 -16.081 1.00 57.33 C ANISOU 8 C GLU A 150 6858 6834 8090 -35 -495 -573 C ATOM 9 O GLU A 150 -57.163 57.816 -16.571 1.00 49.64 O ANISOU 9 O GLU A 150 5888 5839 7136 -25 -524 -583 O ATOM 10 CB GLU A 150 -54.006 57.128 -15.857 1.00 50.75 C ANISOU 10 CB GLU A 150 5979 5739 7564 -156 -778 -572 C ATOM 11 CG GLU A 150 -52.820 57.604 -15.033 1.00 74.78 C ANISOU 11 CG GLU A 150 9060 8577 10774 -121 -1077 -627 C ATOM 12 CD GLU A 150 -52.798 59.108 -14.853 1.00 88.67 C ANISOU 12 CD GLU A 150 10880 10122 12688 -57 -1402 -703 C ATOM 13 OE1 GLU A 150 -52.775 59.828 -15.872 1.00 94.81 O ANISOU 13 OE1 GLU A 150 11520 10833 13670 -185 -1403 -586 O ATOM 14 OE2 GLU A 150 -52.806 59.572 -13.693 1.00 86.28 O ANISOU 14 OE2 GLU A 150 10782 9707 12294 153 -1675 -881 O ATOM 15 N LEU A 151 -56.744 55.614 -16.358 1.00 42.94 N ANISOU 15 N LEU A 151 4966 5122 6226 -107 -317 -486 N ATOM 16 CA LEU A 151 -57.820 55.249 -17.275 1.00 56.99 C ANISOU 16 CA LEU A 151 6675 6970 8008 -177 -194 -403 C ATOM 17 C LEU A 151 -59.185 55.597 -16.694 1.00 61.15 C ANISOU 17 C LEU A 151 7206 7588 8442 -30 -138 -368 C ATOM 18 O LEU A 151 -60.070 56.071 -17.418 1.00 39.70 O ANISOU 18 O LEU A 151 4450 4873 5762 -63 -120 -333 O ATOM 19 CB LEU A 151 -57.740 53.761 -17.612 1.00 53.42 C ANISOU 19 CB LEU A 151 6167 6558 7572 -267 -107 -326 C ATOM 20 CG LEU A 151 -58.794 53.228 -18.584 1.00 60.33 C ANISOU 20 CG LEU A 151 6989 7435 8498 -336 -81 -250 C ATOM 21 CD1 LEU A 151 -58.757 53.996 -19.897 1.00 53.54 C ANISOU 21 CD1 LEU A 151 6164 6509 7668 -384 -124 -282 C ATOM 22 CD2 LEU A 151 -58.592 51.740 -18.824 1.00 48.18 C ANISOU 22 CD2 LEU A 151 5432 5880 6995 -400 -85 -200 C ATOM 23 N ASP A 152 -59.378 55.369 -15.392 1.00 50.99 N ANISOU 23 N ASP A 152 5966 6386 7022 168 -94 -352 N ATOM 24 CA ASP A 152 -60.636 55.758 -14.762 1.00 57.11 C ANISOU 24 CA ASP A 152 6741 7277 7681 392 4 -262 C ATOM 25 C ASP A 152 -60.835 57.268 -14.818 1.00 60.01 C ANISOU 25 C ASP A 152 7231 7581 7987 506 -122 -388 C ATOM 26 O ASP A 152 -61.950 57.749 -15.060 1.00 58.50 O ANISOU 26 O ASP A 152 6997 7451 7779 575 -48 -308 O ATOM 27 CB ASP A 152 -60.677 55.260 -13.318 1.00 52.37 C ANISOU 27 CB ASP A 152 6199 6800 6899 672 98 -196 C ATOM 28 CG ASP A 152 -60.751 53.748 -13.226 1.00 73.20 C ANISOU 28 CG ASP A 152 8671 9510 9632 570 240 -11 C ATOM 29 OD1 ASP A 152 -60.872 53.095 -14.284 1.00 79.29 O ANISOU 29 OD1 ASP A 152 9306 10216 10605 300 229 48 O ATOM 30 OD2 ASP A 152 -60.689 53.213 -12.099 1.00 71.17 O ANISOU 30 OD2 ASP A 152 8439 9360 9244 788 340 74 O ATOM 31 N GLU A 153 -59.759 58.033 -14.613 1.00 58.81 N ANISOU 31 N GLU A 153 7219 7284 7843 520 -343 -569 N ATOM 32 CA GLU A 153 -59.862 59.487 -14.698 1.00 57.33 C ANISOU 32 CA GLU A 153 7147 6983 7652 611 -533 -693 C ATOM 33 C GLU A 153 -60.205 59.934 -16.115 1.00 62.65 C ANISOU 33 C GLU A 153 7689 7612 8501 371 -506 -644 C ATOM 34 O GLU A 153 -61.018 60.846 -16.308 1.00 67.54 O ANISOU 34 O GLU A 153 8342 8234 9085 455 -527 -661 O ATOM 35 CB GLU A 153 -58.556 60.125 -14.225 1.00 65.70 C ANISOU 35 CB GLU A 153 8342 7830 8790 639 -850 -859 C ATOM 36 CG GLU A 153 -58.562 61.643 -14.218 1.00 89.38 C ANISOU 36 CG GLU A 153 11470 10649 11840 741 -1140 -993 C ATOM 37 CD GLU A 153 -57.370 62.221 -13.482 1.00 95.32 C ANISOU 37 CD GLU A 153 12376 11141 12699 827 -1545 -1150 C ATOM 38 OE1 GLU A 153 -56.888 61.572 -12.529 1.00 91.90 O ANISOU 38 OE1 GLU A 153 12054 10722 12141 975 -1587 -1204 O ATOM 39 OE2 GLU A 153 -56.911 63.320 -13.859 1.00104.52 O ANISOU 39 OE2 GLU A 153 13540 12066 14106 746 -1850 -1202 O ATOM 40 N VAL A 154 -59.608 59.292 -17.121 1.00 54.82 N ANISOU 40 N VAL A 154 6570 6587 7671 115 -453 -579 N ATOM 41 CA VAL A 154 -59.912 59.638 -18.508 1.00 65.22 C ANISOU 41 CA VAL A 154 7798 7874 9109 -51 -417 -524 C ATOM 42 C VAL A 154 -61.361 59.299 -18.841 1.00 69.72 C ANISOU 42 C VAL A 154 8311 8558 9620 -34 -275 -439 C ATOM 43 O VAL A 154 -62.038 60.042 -19.566 1.00 60.15 O ANISOU 43 O VAL A 154 7082 7327 8444 -61 -285 -432 O ATOM 44 CB VAL A 154 -58.928 58.934 -19.461 1.00 60.23 C ANISOU 44 CB VAL A 154 7088 7203 8595 -226 -376 -457 C ATOM 45 CG1 VAL A 154 -59.362 59.110 -20.907 1.00 71.14 C ANISOU 45 CG1 VAL A 154 8424 8582 10026 -314 -315 -392 C ATOM 46 CG2 VAL A 154 -57.525 59.479 -19.262 1.00 70.48 C ANISOU 46 CG2 VAL A 154 8375 8363 10041 -257 -525 -466 C ATOM 47 N HIS A 155 -61.860 58.173 -18.324 1.00 63.74 N ANISOU 47 N HIS A 155 7498 7904 8818 4 -156 -341 N ATOM 48 CA HIS A 155 -63.258 57.818 -18.547 1.00 63.24 C ANISOU 48 CA HIS A 155 7323 7914 8790 16 -57 -192 C ATOM 49 C HIS A 155 -64.191 58.833 -17.902 1.00 75.06 C ANISOU 49 C HIS A 155 8852 9485 10183 233 -16 -166 C ATOM 50 O HIS A 155 -65.184 59.250 -18.511 1.00 73.13 O ANISOU 50 O HIS A 155 8538 9245 10002 207 5 -95 O ATOM 51 CB HIS A 155 -63.540 56.413 -18.016 1.00 66.73 C ANISOU 51 CB HIS A 155 7654 8425 9277 18 38 -31 C ATOM 52 CG HIS A 155 -63.065 55.321 -18.921 1.00 73.34 C ANISOU 52 CG HIS A 155 8457 9172 10238 -184 -28 -32 C ATOM 53 ND1 HIS A 155 -62.632 55.557 -20.210 1.00 77.09 N ANISOU 53 ND1 HIS A 155 9001 9544 10746 -307 -123 -135 N ATOM 54 CD2 HIS A 155 -62.959 53.985 -18.730 1.00 79.37 C ANISOU 54 CD2 HIS A 155 9147 9930 11081 -240 -22 63 C ATOM 55 CE1 HIS A 155 -62.280 54.415 -20.771 1.00 76.30 C ANISOU 55 CE1 HIS A 155 8907 9382 10702 -393 -179 -123 C ATOM 56 NE2 HIS A 155 -62.468 53.444 -19.893 1.00 83.00 N ANISOU 56 NE2 HIS A 155 9666 10272 11597 -378 -140 -15 N ATOM 57 N GLN A 156 -63.884 59.250 -16.671 1.00 72.85 N ANISOU 57 N GLN A 156 8702 9255 9721 484 -23 -230 N ATOM 58 CA GLN A 156 -64.693 60.276 -16.020 1.00 80.19 C ANISOU 58 CA GLN A 156 9728 10255 10487 778 -3 -228 C ATOM 59 C GLN A 156 -64.639 61.596 -16.778 1.00 81.77 C ANISOU 59 C GLN A 156 10008 10327 10734 704 -170 -384 C ATOM 60 O GLN A 156 -65.624 62.343 -16.800 1.00 89.01 O ANISOU 60 O GLN A 156 10934 11294 11589 844 -129 -341 O ATOM 61 CB GLN A 156 -64.231 60.478 -14.578 1.00 76.62 C ANISOU 61 CB GLN A 156 9482 9847 9782 1130 -44 -315 C ATOM 62 CG GLN A 156 -64.384 59.248 -13.696 1.00 93.97 C ANISOU 62 CG GLN A 156 11601 12203 11902 1274 160 -121 C ATOM 63 CD GLN A 156 -63.757 59.433 -12.331 1.00 98.94 C ANISOU 63 CD GLN A 156 12487 12858 12250 1647 85 -245 C ATOM 64 OE1 GLN A 156 -63.640 60.555 -11.838 1.00 98.19 O ANISOU 64 OE1 GLN A 156 12649 12694 11964 1923 -101 -434 O ATOM 65 NE2 GLN A 156 -63.343 58.331 -11.714 1.00 93.81 N ANISOU 65 NE2 GLN A 156 11790 12282 11570 1678 190 -152 N ATOM 66 N ALA A 157 -63.500 61.901 -17.403 1.00 80.76 N ANISOU 66 N ALA A 157 9914 10037 10734 498 -346 -525 N ATOM 67 CA ALA A 157 -63.384 63.134 -18.173 1.00 81.34 C ANISOU 67 CA ALA A 157 10020 9977 10907 415 -502 -619 C ATOM 68 C ALA A 157 -64.233 63.074 -19.437 1.00 89.21 C ANISOU 68 C ALA A 157 10878 11008 12009 238 -388 -514 C ATOM 69 O ALA A 157 -64.991 64.005 -19.732 1.00 90.36 O ANISOU 69 O ALA A 157 11041 11147 12144 293 -411 -526 O ATOM 70 CB ALA A 157 -61.916 63.403 -18.514 1.00 76.28 C ANISOU 70 CB ALA A 157 9386 9157 10441 254 -693 -697 C ATOM 71 N LEU A 158 -64.127 61.979 -20.194 1.00 79.00 N ANISOU 71 N LEU A 158 9473 9734 10809 52 -296 -425 N ATOM 72 CA LEU A 158 -64.899 61.858 -21.427 1.00 87.96 C ANISOU 72 CA LEU A 158 10525 10862 12035 -80 -257 -352 C ATOM 73 C LEU A 158 -66.385 61.657 -21.162 1.00 93.15 C ANISOU 73 C LEU A 158 11092 11611 12691 3 -164 -216 C ATOM 74 O LEU A 158 -67.199 61.882 -22.064 1.00 92.51 O ANISOU 74 O LEU A 158 10956 11498 12695 -72 -180 -169 O ATOM 75 CB LEU A 158 -64.352 60.715 -22.289 1.00 79.49 C ANISOU 75 CB LEU A 158 9419 9750 11033 -232 -248 -318 C ATOM 76 CG LEU A 158 -64.296 59.284 -21.743 1.00 94.97 C ANISOU 76 CG LEU A 158 11330 11755 12999 -245 -198 -245 C ATOM 77 CD1 LEU A 158 -65.610 58.534 -21.942 1.00 98.32 C ANISOU 77 CD1 LEU A 158 11637 12190 13531 -271 -189 -98 C ATOM 78 CD2 LEU A 158 -63.143 58.521 -22.379 1.00 99.74 C ANISOU 78 CD2 LEU A 158 11980 12303 13615 -334 -226 -282 C ATOM 79 N GLU A 159 -66.754 61.233 -19.951 1.00 94.78 N ANISOU 79 N GLU A 159 11268 11929 12816 178 -60 -116 N ATOM 80 CA GLU A 159 -68.165 61.085 -19.609 1.00 98.58 C ANISOU 80 CA GLU A 159 11608 12515 13333 301 68 108 C ATOM 81 C GLU A 159 -68.882 62.429 -19.645 1.00111.34 C ANISOU 81 C GLU A 159 13282 14154 14866 444 67 75 C ATOM 82 O GLU A 159 -69.970 62.552 -20.221 1.00113.42 O ANISOU 82 O GLU A 159 13418 14424 15254 399 99 215 O ATOM 83 CB GLU A 159 -68.297 60.436 -18.230 1.00 98.55 C ANISOU 83 CB GLU A 159 11563 12656 13226 536 224 270 C ATOM 84 CG GLU A 159 -69.508 60.895 -17.435 1.00103.14 C ANISOU 84 CG GLU A 159 12076 13397 13714 853 402 494 C ATOM 85 CD GLU A 159 -69.202 61.050 -15.959 1.00110.31 C ANISOU 85 CD GLU A 159 13143 14448 14322 1252 511 495 C ATOM 86 OE1 GLU A 159 -68.443 60.219 -15.417 1.00110.90 O ANISOU 86 OE1 GLU A 159 13239 14536 14363 1250 523 482 O ATOM 87 OE2 GLU A 159 -69.709 62.010 -15.342 1.00112.78 O ANISOU 87 OE2 GLU A 159 13588 14853 14408 1601 567 495 O ATOM 88 N ASP A 160 -68.283 63.453 -19.032 1.00130.02 N ANISOU 88 N ASP A 160 15851 16508 17044 623 -12 -113 N ATOM 89 CA ASP A 160 -68.902 64.773 -19.023 1.00130.94 C ANISOU 89 CA ASP A 160 16059 16625 17067 787 -53 -172 C ATOM 90 C ASP A 160 -68.899 65.404 -20.408 1.00130.28 C ANISOU 90 C ASP A 160 15944 16412 17143 528 -169 -258 C ATOM 91 O ASP A 160 -69.831 66.141 -20.752 1.00140.11 O ANISOU 91 O ASP A 160 17166 17676 18394 579 -150 -217 O ATOM 92 CB ASP A 160 -68.188 65.677 -18.018 1.00133.24 C ANISOU 92 CB ASP A 160 16612 16872 17141 1061 -206 -378 C ATOM 93 CG ASP A 160 -68.366 65.209 -16.586 1.00133.33 C ANISOU 93 CG ASP A 160 16711 17039 16910 1439 -78 -290 C ATOM 94 OD1 ASP A 160 -69.520 64.954 -16.181 1.00126.76 O ANISOU 94 OD1 ASP A 160 15771 16390 16002 1660 162 -38 O ATOM 95 OD2 ASP A 160 -67.351 65.087 -15.868 1.00139.50 O ANISOU 95 OD2 ASP A 160 17656 17758 17589 1536 -210 -440 O ATOM 96 N LEU A 161 -67.867 65.133 -21.205 1.00112.36 N ANISOU 96 N LEU A 161 13676 14026 14990 287 -268 -352 N ATOM 97 CA LEU A 161 -67.784 65.582 -22.594 1.00110.93 C ANISOU 97 CA LEU A 161 13466 13744 14939 87 -339 -388 C ATOM 98 C LEU A 161 -67.877 67.105 -22.711 1.00114.95 C ANISOU 98 C LEU A 161 14060 14184 15433 158 -452 -488 C ATOM 99 O LEU A 161 -68.162 67.651 -23.776 1.00110.96 O ANISOU 99 O LEU A 161 13520 13626 15012 49 -478 -483 O ATOM 100 CB LEU A 161 -68.880 64.912 -23.431 1.00110.42 C ANISOU 100 CB LEU A 161 13274 13706 14974 -16 -270 -250 C ATOM 101 CG LEU A 161 -68.608 64.712 -24.923 1.00103.21 C ANISOU 101 CG LEU A 161 12367 12693 14154 -193 -341 -279 C ATOM 102 CD1 LEU A 161 -67.230 64.104 -25.135 1.00 92.81 C ANISOU 102 CD1 LEU A 161 11102 11335 12827 -259 -357 -330 C ATOM 103 CD2 LEU A 161 -69.683 63.830 -25.544 1.00 88.78 C ANISOU 103 CD2 LEU A 161 10448 10841 12444 -262 -366 -161 C ATOM 104 OXT LEU A 161 -67.667 67.830 -21.737 1.00113.21 O ANISOU 104 OXT LEU A 161 13962 13941 15110 350 -550 -583 O TER 253 LYS B 148 ATOM 254 N ALA B 149 -52.967 49.517 -23.166 1.00 44.75 N ANISOU 254 N ALA B 149 5392 5363 6248 -86 86 -82 N ATOM 255 CA ALA B 149 -53.478 49.521 -24.531 1.00 53.55 C ANISOU 255 CA ALA B 149 6674 6454 7219 89 51 -92 C ATOM 256 C ALA B 149 -54.756 50.340 -24.637 1.00 57.59 C ANISOU 256 C ALA B 149 7159 6923 7797 -3 -42 -161 C ATOM 257 O ALA B 149 -54.949 51.077 -25.610 1.00 55.17 O ANISOU 257 O ALA B 149 6908 6621 7433 109 -11 -120 O ATOM 258 CB ALA B 149 -53.718 48.089 -25.009 1.00 40.64 C ANISOU 258 CB ALA B 149 5255 4751 5436 219 -96 -192 C ATOM 259 N GLU B 150 -55.639 50.234 -23.640 1.00 48.51 N ANISOU 259 N GLU B 150 5918 5747 6766 -179 -135 -234 N ATOM 260 CA GLU B 150 -56.867 51.025 -23.676 1.00 56.60 C ANISOU 260 CA GLU B 150 6896 6746 7863 -248 -200 -264 C ATOM 261 C GLU B 150 -56.566 52.519 -23.594 1.00 56.63 C ANISOU 261 C GLU B 150 6805 6795 7917 -269 -98 -217 C ATOM 262 O GLU B 150 -57.148 53.321 -24.340 1.00 56.16 O ANISOU 262 O GLU B 150 6769 6719 7851 -237 -113 -214 O ATOM 263 CB GLU B 150 -57.800 50.598 -22.545 1.00 48.12 C ANISOU 263 CB GLU B 150 5710 5666 6909 -374 -265 -272 C ATOM 264 CG GLU B 150 -59.194 51.199 -22.630 1.00 72.03 C ANISOU 264 CG GLU B 150 8676 8666 10026 -417 -332 -259 C ATOM 265 CD GLU B 150 -60.182 50.509 -21.709 1.00 79.91 C ANISOU 265 CD GLU B 150 9535 9654 11171 -488 -382 -171 C ATOM 266 OE1 GLU B 150 -59.813 49.481 -21.104 1.00 79.69 O ANISOU 266 OE1 GLU B 150 9477 9628 11174 -508 -387 -136 O ATOM 267 OE2 GLU B 150 -61.326 50.994 -21.588 1.00 96.61 O ANISOU 267 OE2 GLU B 150 11551 11767 13387 -510 -401 -100 O ATOM 268 N LEU B 151 -55.659 52.912 -22.694 1.00 43.87 N ANISOU 268 N LEU B 151 5086 5207 6374 -320 -36 -180 N ATOM 269 CA LEU B 151 -55.290 54.321 -22.585 1.00 57.60 C ANISOU 269 CA LEU B 151 6732 6927 8226 -343 -24 -127 C ATOM 270 C LEU B 151 -54.669 54.832 -23.880 1.00 64.22 C ANISOU 270 C LEU B 151 7563 7765 9072 -242 67 21 C ATOM 271 O LEU B 151 -54.983 55.942 -24.333 1.00 66.41 O ANISOU 271 O LEU B 151 7797 8018 9417 -241 60 65 O ATOM 272 CB LEU B 151 -54.331 54.529 -21.413 1.00 47.20 C ANISOU 272 CB LEU B 151 5329 5580 7023 -395 -60 -117 C ATOM 273 CG LEU B 151 -54.961 54.906 -20.071 1.00 60.95 C ANISOU 273 CG LEU B 151 7081 7313 8765 -416 -162 -241 C ATOM 274 CD1 LEU B 151 -53.895 54.989 -18.992 1.00 60.03 C ANISOU 274 CD1 LEU B 151 6937 7136 8736 -419 -254 -254 C ATOM 275 CD2 LEU B 151 -55.716 56.224 -20.187 1.00 53.02 C ANISOU 275 CD2 LEU B 151 6073 6271 7800 -404 -233 -276 C ATOM 276 N ASP B 152 -53.785 54.038 -24.490 1.00 56.21 N ANISOU 276 N ASP B 152 6593 6788 7976 -120 168 126 N ATOM 277 CA ASP B 152 -53.152 54.463 -25.735 1.00 68.03 C ANISOU 277 CA ASP B 152 8082 8320 9444 64 311 335 C ATOM 278 C ASP B 152 -54.168 54.581 -26.860 1.00 70.09 C ANISOU 278 C ASP B 152 8512 8591 9529 198 291 269 C ATOM 279 O ASP B 152 -54.088 55.501 -27.680 1.00 69.19 O ANISOU 279 O ASP B 152 8355 8495 9437 300 380 418 O ATOM 280 CB ASP B 152 -52.038 53.492 -26.120 1.00 56.54 C ANISOU 280 CB ASP B 152 6670 6927 7884 242 447 476 C ATOM 281 CG ASP B 152 -50.878 53.527 -25.150 1.00 75.27 C ANISOU 281 CG ASP B 152 8842 9276 10480 121 470 600 C ATOM 282 OD1 ASP B 152 -50.909 54.354 -24.214 1.00 73.72 O ANISOU 282 OD1 ASP B 152 8501 8995 10514 -78 344 562 O ATOM 283 OD2 ASP B 152 -49.936 52.727 -25.323 1.00 74.71 O ANISOU 283 OD2 ASP B 152 8779 9259 10348 250 587 728 O ATOM 284 N GLU B 153 -55.136 53.663 -26.917 1.00 65.78 N ANISOU 284 N GLU B 153 8144 8009 8840 202 149 69 N ATOM 285 CA GLU B 153 -56.182 53.764 -27.928 1.00 64.86 C ANISOU 285 CA GLU B 153 8197 7852 8596 317 51 -15 C ATOM 286 C GLU B 153 -57.004 55.032 -27.744 1.00 68.23 C ANISOU 286 C GLU B 153 8501 8261 9165 167 23 -32 C ATOM 287 O GLU B 153 -57.311 55.731 -28.719 1.00 73.85 O ANISOU 287 O GLU B 153 9268 8976 9815 288 51 16 O ATOM 288 CB GLU B 153 -57.085 52.531 -27.878 1.00 64.37 C ANISOU 288 CB GLU B 153 8298 7691 8469 303 -180 -199 C ATOM 289 CG GLU B 153 -57.221 51.814 -29.210 1.00 74.85 C ANISOU 289 CG GLU B 153 9933 8954 9554 611 -303 -258 C ATOM 290 CD GLU B 153 -55.937 51.129 -29.627 1.00 82.41 C ANISOU 290 CD GLU B 153 11018 9985 10309 880 -164 -164 C ATOM 291 OE1 GLU B 153 -55.084 50.876 -28.748 1.00 85.05 O ANISOU 291 OE1 GLU B 153 11192 10384 10740 758 -37 -88 O ATOM 292 OE2 GLU B 153 -55.779 50.842 -30.832 1.00 85.92 O ANISOU 292 OE2 GLU B 153 11741 10426 10480 1252 -185 -160 O ATOM 293 N VAL B 154 -57.373 55.345 -26.498 1.00 66.45 N ANISOU 293 N VAL B 154 8128 8020 9101 -55 -29 -98 N ATOM 294 CA VAL B 154 -58.113 56.579 -26.232 1.00 68.76 C ANISOU 294 CA VAL B 154 8326 8297 9505 -158 -62 -119 C ATOM 295 C VAL B 154 -57.307 57.792 -26.688 1.00 79.43 C ANISOU 295 C VAL B 154 9573 9654 10952 -116 37 40 C ATOM 296 O VAL B 154 -57.808 58.658 -27.418 1.00 71.08 O ANISOU 296 O VAL B 154 8521 8588 9900 -77 42 72 O ATOM 297 CB VAL B 154 -58.480 56.678 -24.741 1.00 64.61 C ANISOU 297 CB VAL B 154 7700 7770 9077 -303 -118 -197 C ATOM 298 CG1 VAL B 154 -59.008 58.065 -24.415 1.00 65.50 C ANISOU 298 CG1 VAL B 154 7745 7866 9278 -347 -154 -215 C ATOM 299 CG2 VAL B 154 -59.495 55.613 -24.363 1.00 61.03 C ANISOU 299 CG2 VAL B 154 7283 7312 8595 -339 -197 -267 C ATOM 300 N HIS B 155 -56.034 57.853 -26.284 1.00 74.42 N ANISOU 300 N HIS B 155 8820 9019 10435 -127 103 176 N ATOM 301 CA HIS B 155 -55.197 59.002 -26.628 1.00 78.78 C ANISOU 301 CA HIS B 155 9202 9538 11192 -112 161 402 C ATOM 302 C HIS B 155 -55.005 59.124 -28.136 1.00 82.30 C ANISOU 302 C HIS B 155 9690 10054 11527 113 333 601 C ATOM 303 O HIS B 155 -54.942 60.237 -28.673 1.00 87.66 O ANISOU 303 O HIS B 155 10251 10710 12344 138 373 769 O ATOM 304 CB HIS B 155 -53.848 58.898 -25.918 1.00 75.65 C ANISOU 304 CB HIS B 155 8646 9098 11001 -165 163 551 C ATOM 305 CG HIS B 155 -53.928 59.105 -24.438 1.00 86.32 C ANISOU 305 CG HIS B 155 9968 10354 12475 -330 -40 375 C ATOM 306 ND1 HIS B 155 -53.067 58.496 -23.552 1.00 96.51 N ANISOU 306 ND1 HIS B 155 11218 11614 13837 -375 -86 376 N ATOM 307 CD2 HIS B 155 -54.764 59.864 -23.690 1.00 88.25 C ANISOU 307 CD2 HIS B 155 10249 10534 12750 -406 -211 196 C ATOM 308 CE1 HIS B 155 -53.371 58.867 -22.321 1.00 97.32 C ANISOU 308 CE1 HIS B 155 11353 11633 13992 -454 -287 194 C ATOM 309 NE2 HIS B 155 -54.396 59.698 -22.378 1.00 91.21 N ANISOU 309 NE2 HIS B 155 10632 10842 13181 -455 -359 87 N ATOM 310 N GLN B 156 -54.916 57.992 -28.837 1.00 79.19 N ANISOU 310 N GLN B 156 9484 9737 10869 318 421 588 N ATOM 311 CA GLN B 156 -54.819 58.028 -30.292 1.00 84.73 C ANISOU 311 CA GLN B 156 10308 10515 11369 635 574 749 C ATOM 312 C GLN B 156 -56.104 58.557 -30.911 1.00 87.33 C ANISOU 312 C GLN B 156 10770 10813 11597 651 471 597 C ATOM 313 O GLN B 156 -56.064 59.353 -31.856 1.00 83.92 O ANISOU 313 O GLN B 156 10322 10422 11143 821 589 777 O ATOM 314 CB GLN B 156 -54.509 56.633 -30.833 1.00 79.94 C ANISOU 314 CB GLN B 156 9952 9968 10455 906 619 709 C ATOM 315 CG GLN B 156 -54.463 56.555 -32.353 1.00 88.24 C ANISOU 315 CG GLN B 156 11228 11101 11199 1346 751 839 C ATOM 316 CD GLN B 156 -54.533 55.131 -32.872 1.00 95.28 C ANISOU 316 CD GLN B 156 12481 11990 11732 1642 659 672 C ATOM 317 OE1 GLN B 156 -55.483 54.400 -32.590 1.00 99.16 O ANISOU 317 OE1 GLN B 156 13150 12358 12170 1518 372 356 O ATOM 318 NE2 GLN B 156 -53.524 54.732 -33.637 1.00 91.33 N ANISOU 318 NE2 GLN B 156 12084 11612 11005 2060 887 914 N ATOM 319 N ALA B 157 -57.252 58.116 -30.396 1.00 87.76 N ANISOU 319 N ALA B 157 10936 10796 11613 488 260 306 N ATOM 320 CA ALA B 157 -58.526 58.589 -30.923 1.00 88.90 C ANISOU 320 CA ALA B 157 11181 10893 11705 482 138 175 C ATOM 321 C ALA B 157 -58.703 60.082 -30.692 1.00 95.13 C ANISOU 321 C ALA B 157 11768 11671 12706 334 171 258 C ATOM 322 O ALA B 157 -59.352 60.761 -31.496 1.00 94.23 O ANISOU 322 O ALA B 157 11708 11551 12543 412 163 264 O ATOM 323 CB ALA B 157 -59.678 57.810 -30.290 1.00 73.92 C ANISOU 323 CB ALA B 157 9361 8910 9817 320 -90 -69 C ATOM 324 N LEU B 158 -58.132 60.609 -29.606 1.00 84.50 N ANISOU 324 N LEU B 158 10210 10300 11596 139 170 310 N ATOM 325 CA LEU B 158 -58.274 62.033 -29.312 1.00 89.79 C ANISOU 325 CA LEU B 158 10715 10913 12489 13 125 366 C ATOM 326 C LEU B 158 -57.548 62.905 -30.325 1.00 98.60 C ANISOU 326 C LEU B 158 11710 12046 13708 151 272 669 C ATOM 327 O LEU B 158 -57.937 64.059 -30.541 1.00102.72 O ANISOU 327 O LEU B 158 12146 12520 14365 100 230 716 O ATOM 328 CB LEU B 158 -57.751 62.333 -27.913 1.00 91.54 C ANISOU 328 CB LEU B 158 10793 11059 12930 -168 12 333 C ATOM 329 CG LEU B 158 -58.485 61.622 -26.786 1.00 94.03 C ANISOU 329 CG LEU B 158 11200 11379 13149 -264 -98 86 C ATOM 330 CD1 LEU B 158 -57.712 61.769 -25.484 1.00 91.39 C ANISOU 330 CD1 LEU B 158 10775 10975 12972 -352 -201 68 C ATOM 331 CD2 LEU B 158 -59.894 62.172 -26.657 1.00 90.16 C ANISOU 331 CD2 LEU B 158 10764 10882 12610 -302 -183 -62 C ATOM 332 N GLU B 159 -56.479 62.391 -30.934 1.00105.30 N ANISOU 332 N GLU B 159 12531 12968 14509 346 459 914 N ATOM 333 CA GLU B 159 -55.739 63.189 -31.903 1.00104.42 C ANISOU 333 CA GLU B 159 12258 12898 14518 528 653 1302 C ATOM 334 C GLU B 159 -56.597 63.505 -33.119 1.00112.35 C ANISOU 334 C GLU B 159 13439 13966 15282 741 720 1284 C ATOM 335 O GLU B 159 -56.515 64.605 -33.678 1.00117.67 O ANISOU 335 O GLU B 159 13957 14634 16116 785 799 1521 O ATOM 336 CB GLU B 159 -54.468 62.454 -32.320 1.00108.83 C ANISOU 336 CB GLU B 159 12764 13557 15028 768 885 1608 C ATOM 337 CG GLU B 159 -53.606 62.023 -31.156 1.00107.42 C ANISOU 337 CG GLU B 159 12430 13312 15074 569 807 1618 C ATOM 338 CD GLU B 159 -52.708 60.863 -31.514 1.00119.82 C ANISOU 338 CD GLU B 159 14073 15004 16449 822 1010 1774 C ATOM 339 OE1 GLU B 159 -52.884 60.293 -32.612 1.00112.99 O ANISOU 339 OE1 GLU B 159 13447 14269 15214 1177 1173 1805 O ATOM 340 OE2 GLU B 159 -51.828 60.519 -30.700 1.00138.77 O ANISOU 340 OE2 GLU B 159 16316 17360 19049 698 986 1856 O ATOM 341 N ASP B 160 -57.433 62.556 -33.537 1.00111.02 N ANISOU 341 N ASP B 160 13592 13832 14757 875 653 1012 N ATOM 342 CA ASP B 160 -58.307 62.746 -34.694 1.00110.58 C ANISOU 342 CA ASP B 160 13759 13803 14453 1102 649 948 C ATOM 343 C ASP B 160 -59.607 63.415 -34.243 1.00113.51 C ANISOU 343 C ASP B 160 14119 14074 14937 824 432 693 C ATOM 344 O ASP B 160 -60.698 62.845 -34.287 1.00115.80 O ANISOU 344 O ASP B 160 14614 14308 15076 797 244 417 O ATOM 345 CB ASP B 160 -58.560 61.414 -35.389 1.00113.15 C ANISOU 345 CB ASP B 160 14455 14154 14383 1407 592 780 C ATOM 346 CG ASP B 160 -59.396 61.561 -36.643 1.00123.89 C ANISOU 346 CG ASP B 160 16097 15511 15464 1704 534 704 C ATOM 347 OD1 ASP B 160 -58.889 62.126 -37.634 1.00122.34 O ANISOU 347 OD1 ASP B 160 15909 15426 15150 2037 768 990 O ATOM 348 OD2 ASP B 160 -60.565 61.121 -36.632 1.00130.88 O ANISOU 348 OD2 ASP B 160 17182 16275 16273 1616 246 387 O ATOM 349 N LEU B 161 -59.465 64.660 -33.798 1.00114.47 N ANISOU 349 N LEU B 161 13981 14151 15360 628 438 817 N ATOM 350 CA LEU B 161 -60.591 65.436 -33.287 1.00114.26 C ANISOU 350 CA LEU B 161 13928 14041 15447 397 256 610 C ATOM 351 C LEU B 161 -60.927 66.602 -34.208 1.00116.46 C ANISOU 351 C LEU B 161 14162 14323 15766 486 315 750 C ATOM 352 O LEU B 161 -60.925 66.466 -35.429 1.00120.36 O ANISOU 352 O LEU B 161 14795 14892 16043 775 443 865 O ATOM 353 CB LEU B 161 -60.290 65.956 -31.881 1.00110.01 C ANISOU 353 CB LEU B 161 13186 13413 15198 122 135 569 C ATOM 354 CG LEU B 161 -61.155 65.402 -30.750 1.00105.52 C ANISOU 354 CG LEU B 161 12704 12814 14574 -43 -31 268 C ATOM 355 CD1 LEU B 161 -60.608 65.828 -29.395 1.00106.20 C ANISOU 355 CD1 LEU B 161 12649 12820 14881 -203 -144 245 C ATOM 356 CD2 LEU B 161 -62.590 65.862 -30.914 1.00101.26 C ANISOU 356 CD2 LEU B 161 12246 12259 13970 -82 -127 106 C ATOM 357 OXT LEU B 161 -61.209 67.709 -33.749 1.00113.91 O ANISOU 357 OXT LEU B 161 13684 13922 15676 302 223 749 O TER 358 LEU B 161 ATOM 359 N MET C 1 -61.251 53.894 -28.842 1.00101.61 N ANISOU 359 N MET C 1 13515 11169 13924 1423 -2362 2137 N ATOM 360 CA MET C 1 -62.141 52.746 -28.969 1.00116.16 C ANISOU 360 CA MET C 1 15357 12842 15937 1366 -2543 2240 C ATOM 361 C MET C 1 -63.234 53.006 -30.001 1.00109.79 C ANISOU 361 C MET C 1 14578 11922 15215 1330 -2655 2224 C ATOM 362 O MET C 1 -63.173 53.977 -30.754 1.00 97.59 O ANISOU 362 O MET C 1 13086 10442 13552 1375 -2572 2103 O ATOM 363 CB MET C 1 -62.766 52.400 -27.617 1.00114.94 C ANISOU 363 CB MET C 1 15056 12738 15880 1300 -2494 2479 C ATOM 364 CG MET C 1 -63.524 53.549 -26.974 1.00116.72 C ANISOU 364 CG MET C 1 15190 13130 16029 1298 -2313 2586 C ATOM 365 SD MET C 1 -64.391 53.061 -25.472 1.00160.14 S ANISOU 365 SD MET C 1 20523 18712 21609 1331 -2208 2953 S ATOM 366 CE MET C 1 -65.553 51.866 -26.127 1.00128.39 C ANISOU 366 CE MET C 1 16356 14431 17996 1183 -2437 3192 C ATOM 367 N ASP C 2 -64.239 52.127 -30.026 1.00118.96 N ANISOU 367 N ASP C 2 15686 12891 16621 1245 -2867 2370 N ATOM 368 CA ASP C 2 -65.316 52.259 -31.002 1.00109.58 C ANISOU 368 CA ASP C 2 14525 11537 15573 1204 -3054 2364 C ATOM 369 C ASP C 2 -66.265 53.392 -30.628 1.00114.14 C ANISOU 369 C ASP C 2 14942 12264 16161 1115 -2860 2504 C ATOM 370 O ASP C 2 -66.577 54.252 -31.459 1.00109.79 O ANISOU 370 O ASP C 2 14456 11732 15527 1133 -2838 2382 O ATOM 371 CB ASP C 2 -66.077 50.938 -31.122 1.00118.94 C ANISOU 371 CB ASP C 2 15673 12409 17110 1127 -3420 2512 C ATOM 372 CG ASP C 2 -67.236 51.018 -32.098 1.00138.04 C ANISOU 372 CG ASP C 2 18106 14633 19710 1060 -3650 2482 C ATOM 373 OD1 ASP C 2 -67.352 52.039 -32.809 1.00126.61 O ANISOU 373 OD1 ASP C 2 16758 13242 18105 1132 -3590 2363 O ATOM 374 OD2 ASP C 2 -68.035 50.059 -32.152 1.00148.58 O ANISOU 374 OD2 ASP C 2 19335 15767 21352 919 -3884 2565 O ATOM 375 N LYS C 3 -66.738 53.406 -29.379 1.00120.17 N ANISOU 375 N LYS C 3 15508 13147 17006 1060 -2706 2774 N ATOM 376 CA LYS C 3 -67.713 54.413 -28.971 1.00115.16 C ANISOU 376 CA LYS C 3 14734 12659 16362 1035 -2518 2943 C ATOM 377 C LYS C 3 -67.096 55.806 -28.923 1.00107.53 C ANISOU 377 C LYS C 3 13869 11918 15071 1120 -2293 2731 C ATOM 378 O LYS C 3 -67.750 56.790 -29.288 1.00105.90 O ANISOU 378 O LYS C 3 13645 11770 14822 1105 -2220 2716 O ATOM 379 CB LYS C 3 -68.315 54.041 -27.616 1.00118.62 C ANISOU 379 CB LYS C 3 14959 13194 16918 1053 -2376 3326 C ATOM 380 CG LYS C 3 -69.370 52.948 -27.691 1.00114.64 C ANISOU 380 CG LYS C 3 14240 12452 16866 934 -2592 3672 C ATOM 381 CD LYS C 3 -70.521 53.370 -28.590 1.00118.01 C ANISOU 381 CD LYS C 3 14594 12766 17478 819 -2694 3689 C ATOM 382 CE LYS C 3 -71.579 52.285 -28.687 1.00111.01 C ANISOU 382 CE LYS C 3 13469 11683 17026 637 -2870 3902 C ATOM 383 NZ LYS C 3 -72.708 52.692 -29.569 1.00109.58 N ANISOU 383 NZ LYS C 3 13209 11374 17053 515 -3006 3911 N ATOM 384 N LEU C 4 -65.843 55.912 -28.477 1.00100.99 N ANISOU 384 N LEU C 4 13132 11190 14051 1201 -2214 2582 N ATOM 385 CA LEU C 4 -65.185 57.214 -28.426 1.00100.80 C ANISOU 385 CA LEU C 4 13176 11318 13806 1267 -2079 2408 C ATOM 386 C LEU C 4 -65.010 57.793 -29.825 1.00 90.60 C ANISOU 386 C LEU C 4 11960 9970 12494 1251 -2120 2220 C ATOM 387 O LEU C 4 -65.282 58.977 -30.062 1.00 81.80 O ANISOU 387 O LEU C 4 10838 8939 11304 1252 -2032 2167 O ATOM 388 CB LEU C 4 -63.835 57.093 -27.718 1.00 84.88 C ANISOU 388 CB LEU C 4 11214 9359 11677 1344 -2057 2318 C ATOM 389 CG LEU C 4 -62.997 58.371 -27.670 1.00 81.36 C ANISOU 389 CG LEU C 4 10811 9000 11103 1397 -2007 2161 C ATOM 390 CD1 LEU C 4 -63.739 59.471 -26.928 1.00 89.96 C ANISOU 390 CD1 LEU C 4 11901 10202 12077 1459 -1932 2204 C ATOM 391 CD2 LEU C 4 -61.647 58.103 -27.030 1.00 82.49 C ANISOU 391 CD2 LEU C 4 10982 9142 11217 1456 -2050 2102 C ATOM 392 N ARG C 5 -64.557 56.966 -30.770 1.00 83.76 N ANISOU 392 N ARG C 5 11184 8965 11675 1277 -2254 2126 N ATOM 393 CA ARG C 5 -64.391 57.434 -32.142 1.00 93.21 C ANISOU 393 CA ARG C 5 12484 10123 12808 1346 -2274 1975 C ATOM 394 C ARG C 5 -65.730 57.787 -32.777 1.00 87.67 C ANISOU 394 C ARG C 5 11776 9348 12186 1282 -2348 2002 C ATOM 395 O ARG C 5 -65.811 58.738 -33.564 1.00 75.56 O ANISOU 395 O ARG C 5 10280 7865 10566 1321 -2277 1912 O ATOM 396 CB ARG C 5 -63.662 56.375 -32.970 1.00 89.67 C ANISOU 396 CB ARG C 5 12191 9544 12337 1483 -2414 1877 C ATOM 397 CG ARG C 5 -62.610 56.933 -33.912 1.00 92.11 C ANISOU 397 CG ARG C 5 12581 9932 12486 1668 -2290 1774 C ATOM 398 CD ARG C 5 -61.468 55.947 -34.104 1.00 87.51 C ANISOU 398 CD ARG C 5 12100 9310 11841 1840 -2325 1742 C ATOM 399 NE ARG C 5 -60.820 55.616 -32.840 1.00 93.94 N ANISOU 399 NE ARG C 5 12794 10180 12717 1740 -2279 1818 N ATOM 400 CZ ARG C 5 -59.735 54.861 -32.729 1.00 99.09 C ANISOU 400 CZ ARG C 5 13485 10825 13338 1853 -2279 1818 C ATOM 401 NH1 ARG C 5 -59.141 54.345 -33.793 1.00105.58 N ANISOU 401 NH1 ARG C 5 14467 11603 14045 2102 -2299 1762 N ATOM 402 NH2 ARG C 5 -59.234 54.617 -31.521 1.00 94.26 N ANISOU 402 NH2 ARG C 5 12769 10258 12789 1753 -2255 1882 N ATOM 403 N GLU C 6 -66.791 57.052 -32.435 1.00 86.77 N ANISOU 403 N GLU C 6 11587 9109 12275 1181 -2492 2162 N ATOM 404 CA GLU C 6 -68.118 57.387 -32.939 1.00 88.20 C ANISOU 404 CA GLU C 6 11716 9201 12595 1101 -2581 2238 C ATOM 405 C GLU C 6 -68.596 58.724 -32.385 1.00 86.30 C ANISOU 405 C GLU C 6 11360 9171 12259 1064 -2334 2310 C ATOM 406 O GLU C 6 -69.178 59.534 -33.117 1.00 78.55 O ANISOU 406 O GLU C 6 10396 8191 11256 1049 -2323 2251 O ATOM 407 CB GLU C 6 -69.107 56.274 -32.590 1.00 92.16 C ANISOU 407 CB GLU C 6 12090 9498 13428 992 -2805 2481 C ATOM 408 CG GLU C 6 -70.445 56.374 -33.306 1.00104.34 C ANISOU 408 CG GLU C 6 13576 10858 15211 903 -3004 2574 C ATOM 409 CD GLU C 6 -70.363 55.960 -34.764 1.00105.07 C ANISOU 409 CD GLU C 6 13922 10695 15307 994 -3339 2322 C ATOM 410 OE1 GLU C 6 -69.329 55.384 -35.166 1.00103.65 O ANISOU 410 OE1 GLU C 6 13949 10468 14966 1144 -3422 2122 O ATOM 411 OE2 GLU C 6 -71.333 56.209 -35.510 1.00 97.25 O ANISOU 411 OE2 GLU C 6 12940 9548 14463 954 -3527 2328 O ATOM 412 N LYS C 7 -68.358 58.974 -31.095 1.00 82.51 N ANISOU 412 N LYS C 7 10792 8861 11699 1084 -2156 2424 N ATOM 413 CA LYS C 7 -68.720 60.263 -30.514 1.00 86.64 C ANISOU 413 CA LYS C 7 11269 9572 12080 1119 -1960 2458 C ATOM 414 C LYS C 7 -67.921 61.396 -31.145 1.00 74.05 C ANISOU 414 C LYS C 7 9773 8045 10320 1157 -1905 2217 C ATOM 415 O LYS C 7 -68.450 62.492 -31.362 1.00 78.53 O ANISOU 415 O LYS C 7 10328 8682 10829 1152 -1830 2192 O ATOM 416 CB LYS C 7 -68.509 60.237 -29.000 1.00 77.66 C ANISOU 416 CB LYS C 7 10091 8581 10834 1221 -1829 2598 C ATOM 417 CG LYS C 7 -69.427 59.281 -28.259 1.00 86.80 C ANISOU 417 CG LYS C 7 11094 9718 12169 1221 -1813 2940 C ATOM 418 CD LYS C 7 -69.040 59.174 -26.794 1.00 99.10 C ANISOU 418 CD LYS C 7 12659 11435 13558 1397 -1670 3065 C ATOM 419 CE LYS C 7 -69.899 58.148 -26.074 1.00107.89 C ANISOU 419 CE LYS C 7 13576 12539 14878 1424 -1618 3480 C ATOM 420 NZ LYS C 7 -69.490 57.981 -24.653 1.00 92.43 N ANISOU 420 NZ LYS C 7 11654 10751 12714 1655 -1464 3613 N ATOM 421 N ILE C 8 -66.645 61.150 -31.451 1.00 77.28 N ANISOU 421 N ILE C 8 10253 8430 10678 1202 -1936 2076 N ATOM 422 CA ILE C 8 -65.830 62.174 -32.100 1.00 78.11 C ANISOU 422 CA ILE C 8 10389 8585 10705 1245 -1876 1935 C ATOM 423 C ILE C 8 -66.346 62.459 -33.506 1.00 76.03 C ANISOU 423 C ILE C 8 10172 8263 10452 1250 -1896 1871 C ATOM 424 O ILE C 8 -66.406 63.618 -33.939 1.00 82.27 O ANISOU 424 O ILE C 8 10941 9118 11202 1254 -1816 1826 O ATOM 425 CB ILE C 8 -64.350 61.749 -32.110 1.00 77.66 C ANISOU 425 CB ILE C 8 10350 8516 10640 1315 -1885 1883 C ATOM 426 CG1 ILE C 8 -63.808 61.681 -30.682 1.00 79.42 C ANISOU 426 CG1 ILE C 8 10545 8790 10843 1323 -1893 1921 C ATOM 427 CG2 ILE C 8 -63.524 62.712 -32.943 1.00 84.01 C ANISOU 427 CG2 ILE C 8 11123 9355 11442 1374 -1813 1832 C ATOM 428 CD1 ILE C 8 -62.421 61.091 -30.586 1.00 88.56 C ANISOU 428 CD1 ILE C 8 11700 9916 12034 1374 -1923 1901 C ATOM 429 N ASN C 9 -66.719 61.409 -34.244 1.00 71.86 N ANISOU 429 N ASN C 9 9730 7592 9984 1272 -2038 1859 N ATOM 430 CA ASN C 9 -67.309 61.607 -35.564 1.00 76.98 C ANISOU 430 CA ASN C 9 10475 8154 10620 1323 -2113 1781 C ATOM 431 C ASN C 9 -68.607 62.397 -35.472 1.00 72.30 C ANISOU 431 C ASN C 9 9797 7583 10090 1203 -2092 1847 C ATOM 432 O ASN C 9 -68.863 63.282 -36.295 1.00 73.00 O ANISOU 432 O ASN C 9 9918 7702 10117 1234 -2042 1776 O ATOM 433 CB ASN C 9 -67.551 60.259 -36.243 1.00 74.27 C ANISOU 433 CB ASN C 9 10282 7592 10346 1395 -2372 1738 C ATOM 434 CG ASN C 9 -66.270 59.617 -36.739 1.00 97.47 C ANISOU 434 CG ASN C 9 13365 10516 13151 1603 -2379 1643 C ATOM 435 OD1 ASN C 9 -65.172 60.010 -36.346 1.00103.59 O ANISOU 435 OD1 ASN C 9 14068 11443 13849 1645 -2184 1664 O ATOM 436 ND2 ASN C 9 -66.405 58.624 -37.610 1.00107.71 N ANISOU 436 ND2 ASN C 9 14877 11613 14435 1759 -2632 1548 N ATOM 437 N ALA C 10 -69.436 62.095 -34.469 1.00 72.30 N ANISOU 437 N ALA C 10 9676 7582 10214 1093 -2106 2017 N ATOM 438 CA ALA C 10 -70.682 62.836 -34.290 1.00 75.07 C ANISOU 438 CA ALA C 10 9922 7976 10625 1013 -2050 2135 C ATOM 439 C ALA C 10 -70.412 64.300 -33.965 1.00 76.01 C ANISOU 439 C ALA C 10 10024 8287 10569 1046 -1851 2069 C ATOM 440 O ALA C 10 -71.114 65.193 -34.454 1.00 79.86 O ANISOU 440 O ALA C 10 10498 8803 11042 1021 -1809 2052 O ATOM 441 CB ALA C 10 -71.525 62.187 -33.193 1.00 72.26 C ANISOU 441 CB ALA C 10 9408 7614 10435 953 -2051 2415 C ATOM 442 N ALA C 11 -69.392 64.566 -33.146 1.00 72.95 N ANISOU 442 N ALA C 11 9645 8003 10071 1105 -1769 2028 N ATOM 443 CA ALA C 11 -69.049 65.944 -32.807 1.00 77.10 C ANISOU 443 CA ALA C 11 10169 8646 10479 1145 -1676 1953 C ATOM 444 C ALA C 11 -68.576 66.710 -34.037 1.00 73.76 C ANISOU 444 C ALA C 11 9766 8204 10055 1146 -1663 1828 C ATOM 445 O ALA C 11 -68.995 67.851 -34.275 1.00 76.66 O ANISOU 445 O ALA C 11 10113 8620 10392 1133 -1615 1798 O ATOM 446 CB ALA C 11 -67.982 65.964 -31.712 1.00 64.09 C ANISOU 446 CB ALA C 11 8541 7046 8765 1217 -1684 1928 C ATOM 447 N ARG C 12 -67.694 66.096 -34.833 1.00 69.53 N ANISOU 447 N ARG C 12 9269 7607 9540 1197 -1690 1778 N ATOM 448 CA ARG C 12 -67.229 66.753 -36.052 1.00 77.90 C ANISOU 448 CA ARG C 12 10338 8675 10584 1268 -1631 1726 C ATOM 449 C ARG C 12 -68.377 66.977 -37.029 1.00 74.81 C ANISOU 449 C ARG C 12 10008 8244 10172 1261 -1651 1693 C ATOM 450 O ARG C 12 -68.444 68.020 -37.692 1.00 75.21 O ANISOU 450 O ARG C 12 10033 8343 10199 1284 -1571 1672 O ATOM 451 CB ARG C 12 -66.111 65.940 -36.709 1.00 83.25 C ANISOU 451 CB ARG C 12 11068 9317 11246 1411 -1624 1723 C ATOM 452 CG ARG C 12 -65.841 66.344 -38.156 1.00 93.60 C ANISOU 452 CG ARG C 12 12426 10645 12493 1580 -1535 1718 C ATOM 453 CD ARG C 12 -64.381 66.191 -38.562 1.00 97.94 C ANISOU 453 CD ARG C 12 12928 11241 13044 1765 -1421 1813 C ATOM 454 NE ARG C 12 -63.906 64.816 -38.466 1.00107.39 N ANISOU 454 NE ARG C 12 14242 12377 14184 1869 -1495 1789 N ATOM 455 CZ ARG C 12 -62.849 64.438 -37.761 1.00104.64 C ANISOU 455 CZ ARG C 12 13802 12047 13908 1867 -1473 1863 C ATOM 456 NH1 ARG C 12 -62.117 65.312 -37.090 1.00110.57 N ANISOU 456 NH1 ARG C 12 14346 12849 14818 1769 -1417 1966 N ATOM 457 NH2 ARG C 12 -62.511 63.152 -37.737 1.00107.25 N ANISOU 457 NH2 ARG C 12 14260 12317 14174 1970 -1550 1829 N TER 473 HOH C 215 ATOM 474 N MET D 1 -57.751 65.010 -18.667 1.00137.69 N ANISOU 474 N MET D 1 19229 15658 17428 2926 -3905 1154 N ATOM 475 CA MET D 1 -56.414 65.203 -18.122 1.00143.54 C ANISOU 475 CA MET D 1 19982 16174 18382 2874 -4251 997 C ATOM 476 C MET D 1 -55.433 65.653 -19.202 1.00139.35 C ANISOU 476 C MET D 1 19124 15434 18390 2525 -4414 1052 C ATOM 477 O MET D 1 -55.607 65.345 -20.382 1.00143.19 O ANISOU 477 O MET D 1 19362 15981 19063 2329 -4194 1244 O ATOM 478 CB MET D 1 -55.918 63.911 -17.473 1.00124.83 C ANISOU 478 CB MET D 1 17643 13864 15924 2940 -4173 1059 C ATOM 479 CG MET D 1 -55.491 62.849 -18.474 1.00118.36 C ANISOU 479 CG MET D 1 16525 13060 15387 2671 -3992 1276 C ATOM 480 SD MET D 1 -54.692 61.421 -17.719 1.00132.74 S ANISOU 480 SD MET D 1 18368 14897 17168 2719 -3970 1325 S ATOM 481 CE MET D 1 -54.031 60.597 -19.169 1.00106.24 C ANISOU 481 CE MET D 1 14609 11552 14206 2315 -3720 1499 C ATOM 482 N ASP D 2 -54.395 66.373 -18.784 1.00137.26 N ANISOU 482 N ASP D 2 18854 14916 18383 2462 -4792 908 N ATOM 483 CA ASP D 2 -53.312 66.820 -19.670 1.00138.53 C ANISOU 483 CA ASP D 2 18655 14871 19110 2145 -4940 1025 C ATOM 484 C ASP D 2 -53.906 67.579 -20.854 1.00123.90 C ANISOU 484 C ASP D 2 16613 13057 17408 2006 -4797 1140 C ATOM 485 O ASP D 2 -54.752 68.467 -20.656 1.00120.29 O ANISOU 485 O ASP D 2 16347 12611 16746 2129 -4868 998 O ATOM 486 CB ASP D 2 -52.466 65.614 -20.062 1.00142.68 C ANISOU 486 CB ASP D 2 18939 15432 19842 2002 -4774 1229 C ATOM 487 CG ASP D 2 -51.125 66.015 -20.656 1.00144.75 C ANISOU 487 CG ASP D 2 18837 15480 20679 1739 -4933 1378 C ATOM 488 OD1 ASP D 2 -50.837 67.234 -20.723 1.00150.65 O ANISOU 488 OD1 ASP D 2 19512 16027 21702 1642 -5207 1326 O ATOM 489 OD2 ASP D 2 -50.378 65.111 -21.087 1.00135.15 O ANISOU 489 OD2 ASP D 2 17395 14303 19651 1636 -4767 1575 O ATOM 490 N LYS D 3 -53.524 67.245 -22.083 1.00126.88 N ANISOU 490 N LYS D 3 16636 13471 18101 1788 -4573 1399 N ATOM 491 CA LYS D 3 -54.056 67.896 -23.265 1.00117.24 C ANISOU 491 CA LYS D 3 15230 12302 17015 1675 -4404 1529 C ATOM 492 C LYS D 3 -55.334 67.240 -23.768 1.00104.46 C ANISOU 492 C LYS D 3 13707 10966 15016 1728 -3985 1551 C ATOM 493 O LYS D 3 -55.931 67.729 -24.734 1.00108.14 O ANISOU 493 O LYS D 3 14060 11521 15507 1633 -3779 1611 O ATOM 494 CB LYS D 3 -53.000 67.923 -24.371 1.00117.04 C ANISOU 494 CB LYS D 3 14775 12213 17481 1451 -4297 1812 C ATOM 495 CG LYS D 3 -51.745 68.706 -23.990 1.00123.76 C ANISOU 495 CG LYS D 3 15453 12794 18777 1313 -4650 1823 C ATOM 496 CD LYS D 3 -52.103 70.080 -23.461 1.00122.31 C ANISOU 496 CD LYS D 3 15434 12425 18612 1327 -5012 1601 C ATOM 497 CE LYS D 3 -51.581 70.241 -22.048 1.00135.50 C ANISOU 497 CE LYS D 3 17370 13877 20239 1417 -5453 1335 C ATOM 498 NZ LYS D 3 -51.969 71.559 -21.487 1.00128.17 N ANISOU 498 NZ LYS D 3 16673 12749 19278 1480 -5834 1076 N ATOM 499 N LEU D 4 -55.765 66.144 -23.146 1.00112.35 N ANISOU 499 N LEU D 4 14890 12128 15668 1840 -3805 1496 N ATOM 500 CA LEU D 4 -57.067 65.580 -23.485 1.00115.11 C ANISOU 500 CA LEU D 4 15316 12737 15684 1857 -3410 1509 C ATOM 501 C LEU D 4 -58.187 66.516 -23.051 1.00109.46 C ANISOU 501 C LEU D 4 14812 12069 14710 2019 -3462 1393 C ATOM 502 O LEU D 4 -59.133 66.762 -23.812 1.00 91.69 O ANISOU 502 O LEU D 4 12506 9946 12385 1948 -3222 1435 O ATOM 503 CB LEU D 4 -57.216 64.198 -22.844 1.00102.08 C ANISOU 503 CB LEU D 4 13769 11215 13801 1941 -3246 1535 C ATOM 504 CG LEU D 4 -58.464 63.830 -22.035 1.00 95.43 C ANISOU 504 CG LEU D 4 13146 10551 12561 2146 -3086 1525 C ATOM 505 CD1 LEU D 4 -59.645 63.504 -22.948 1.00101.61 C ANISOU 505 CD1 LEU D 4 13826 11501 13281 2030 -2743 1639 C ATOM 506 CD2 LEU D 4 -58.192 62.660 -21.094 1.00 95.84 C ANISOU 506 CD2 LEU D 4 13294 10652 12467 2272 -3059 1566 C ATOM 507 N ARG D 5 -58.093 67.051 -21.835 1.00105.16 N ANISOU 507 N ARG D 5 14533 11416 14008 2273 -3793 1244 N ATOM 508 CA ARG D 5 -59.089 68.005 -21.367 1.00102.71 C ANISOU 508 CA ARG D 5 14466 11143 13415 2505 -3869 1129 C ATOM 509 C ARG D 5 -59.014 69.298 -22.167 1.00107.68 C ANISOU 509 C ARG D 5 14970 11622 14322 2358 -4045 1092 C ATOM 510 O ARG D 5 -60.047 69.878 -22.520 1.00102.08 O ANISOU 510 O ARG D 5 14304 11028 13453 2390 -3888 1083 O ATOM 511 CB ARG D 5 -58.894 68.259 -19.872 1.00114.02 C ANISOU 511 CB ARG D 5 16241 12506 14575 2842 -4154 938 C ATOM 512 CG ARG D 5 -59.841 69.282 -19.280 1.00114.17 C ANISOU 512 CG ARG D 5 16538 12588 14253 3116 -4189 784 C ATOM 513 CD ARG D 5 -59.911 69.181 -17.762 1.00109.66 C ANISOU 513 CD ARG D 5 16324 12070 13273 3498 -4260 622 C ATOM 514 NE ARG D 5 -58.601 69.007 -17.144 1.00108.56 N ANISOU 514 NE ARG D 5 16227 11704 13315 3454 -4598 472 N ATOM 515 CZ ARG D 5 -58.177 67.882 -16.581 1.00102.95 C ANISOU 515 CZ ARG D 5 15534 11062 12519 3518 -4507 540 C ATOM 516 NH1 ARG D 5 -58.944 66.806 -16.518 1.00106.13 N ANISOU 516 NH1 ARG D 5 15908 11744 12671 3627 -4095 766 N ATOM 517 NH2 ARG D 5 -56.952 67.839 -16.065 1.00103.08 N ANISOU 517 NH2 ARG D 5 15582 10845 12738 3460 -4850 393 N ATOM 518 N GLU D 6 -57.800 69.748 -22.489 1.00107.96 N ANISOU 518 N GLU D 6 14808 11407 14805 2178 -4341 1108 N ATOM 519 CA GLU D 6 -57.646 70.907 -23.363 1.00102.66 C ANISOU 519 CA GLU D 6 13930 10603 14472 1991 -4448 1143 C ATOM 520 C GLU D 6 -58.300 70.662 -24.720 1.00103.25 C ANISOU 520 C GLU D 6 13777 10882 14570 1810 -4004 1319 C ATOM 521 O GLU D 6 -58.964 71.551 -25.267 1.00105.26 O ANISOU 521 O GLU D 6 14011 11157 14827 1777 -3966 1305 O ATOM 522 CB GLU D 6 -56.159 71.240 -23.519 1.00110.23 C ANISOU 522 CB GLU D 6 14620 11315 15949 1773 -4702 1207 C ATOM 523 CG GLU D 6 -55.693 71.433 -24.959 1.00115.32 C ANISOU 523 CG GLU D 6 14837 11948 17031 1518 -4518 1494 C ATOM 524 CD GLU D 6 -55.663 72.887 -25.384 1.00114.69 C ANISOU 524 CD GLU D 6 14629 11708 17238 1400 -4710 1490 C ATOM 525 OE1 GLU D 6 -54.833 73.646 -24.841 1.00115.86 O ANISOU 525 OE1 GLU D 6 14747 11593 17683 1321 -5093 1407 O ATOM 526 OE2 GLU D 6 -56.467 73.271 -26.260 1.00128.26 O ANISOU 526 OE2 GLU D 6 16281 13544 18908 1378 -4498 1571 O ATOM 527 N LYS D 7 -58.155 69.448 -25.258 1.00108.56 N ANISOU 527 N LYS D 7 14307 11719 15223 1700 -3652 1453 N ATOM 528 CA LYS D 7 -58.722 69.124 -26.562 1.00100.85 C ANISOU 528 CA LYS D 7 13158 10925 14236 1554 -3245 1579 C ATOM 529 C LYS D 7 -60.244 69.106 -26.514 1.00 96.03 C ANISOU 529 C LYS D 7 12726 10504 13255 1633 -3024 1503 C ATOM 530 O LYS D 7 -60.908 69.646 -27.408 1.00 96.28 O ANISOU 530 O LYS D 7 12682 10600 13301 1553 -2872 1532 O ATOM 531 CB LYS D 7 -58.179 67.778 -27.049 1.00108.24 C ANISOU 531 CB LYS D 7 13966 11950 15210 1482 -3001 1707 C ATOM 532 CG LYS D 7 -56.955 67.877 -27.942 1.00112.29 C ANISOU 532 CG LYS D 7 14179 12369 16119 1376 -2995 1907 C ATOM 533 CD LYS D 7 -57.322 67.584 -29.392 1.00103.71 C ANISOU 533 CD LYS D 7 12968 11437 15001 1333 -2631 2032 C ATOM 534 CE LYS D 7 -56.096 67.561 -30.291 1.00 98.66 C ANISOU 534 CE LYS D 7 12034 10754 14696 1321 -2545 2297 C ATOM 535 NZ LYS D 7 -56.428 67.135 -31.681 1.00 97.12 N ANISOU 535 NZ LYS D 7 11797 10724 14379 1383 -2189 2401 N ATOM 536 N ILE D 8 -60.819 68.482 -25.483 1.00 93.82 N ANISOU 536 N ILE D 8 12664 10322 12662 1804 -2990 1445 N ATOM 537 CA ILE D 8 -62.277 68.432 -25.399 1.00 97.65 C ANISOU 537 CA ILE D 8 13263 10990 12847 1897 -2759 1459 C ATOM 538 C ILE D 8 -62.838 69.831 -25.171 1.00101.02 C ANISOU 538 C ILE D 8 13821 11378 13183 2021 -2917 1351 C ATOM 539 O ILE D 8 -63.881 70.190 -25.731 1.00100.18 O ANISOU 539 O ILE D 8 13691 11384 12989 1990 -2725 1389 O ATOM 540 CB ILE D 8 -62.741 67.435 -24.317 1.00100.28 C ANISOU 540 CB ILE D 8 13752 11450 12900 2091 -2652 1511 C ATOM 541 CG1 ILE D 8 -62.347 67.898 -22.915 1.00103.81 C ANISOU 541 CG1 ILE D 8 14465 11819 13159 2395 -2947 1383 C ATOM 542 CG2 ILE D 8 -62.184 66.047 -24.593 1.00103.73 C ANISOU 542 CG2 ILE D 8 14058 11902 13454 1953 -2527 1610 C ATOM 543 CD1 ILE D 8 -62.857 67.005 -21.800 1.00106.17 C ANISOU 543 CD1 ILE D 8 14929 12274 13137 2664 -2804 1476 C ATOM 544 N ASN D 9 -62.132 70.660 -24.394 1.00 98.98 N ANISOU 544 N ASN D 9 13707 10930 12973 2164 -3312 1211 N ATOM 545 CA ASN D 9 -62.585 72.030 -24.176 1.00100.05 C ANISOU 545 CA ASN D 9 13998 10980 13036 2307 -3539 1081 C ATOM 546 C ASN D 9 -62.553 72.829 -25.473 1.00 92.27 C ANISOU 546 C ASN D 9 12762 9933 12365 2042 -3504 1134 C ATOM 547 O ASN D 9 -63.516 73.530 -25.804 1.00 95.31 O ANISOU 547 O ASN D 9 13192 10398 12624 2072 -3403 1111 O ATOM 548 CB ASN D 9 -61.729 72.707 -23.104 1.00 97.39 C ANISOU 548 CB ASN D 9 13889 10378 12737 2526 -4078 901 C ATOM 549 CG ASN D 9 -61.894 72.072 -21.738 1.00110.97 C ANISOU 549 CG ASN D 9 15917 12196 14052 2864 -4081 822 C ATOM 550 OD1 ASN D 9 -62.946 71.520 -21.421 1.00123.46 O ANISOU 550 OD1 ASN D 9 17619 14027 15262 3071 -3763 923 O ATOM 551 ND2 ASN D 9 -60.847 72.144 -20.922 1.00120.74 N ANISOU 551 ND2 ASN D 9 17249 13249 15379 2900 -4392 660 N ATOM 552 N ALA D 10 -61.455 72.728 -26.228 1.00 93.25 N ANISOU 552 N ALA D 10 12608 9926 12896 1808 -3560 1238 N ATOM 553 CA ALA D 10 -61.348 73.475 -27.478 1.00 93.47 C ANISOU 553 CA ALA D 10 12376 9909 13227 1603 -3495 1346 C ATOM 554 C ALA D 10 -62.376 73.004 -28.500 1.00 91.63 C ANISOU 554 C ALA D 10 12073 9922 12822 1512 -3042 1426 C ATOM 555 O ALA D 10 -62.969 73.822 -29.214 1.00 81.96 O ANISOU 555 O ALA D 10 10791 8722 11629 1455 -2972 1434 O ATOM 556 CB ALA D 10 -59.932 73.355 -28.043 1.00 97.49 C ANISOU 556 CB ALA D 10 12579 10262 14202 1438 -3590 1526 C ATOM 557 N ALA D 11 -62.607 71.690 -28.583 1.00 93.14 N ANISOU 557 N ALA D 11 12271 10266 12851 1500 -2772 1482 N ATOM 558 CA ALA D 11 -63.585 71.176 -29.536 1.00 90.33 C ANISOU 558 CA ALA D 11 11868 10082 12372 1424 -2435 1548 C ATOM 559 C ALA D 11 -64.998 71.606 -29.165 1.00 87.63 C ANISOU 559 C ALA D 11 11683 9849 11764 1522 -2360 1492 C ATOM 560 O ALA D 11 -65.778 72.013 -30.037 1.00 86.32 O ANISOU 560 O ALA D 11 11459 9744 11594 1447 -2215 1517 O ATOM 561 CB ALA D 11 -63.488 69.653 -29.618 1.00 68.94 C ANISOU 561 CB ALA D 11 9147 7451 9595 1402 -2258 1618 C ATOM 562 N ARG D 12 -65.347 71.521 -27.877 1.00 77.31 N ANISOU 562 N ARG D 12 10577 8576 10220 1726 -2445 1440 N ATOM 563 CA ARG D 12 -66.652 71.997 -27.433 1.00 90.27 C ANISOU 563 CA ARG D 12 12364 10341 11594 1892 -2353 1438 C ATOM 564 C ARG D 12 -66.818 73.485 -27.715 1.00 90.92 C ANISOU 564 C ARG D 12 12482 10342 11720 1907 -2515 1330 C ATOM 565 O ARG D 12 -67.892 73.925 -28.141 1.00 84.19 O ANISOU 565 O ARG D 12 11626 9591 10770 1906 -2356 1363 O ATOM 566 CB ARG D 12 -66.833 71.694 -25.943 1.00 95.43 C ANISOU 566 CB ARG D 12 13251 11056 11953 2206 -2412 1432 C ATOM 567 CG ARG D 12 -67.769 72.641 -25.205 1.00113.95 C ANISOU 567 CG ARG D 12 15823 13478 13993 2516 -2444 1390 C ATOM 568 CD ARG D 12 -66.990 73.703 -24.438 1.00112.73 C ANISOU 568 CD ARG D 12 15909 13128 13793 2730 -2880 1159 C ATOM 569 NE ARG D 12 -67.821 74.851 -24.097 1.00112.20 N ANISOU 569 NE ARG D 12 16058 13090 13482 2995 -2959 1076 N ATOM 570 CZ ARG D 12 -67.354 76.001 -23.630 1.00108.33 C ANISOU 570 CZ ARG D 12 15792 12390 12977 3179 -3395 853 C ATOM 571 NH1 ARG D 12 -66.060 76.190 -23.428 1.00109.80 N ANISOU 571 NH1 ARG D 12 15987 12304 13428 3104 -3811 714 N ATOM 572 NH2 ARG D 12 -68.205 76.988 -23.368 1.00100.61 N ANISOU 572 NH2 ARG D 12 15026 11457 11745 3441 -3438 778 N END If you find results from this site helpful for your research, please cite one of our papers:
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