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pdb2btm.pdb
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pdb2btm.pdb
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HEADER ISOMERASE 04-JAN-99 2BTM
TITLE DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF
TITLE 2 THERMOPHILIC TIMS TO HIGH TEMPERATURES?
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TIM;
COMPND 5 EC: 5.3.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS THERMOPHILIC TRIOSE-PHOSPHATE, GLYCOLYSIS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.F.DELBONI,S.C.MANDE,W.G.J.HOL
REVDAT 2 29-DEC-99 2BTM 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 13-JAN-99 2BTM 0
JRNL AUTH M.ALVAREZ,J.WOUTERS,D.MAES,V.MAINFROID,
JRNL AUTH 2 F.RENTIER-DELRUE,L.WYNS,E.DEPIEREUX,J.A.MARTIAL
JRNL TITL LYS13 PLAYS A CRUCIAL ROLE IN THE FUNCTIONAL
JRNL TITL 2 ADAPTATION OF THE THERMOPHILIC TRIOSE-PHOSPHATE
JRNL TITL 3 ISOMERASE FROM BACILLUS STEAROTHERMOPHILUS TO HIGH
JRNL TITL 4 TEMPERATURES
JRNL REF J.BIOL.CHEM. V. 274 19181 1999
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.RENTIER-DELRUE,S.C.MANDE,S.MOYENS,P.TERPSTRA,
REMARK 1 AUTH 2 V.MAINFROID,K.GORAJ,M.LION,W.G.HOL,J.A.MARTIAL
REMARK 1 TITL CLONING AND OVEREXPRESSION OF THE TRIOSEPHOSPHATE
REMARK 1 TITL 2 ISOMERASE GENES FROM PSYCHROPHILIC AND
REMARK 1 TITL 3 THERMOPHILIC BACTERIA. STRUCTURAL COMPARISON OF
REMARK 1 TITL 4 THE PREDICTED PROTEIN SEQUENCES
REMARK 1 REF J.MOL.BIOL. V. 229 85 1993
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.4A
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 22732
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 22
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 289
REMARK 3 BIN R VALUE (WORKING SET) : 0.2474
REMARK 3 BIN FREE R VALUE : 0.2923
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3672
REMARK 3 NUCLEIC ACID ATOMS : NULL
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.25
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : PGA.PAR
REMARK 3 TOPOLOGY FILE 1 : WATER.TOP
REMARK 3 TOPOLOGY FILE 2 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 3 : PGA.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE INITIAL STAGES OF
REMARK 3 REFINEMENT WERE CARRIED OUT WITH X-PLOR
REMARK 4
REMARK 4 2BTM COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-1999.
REMARK 100 THE RCSB ID CODE IS RCSB008397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-1998
REMARK 200 TEMPERATURE (KELVIN) : 297.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22732
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.27800
REMARK 200 R SYM FOR SHELL (I) : 0.29200
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1BTM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 1/2-X,1/2+Y,-Z
REMARK 290 4555 1/2+X,1/2-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 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 39.06600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.95650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.06600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.95650
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 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 GLU A 252
REMARK 465 GLU B 252
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 99 CD OE1 NE2
REMARK 470 GLU A 106 CD OE1 OE2
REMARK 470 GLU A 131 CG CD OE1 OE2
REMARK 470 GLU A 134 CG CD OE1 OE2
REMARK 470 GLN A 137 CD OE1 NE2
REMARK 470 GLU A 147 CD OE1 OE2
REMARK 470 GLU A 156 CG CD OE1 OE2
REMARK 470 LYS A 159 CE NZ
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 ARG A 195 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 200 CG CD OE1 OE2
REMARK 470 GLU A 203 CD OE1 OE2
REMARK 470 ARG A 219 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 225 CG CD OE1 NE2
REMARK 470 HIS A 251 CA C O CB CG ND1 CD2
REMARK 470 HIS A 251 CE1 NE2
REMARK 470 GLU B 106 CD OE1 OE2
REMARK 470 GLU B 131 OE1 OE2
REMARK 470 GLU B 156 CG CD OE1 OE2
REMARK 470 GLN B 160 CD OE1 NE2
REMARK 470 GLU B 203 CD OE1 OE2
REMARK 470 ARG B 219 CD NE CZ NH1 NH2
REMARK 470 GLN B 225 CD OE1 NE2
REMARK 470 GLU B 238 CG CD OE1 OE2
REMARK 470 HIS B 251 CA C O CB CG ND1 CD2
REMARK 470 HIS B 251 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 14 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 VAL A 25 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 ILE A 123 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 TYR A 209 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 LEU A 231 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 THR B 14 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ILE B 123 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 TYR B 209 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 LEU B 231 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 72 DISTANCE = 5.13 ANGSTROMS
REMARK 525 0 HOH 97 DISTANCE = 15.42 ANGSTROMS
REMARK 525 0 HOH 98 DISTANCE = 23.45 ANGSTROMS
REMARK 525 0 HOH 99 DISTANCE = 25.07 ANGSTROMS
REMARK 525 0 HOH 100 DISTANCE = 22.45 ANGSTROMS
REMARK 525 0 HOH 101 DISTANCE = 31.32 ANGSTROMS
REMARK 525 0 HOH 102 DISTANCE = 19.29 ANGSTROMS
REMARK 525 0 HOH 103 DISTANCE = 23.15 ANGSTROMS
REMARK 525 0 HOH 104 DISTANCE = 20.88 ANGSTROMS
REMARK 525 0 HOH 105 DISTANCE = 35.61 ANGSTROMS
REMARK 525 0 HOH 106 DISTANCE = 35.40 ANGSTROMS
REMARK 525 0 HOH 107 DISTANCE = 7.40 ANGSTROMS
REMARK 525 0 HOH 108 DISTANCE = 24.23 ANGSTROMS
REMARK 525 0 HOH 109 DISTANCE = 7.71 ANGSTROMS
REMARK 525 0 HOH 110 DISTANCE = 22.89 ANGSTROMS
REMARK 525 0 HOH 111 DISTANCE = 20.99 ANGSTROMS
REMARK 525 0 HOH 112 DISTANCE = 31.50 ANGSTROMS
REMARK 525 0 HOH 113 DISTANCE = 8.98 ANGSTROMS
REMARK 525 0 HOH 114 DISTANCE = 18.86 ANGSTROMS
REMARK 525 0 HOH 115 DISTANCE = 44.00 ANGSTROMS
REMARK 525 0 HOH 117 DISTANCE = 33.62 ANGSTROMS
REMARK 525 0 HOH 118 DISTANCE = 11.46 ANGSTROMS
REMARK 525 0 HOH 119 DISTANCE = 22.40 ANGSTROMS
DBREF 2BTM A 1 251 SWS P00943 TPIS_BACST 2 252
DBREF 2BTM B 1 251 SWS P00943 TPIS_BACST 2 252
SEQADV 2BTM ASN A 12 SWS P00943 HIS 13 ENGINEERED
SEQADV 2BTM ASN B 12 SWS P00943 HIS 13 ENGINEERED
SEQADV 2BTM GLY A 13 SWS P00943 LYS 14 ENGINEERED
SEQADV 2BTM GLY B 13 SWS P00943 LYS 14 ENGINEERED
SEQADV 2BTM ALA A 230 SWS P00943 PRO 231 ENGINEERED
SEQADV 2BTM ALA B 230 SWS P00943 PRO 231 ENGINEERED
SEQRES 1 A 252 ARG LYS PRO ILE ILE ALA GLY ASN TRP LYS MET ASN GLY
SEQRES 2 A 252 THR LEU ALA GLU ALA VAL GLN PHE VAL GLU ASP VAL LYS
SEQRES 3 A 252 GLY HIS VAL PRO PRO ALA ASP GLU VAL ILE SER VAL VAL
SEQRES 4 A 252 CYS ALA PRO PHE LEU PHE LEU ASP ARG LEU VAL GLN ALA
SEQRES 5 A 252 ALA ASP GLY THR ASP LEU LYS ILE GLY ALA GLN THR MET
SEQRES 6 A 252 HIS PHE ALA ASP GLN GLY ALA TYR THR GLY GLU VAL SER
SEQRES 7 A 252 PRO VAL MET LEU LYS ASP LEU GLY VAL THR TYR VAL ILE
SEQRES 8 A 252 LEU GLY HIS SER GLU ARG ARG GLN MET PHE ALA GLU THR
SEQRES 9 A 252 ASP GLU THR VAL ASN LYS LYS VAL LEU ALA ALA PHE THR
SEQRES 10 A 252 ARG GLY LEU ILE PRO ILE ILE CYS CYS GLY GLU SER LEU
SEQRES 11 A 252 GLU GLU ARG GLU ALA GLY GLN THR ASN ALA VAL VAL ALA
SEQRES 12 A 252 SER GLN VAL GLU LYS ALA LEU ALA GLY LEU THR PRO GLU
SEQRES 13 A 252 GLN VAL LYS GLN ALA VAL ILE ALA TYR GLU PRO ILE TRP
SEQRES 14 A 252 ALA ILE GLY THR GLY LYS SER SER THR PRO GLU ASP ALA
SEQRES 15 A 252 ASN SER VAL CYS GLY HIS ILE ARG SER VAL VAL SER ARG
SEQRES 16 A 252 LEU PHE GLY PRO GLU ALA ALA GLU ALA ILE ARG ILE GLN
SEQRES 17 A 252 TYR GLY GLY SER VAL LYS PRO ASP ASN ILE ARG ASP PHE
SEQRES 18 A 252 LEU ALA GLN GLN GLN ILE ASP GLY ALA LEU VAL GLY GLY
SEQRES 19 A 252 ALA SER LEU GLU PRO ALA SER PHE LEU GLN LEU VAL GLU
SEQRES 20 A 252 ALA GLY ARG HIS GLU
SEQRES 1 B 252 ARG LYS PRO ILE ILE ALA GLY ASN TRP LYS MET ASN GLY
SEQRES 2 B 252 THR LEU ALA GLU ALA VAL GLN PHE VAL GLU ASP VAL LYS
SEQRES 3 B 252 GLY HIS VAL PRO PRO ALA ASP GLU VAL ILE SER VAL VAL
SEQRES 4 B 252 CYS ALA PRO PHE LEU PHE LEU ASP ARG LEU VAL GLN ALA
SEQRES 5 B 252 ALA ASP GLY THR ASP LEU LYS ILE GLY ALA GLN THR MET
SEQRES 6 B 252 HIS PHE ALA ASP GLN GLY ALA TYR THR GLY GLU VAL SER
SEQRES 7 B 252 PRO VAL MET LEU LYS ASP LEU GLY VAL THR TYR VAL ILE
SEQRES 8 B 252 LEU GLY HIS SER GLU ARG ARG GLN MET PHE ALA GLU THR
SEQRES 9 B 252 ASP GLU THR VAL ASN LYS LYS VAL LEU ALA ALA PHE THR
SEQRES 10 B 252 ARG GLY LEU ILE PRO ILE ILE CYS CYS GLY GLU SER LEU
SEQRES 11 B 252 GLU GLU ARG GLU ALA GLY GLN THR ASN ALA VAL VAL ALA
SEQRES 12 B 252 SER GLN VAL GLU LYS ALA LEU ALA GLY LEU THR PRO GLU
SEQRES 13 B 252 GLN VAL LYS GLN ALA VAL ILE ALA TYR GLU PRO ILE TRP
SEQRES 14 B 252 ALA ILE GLY THR GLY LYS SER SER THR PRO GLU ASP ALA
SEQRES 15 B 252 ASN SER VAL CYS GLY HIS ILE ARG SER VAL VAL SER ARG
SEQRES 16 B 252 LEU PHE GLY PRO GLU ALA ALA GLU ALA ILE ARG ILE GLN
SEQRES 17 B 252 TYR GLY GLY SER VAL LYS PRO ASP ASN ILE ARG ASP PHE
SEQRES 18 B 252 LEU ALA GLN GLN GLN ILE ASP GLY ALA LEU VAL GLY GLY
SEQRES 19 B 252 ALA SER LEU GLU PRO ALA SER PHE LEU GLN LEU VAL GLU
SEQRES 20 B 252 ALA GLY ARG HIS GLU
HET PGA 301 9
HET PGA 302 9
HETNAM PGA 2-PHOSPHOGLYCOLIC ACID
FORMUL 3 PGA 2(C2 H5 O6 P1)
FORMUL 5 HOH *121(H2 O1)
HELIX 1 1 LEU A 15 VAL A 25 1 11
HELIX 2 2 PHE A 43 ALA A 53 1 11
HELIX 3 3 PRO A 79 LEU A 85 1 7
HELIX 4 4 SER A 95 MET A 100 1 6
HELIX 5 5 ASP A 105 ARG A 118 1 14
HELIX 6 6 LEU A 130 GLU A 134 1 5
HELIX 7 7 THR A 138 LEU A 150 1 13
HELIX 8 8 PRO A 155 GLN A 160 1 6
HELIX 9 9 ILE A 168 ALA A 170 5 3
HELIX 10 10 PRO A 179 PHE A 197 1 19
HELIX 11 11 PRO A 199 ALA A 202 1 4
HELIX 12 12 ILE A 218 LEU A 222 1 5
HELIX 13 13 GLY A 234 SER A 236 5 3
HELIX 14 14 PRO A 239 GLY A 249 1 11
HELIX 15 15 LEU B 15 VAL B 25 1 11
HELIX 16 16 PHE B 43 ALA B 53 5 11
HELIX 17 17 PRO B 79 LEU B 85 1 7
HELIX 18 18 SER B 95 MET B 100 1 6
HELIX 19 19 ASP B 105 THR B 117 1 13
HELIX 20 20 LEU B 130 GLU B 134 1 5
HELIX 21 21 THR B 138 LEU B 150 1 13
HELIX 22 22 PRO B 155 GLN B 160 1 6
HELIX 23 23 ILE B 168 ALA B 170 5 3
HELIX 24 24 PRO B 179 PHE B 197 1 19
HELIX 25 25 PRO B 199 ALA B 204 1 6
HELIX 26 26 ILE B 218 LEU B 222 1 5
HELIX 27 27 GLY B 234 SER B 236 5 3
HELIX 28 28 PRO B 239 GLY B 249 1 11
SHEET 1 A 8 TYR A 89 LEU A 92 0
SHEET 2 A 8 ILE A 121 CYS A 126 1 N ILE A 121 O VAL A 90
SHEET 3 A 8 VAL A 162 GLU A 166 1 N VAL A 162 O ILE A 124
SHEET 4 A 8 ARG A 206 GLY A 210 1 N ARG A 206 O ILE A 163
SHEET 5 A 8 GLY A 229 VAL A 232 1 N GLY A 229 O TYR A 209
SHEET 6 A 8 PRO A 3 ASN A 8 1 N ILE A 4 O ALA A 230
SHEET 7 A 8 VAL A 35 ALA A 41 1 N ILE A 36 O PRO A 3
SHEET 8 A 8 LEU A 58 ALA A 62 1 N LYS A 59 O SER A 37
SHEET 1 B 8 TYR B 89 LEU B 92 0
SHEET 2 B 8 ILE B 121 CYS B 126 1 N ILE B 121 O VAL B 90
SHEET 3 B 8 VAL B 162 TYR B 165 1 N VAL B 162 O ILE B 124
SHEET 4 B 8 ARG B 206 GLY B 210 1 N ARG B 206 O ILE B 163
SHEET 5 B 8 GLY B 229 VAL B 232 1 N GLY B 229 O TYR B 209
SHEET 6 B 8 PRO B 3 ASN B 8 1 N ILE B 4 O ALA B 230
SHEET 7 B 8 VAL B 35 ALA B 41 1 N ILE B 36 O PRO B 3
SHEET 8 B 8 LYS B 59 ALA B 62 1 N LYS B 59 O VAL B 39
CRYST1 78.132 107.913 70.980 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012799 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009267 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014088 0.00000
ATOM 1 N ARG A 1 -19.349 2.756 72.289 1.00 38.75 N
ATOM 2 CA ARG A 1 -19.260 3.637 71.085 1.00 37.22 C
ATOM 3 C ARG A 1 -18.212 3.113 70.111 1.00 35.65 C
ATOM 4 O ARG A 1 -17.031 3.034 70.444 1.00 34.72 O
ATOM 5 CB ARG A 1 -18.896 5.066 71.505 1.00 36.99 C
ATOM 6 CG ARG A 1 -20.078 6.018 71.654 1.00 38.29 C
ATOM 7 CD ARG A 1 -19.639 7.312 72.315 1.00 37.71 C
ATOM 8 NE ARG A 1 -19.462 7.129 73.752 1.00 43.76 N
ATOM 9 CZ ARG A 1 -18.623 7.833 74.505 1.00 45.02 C
ATOM 10 NH1 ARG A 1 -17.864 8.772 73.963 1.00 47.56 N
ATOM 11 NH2 ARG A 1 -18.545 7.600 75.805 1.00 48.69 N
ATOM 12 N LYS A 2 -18.635 2.748 68.906 1.00 34.80 N
ATOM 13 CA LYS A 2 -17.677 2.245 67.933 1.00 34.47 C
ATOM 14 C LYS A 2 -16.864 3.406 67.388 1.00 33.91 C
ATOM 15 O LYS A 2 -17.415 4.424 66.986 1.00 34.43 O
ATOM 16 CB LYS A 2 -18.380 1.521 66.783 1.00 34.73 C
ATOM 17 CG LYS A 2 -17.405 0.983 65.741 1.00 37.84 C
ATOM 18 CD LYS A 2 -18.059 0.030 64.751 1.00 38.53 C
ATOM 19 CE LYS A 2 -19.133 0.710 63.934 1.00 38.66 C
ATOM 20 NZ LYS A 2 -19.666 -0.193 62.877 1.00 39.99 N
ATOM 21 N PRO A 3 -15.531 3.275 67.383 1.00 33.16 N
ATOM 22 CA PRO A 3 -14.701 4.365 66.866 1.00 31.41 C
ATOM 23 C PRO A 3 -14.880 4.560 65.358 1.00 31.27 C
ATOM 24 O PRO A 3 -15.264 3.634 64.632 1.00 29.16 O
ATOM 25 CB PRO A 3 -13.288 3.930 67.247 1.00 29.50 C
ATOM 26 CG PRO A 3 -13.377 2.438 67.184 1.00 31.44 C
ATOM 27 CD PRO A 3 -14.698 2.157 67.860 1.00 31.81 C
ATOM 28 N ILE A 4 -14.616 5.778 64.900 1.00 29.02 N
ATOM 29 CA ILE A 4 -14.743 6.104 63.492 1.00 26.17 C
ATOM 30 C ILE A 4 -13.631 7.042 63.057 1.00 25.84 C
ATOM 31 O ILE A 4 -13.442 8.124 63.620 1.00 23.05 O
ATOM 32 CB ILE A 4 -16.121 6.747 63.175 1.00 24.43 C
ATOM 33 CG1 ILE A 4 -16.103 7.333 61.758 1.00 24.23 C
ATOM 34 CG2 ILE A 4 -16.467 7.797 64.218 1.00 23.33 C
ATOM 35 CD1 ILE A 4 -17.457 7.742 61.226 1.00 20.93 C
ATOM 36 N ILE A 5 -12.881 6.598 62.058 1.00 25.18 N
ATOM 37 CA ILE A 5 -11.783 7.377 61.521 1.00 25.51 C
ATOM 38 C ILE A 5 -12.128 7.741 60.086 1.00 23.92 C
ATOM 39 O ILE A 5 -12.292 6.869 59.226 1.00 22.98 O
ATOM 40 CB ILE A 5 -10.450 6.586 61.547 1.00 24.88 C
ATOM 41 CG1 ILE A 5 -9.926 6.475 62.980 1.00 28.99 C
ATOM 42 CG2 ILE A 5 -9.406 7.294 60.701 1.00 25.91 C
ATOM 43 CD1 ILE A 5 -10.664 5.486 63.845 1.00 30.90 C
ATOM 44 N ALA A 6 -12.241 9.035 59.831 1.00 21.21 N
ATOM 45 CA ALA A 6 -12.578 9.496 58.497 1.00 20.48 C
ATOM 46 C ALA A 6 -11.447 10.309 57.902 1.00 19.95 C
ATOM 47 O ALA A 6 -10.911 11.219 58.534 1.00 21.70 O
ATOM 48 CB ALA A 6 -13.857 10.329 58.537 1.00 20.07 C
ATOM 49 N GLY A 7 -11.078 9.958 56.681 1.00 19.52 N
ATOM 50 CA GLY A 7 -10.027 10.683 56.005 1.00 19.90 C
ATOM 51 C GLY A 7 -10.657 11.712 55.088 1.00 18.57 C
ATOM 52 O GLY A 7 -11.546 11.392 54.298 1.00 19.14 O
ATOM 53 N ASN A 8 -10.216 12.956 55.212 1.00 17.41 N
ATOM 54 CA ASN A 8 -10.720 14.036 54.376 1.00 17.38 C
ATOM 55 C ASN A 8 -9.598 14.452 53.425 1.00 16.22 C
ATOM 56 O ASN A 8 -8.709 15.229 53.778 1.00 14.80 O
ATOM 57 CB ASN A 8 -11.170 15.210 55.255 1.00 16.40 C
ATOM 58 CG ASN A 8 -11.548 16.433 54.448 1.00 17.25 C
ATOM 59 OD1 ASN A 8 -11.883 16.330 53.263 1.00 13.45 O
ATOM 60 ND2 ASN A 8 -11.508 17.602 55.088 1.00 15.83 N
ATOM 61 N TRP A 9 -9.636 13.902 52.218 1.00 16.40 N
ATOM 62 CA TRP A 9 -8.614 14.186 51.221 1.00 18.45 C
ATOM 63 C TRP A 9 -8.620 15.631 50.756 1.00 17.94 C
ATOM 64 O TRP A 9 -7.653 16.094 50.145 1.00 18.36 O
ATOM 65 CB TRP A 9 -8.806 13.297 49.993 1.00 19.50 C
ATOM 66 CG TRP A 9 -8.509 11.859 50.205 1.00 20.77 C
ATOM 67 CD1 TRP A 9 -7.899 11.293 51.285 1.00 22.64 C
ATOM 68 CD2 TRP A 9 -8.754 10.798 49.278 1.00 20.87 C
ATOM 69 NE1 TRP A 9 -7.746 9.941 51.088 1.00 22.59 N
ATOM 70 CE2 TRP A 9 -8.263 9.611 49.863 1.00 23.03 C
ATOM 71 CE3 TRP A 9 -9.341 10.735 48.009 1.00 21.07 C
ATOM 72 CZ2 TRP A 9 -8.338 8.373 49.220 1.00 21.48 C
ATOM 73 CZ3 TRP A 9 -9.415 9.505 47.368 1.00 22.84 C
ATOM 74 CH2 TRP A 9 -8.917 8.341 47.978 1.00 23.76 C
ATOM 75 N LYS A 10 -9.714 16.330 51.040 1.00 17.16 N
ATOM 76 CA LYS A 10 -9.886 17.709 50.613 1.00 15.50 C
ATOM 77 C LYS A 10 -9.702 17.746 49.101 1.00 15.79 C
ATOM 78 O LYS A 10 -10.027 16.777 48.415 1.00 16.35 O
ATOM 79 CB LYS A 10 -8.887 18.627 51.315 1.00 17.93 C
ATOM 80 CG LYS A 10 -9.014 18.561 52.821 1.00 20.00 C
ATOM 81 CD LYS A 10 -8.245 19.647 53.530 1.00 22.16 C
ATOM 82 CE LYS A 10 -8.423 19.498 55.033 1.00 24.56 C
ATOM 83 NZ LYS A 10 -7.730 20.558 55.803 1.00 25.54 N
ATOM 84 N MET A 11 -9.176 18.844 48.574 1.00 16.57 N
ATOM 85 CA MET A 11 -9.004 18.952 47.132 1.00 16.68 C
ATOM 86 C MET A 11 -7.659 18.407 46.684 1.00 17.60 C
ATOM 87 O MET A 11 -6.769 19.166 46.295 1.00 16.01 O
ATOM 88 CB MET A 11 -9.153 20.407 46.699 1.00 17.76 C
ATOM 89 CG MET A 11 -9.168 20.595 45.197 1.00 16.51 C
ATOM 90 SD MET A 11 -9.692 22.251 44.779 1.00 18.38 S
ATOM 91 CE MET A 11 -8.119 23.157 44.946 1.00 11.43 C
ATOM 92 N ASN A 12 -7.526 17.083 46.735 1.00 16.79 N
ATOM 93 CA ASN A 12 -6.286 16.425 46.358 1.00 17.58 C
ATOM 94 C ASN A 12 -6.508 15.187 45.523 1.00 19.28 C
ATOM 95 O ASN A 12 -7.575 14.569 45.567 1.00 21.00 O
ATOM 96 CB ASN A 12 -5.496 16.024 47.607 1.00 16.09 C
ATOM 97 CG ASN A 12 -4.888 17.214 48.322 1.00 18.56 C
ATOM 98 OD1 ASN A 12 -3.979 17.853 47.808 1.00 22.18 O
ATOM 99 ND2 ASN A 12 -5.390 17.514 49.514 1.00 18.09 N
ATOM 100 N GLY A 13 -5.479 14.832 44.764 1.00 21.32 N
ATOM 101 CA GLY A 13 -5.521 13.640 43.942 1.00 22.71 C
ATOM 102 C GLY A 13 -6.109 13.754 42.553 1.00 24.14 C
ATOM 103 O GLY A 13 -6.688 14.769 42.168 1.00 24.18 O
ATOM 104 N THR A 14 -5.923 12.679 41.799 1.00 24.46 N
ATOM 105 CA THR A 14 -6.437 12.544 40.446 1.00 25.16 C
ATOM 106 C THR A 14 -7.222 11.244 40.515 1.00 22.75 C
ATOM 107 O THR A 14 -7.046 10.470 41.452 1.00 23.36 O
ATOM 108 CB THR A 14 -5.299 12.399 39.420 1.00 25.05 C
ATOM 109 OG1 THR A 14 -4.375 11.394 39.863 1.00 27.17 O
ATOM 110 CG2 THR A 14 -4.573 13.714 39.256 1.00 28.07 C
ATOM 111 N LEU A 15 -8.080 10.999 39.538 1.00 22.31 N
ATOM 112 CA LEU A 15 -8.885 9.788 39.548 1.00 22.39 C
ATOM 113 C LEU A 15 -8.059 8.512 39.718 1.00 22.52 C
ATOM 114 O LEU A 15 -8.357 7.679 40.572 1.00 21.27 O
ATOM 115 CB LEU A 15 -9.716 9.709 38.266 1.00 20.85 C
ATOM 116 CG LEU A 15 -10.652 8.502 38.144 1.00 22.44 C
ATOM 117 CD1 LEU A 15 -11.470 8.336 39.412 1.00 22.97 C
ATOM 118 CD2 LEU A 15 -11.558 8.680 36.949 1.00 22.69 C
ATOM 119 N ALA A 16 -7.016 8.364 38.910 1.00 22.83 N
ATOM 120 CA ALA A 16 -6.170 7.178 38.974 1.00 23.92 C
ATOM 121 C ALA A 16 -5.598 6.928 40.365 1.00 24.69 C
ATOM 122 O ALA A 16 -5.694 5.821 40.893 1.00 27.37 O
ATOM 123 CB ALA A 16 -5.038 7.289 37.956 1.00 20.82 C
ATOM 124 N GLU A 17 -4.998 7.951 40.959 1.00 25.70 N
ATOM 125 CA GLU A 17 -4.411 7.806 42.286 1.00 26.35 C
ATOM 126 C GLU A 17 -5.460 7.427 43.315 1.00 22.55 C
ATOM 127 O GLU A 17 -5.218 6.592 44.186 1.00 24.00 O
ATOM 128 CB GLU A 17 -3.743 9.108 42.724 1.00 29.28 C
ATOM 129 CG GLU A 17 -2.696 9.624 41.767 1.00 38.45 C
ATOM 130 CD GLU A 17 -1.990 10.848 42.310 1.00 42.89 C
ATOM 131 OE1 GLU A 17 -1.242 10.711 43.304 1.00 46.22 O
ATOM 132 OE2 GLU A 17 -2.192 11.946 41.752 1.00 46.48 O
ATOM 133 N ALA A 18 -6.621 8.061 43.214 1.00 19.05 N
ATOM 134 CA ALA A 18 -7.721 7.813 44.134 1.00 18.43 C
ATOM 135 C ALA A 18 -8.173 6.355 44.065 1.00 17.33 C
ATOM 136 O ALA A 18 -8.450 5.734 45.088 1.00 16.82 O
ATOM 137 CB ALA A 18 -8.893 8.755 43.809 1.00 18.91 C
ATOM 138 N VAL A 19 -8.247 5.820 42.854 1.00 17.95 N
ATOM 139 CA VAL A 19 -8.658 4.439 42.658 1.00 21.33 C
ATOM 140 C VAL A 19 -7.606 3.486 43.217 1.00 22.45 C
ATOM 141 O VAL A 19 -7.935 2.493 43.871 1.00 22.94 O
ATOM 142 CB VAL A 19 -8.888 4.141 41.151 1.00 21.41 C
ATOM 143 CG1 VAL A 19 -8.903 2.634 40.902 1.00 20.06 C
ATOM 144 CG2 VAL A 19 -10.220 4.751 40.707 1.00 19.05 C
ATOM 145 N GLN A 20 -6.341 3.798 42.962 1.00 22.88 N
ATOM 146 CA GLN A 20 -5.245 2.963 43.433 1.00 23.55 C
ATOM 147 C GLN A 20 -5.269 2.952 44.959 1.00 22.46 C
ATOM 148 O GLN A 20 -5.084 1.907 45.596 1.00 20.35 O
ATOM 149 CB GLN A 20 -3.912 3.510 42.913 1.00 23.68 C
ATOM 150 CG GLN A 20 -2.738 2.555 43.055 1.00 28.64 C
ATOM 151 CD GLN A 20 -3.058 1.168 42.523 1.00 32.81 C
ATOM 152 OE1 GLN A 20 -3.493 0.286 43.268 1.00 35.78 O
ATOM 153 NE2 GLN A 20 -2.866 0.974 41.224 1.00 35.61 N
ATOM 154 N PHE A 21 -5.523 4.125 45.531 1.00 19.15 N
ATOM 155 CA PHE A 21 -5.590 4.287 46.975 1.00 20.17 C
ATOM 156 C PHE A 21 -6.629 3.345 47.585 1.00 21.31 C
ATOM 157 O PHE A 21 -6.352 2.648 48.565 1.00 22.22 O
ATOM 158 CB PHE A 21 -5.942 5.741 47.317 1.00 18.77 C
ATOM 159 CG PHE A 21 -6.020 6.025 48.795 1.00 18.74 C
ATOM 160 CD1 PHE A 21 -6.965 5.390 49.597 1.00 18.51 C
ATOM 161 CD2 PHE A 21 -5.155 6.939 49.383 1.00 19.04 C
ATOM 162 CE1 PHE A 21 -7.046 5.665 50.965 1.00 21.46 C
ATOM 163 CE2 PHE A 21 -5.229 7.220 50.748 1.00 19.16 C
ATOM 164 CZ PHE A 21 -6.175 6.583 51.538 1.00 19.82 C
ATOM 165 N VAL A 22 -7.829 3.335 47.014 1.00 20.57 N
ATOM 166 CA VAL A 22 -8.893 2.481 47.526 1.00 22.01 C
ATOM 167 C VAL A 22 -8.518 1.015 47.359 1.00 22.56 C
ATOM 168 O VAL A 22 -8.663 0.215 48.279 1.00 22.73 O
ATOM 169 CB VAL A 22 -10.228 2.758 46.798 1.00 20.39 C
ATOM 170 CG1 VAL A 22 -11.246 1.676 47.127 1.00 18.89 C
ATOM 171 CG2 VAL A 22 -10.759 4.113 47.215 1.00 21.26 C
ATOM 172 N GLU A 23 -8.031 0.681 46.172 1.00 23.61 N
ATOM 173 CA GLU A 23 -7.624 -0.674 45.852 1.00 24.49 C
ATOM 174 C GLU A 23 -6.544 -1.176 46.815 1.00 25.39 C
ATOM 175 O GLU A 23 -6.575 -2.332 47.240 1.00 27.32 O
ATOM 176 CB GLU A 23 -7.110 -0.714 44.410 1.00 26.74 C
ATOM 177 CG GLU A 23 -7.620 -1.882 43.596 1.00 31.95 C
ATOM 178 CD GLU A 23 -9.134 -1.974 43.588 1.00 34.10 C
ATOM 179 OE1 GLU A 23 -9.793 -1.044 43.081 1.00 36.75 O
ATOM 180 OE2 GLU A 23 -9.665 -2.979 44.094 1.00 35.75 O
ATOM 181 N ASP A 24 -5.599 -0.311 47.175 1.00 23.72 N
ATOM 182 CA ASP A 24 -4.526 -0.714 48.074 1.00 24.06 C
ATOM 183 C ASP A 24 -4.989 -0.890 49.507 1.00 24.61 C
ATOM 184 O ASP A 24 -4.445 -1.707 50.251 1.00 27.81 O
ATOM 185 CB ASP A 24 -3.391 0.316 48.088 1.00 25.30 C
ATOM 186 CG ASP A 24 -2.714 0.466 46.752 1.00 27.95 C
ATOM 187 OD1 ASP A 24 -2.658 -0.522 45.992 1.00 28.99 O
ATOM 188 OD2 ASP A 24 -2.218 1.577 46.470 1.00 33.54 O
ATOM 189 N VAL A 25 -6.005 -0.129 49.884 1.00 23.17 N
ATOM 190 CA VAL A 25 -6.509 -0.131 51.249 1.00 22.97 C
ATOM 191 C VAL A 25 -7.787 -0.903 51.572 1.00 21.62 C
ATOM 192 O VAL A 25 -7.901 -1.488 52.648 1.00 22.32 O
ATOM 193 CB VAL A 25 -6.720 1.339 51.712 1.00 24.84 C
ATOM 194 CG1 VAL A 25 -7.475 1.379 53.020 1.00 26.63 C
ATOM 195 CG2 VAL A 25 -5.373 2.042 51.847 1.00 25.63 C
ATOM 196 N LYS A 26 -8.746 -0.897 50.655 1.00 20.98 N
ATOM 197 CA LYS A 26 -10.039 -1.527 50.909 1.00 21.65 C
ATOM 198 C LYS A 26 -10.046 -2.898 51.575 1.00 20.96 C
ATOM 199 O LYS A 26 -10.862 -3.154 52.460 1.00 21.22 O
ATOM 200 CB LYS A 26 -10.870 -1.577 49.620 1.00 20.17 C
ATOM 201 CG LYS A 26 -10.467 -2.633 48.622 1.00 17.61 C
ATOM 202 CD LYS A 26 -11.300 -2.461 47.364 1.00 20.54 C
ATOM 203 CE LYS A 26 -11.178 -3.641 46.421 1.00 17.91 C
ATOM 204 NZ LYS A 26 -11.955 -3.395 45.182 1.00 19.06 N
ATOM 205 N GLY A 27 -9.138 -3.775 51.170 1.00 21.16 N
ATOM 206 CA GLY A 27 -9.116 -5.100 51.752 1.00 21.24 C
ATOM 207 C GLY A 27 -8.306 -5.256 53.020 1.00 22.09 C
ATOM 208 O GLY A 27 -8.289 -6.339 53.604 1.00 23.68 O
ATOM 209 N HIS A 28 -7.643 -4.195 53.464 1.00 22.45 N
ATOM 210 CA HIS A 28 -6.821 -4.293 54.662 1.00 25.16 C
ATOM 211 C HIS A 28 -7.294 -3.412 55.794 1.00 26.30 C
ATOM 212 O HIS A 28 -6.630 -3.267 56.815 1.00 26.50 O
ATOM 213 CB HIS A 28 -5.365 -3.997 54.312 1.00 23.58 C
ATOM 214 CG HIS A 28 -4.849 -4.856 53.206 1.00 26.37 C
ATOM 215 ND1 HIS A 28 -4.985 -4.517 51.878 1.00 31.22 N
ATOM 216 CD2 HIS A 28 -4.314 -6.100 53.224 1.00 29.05 C
ATOM 217 CE1 HIS A 28 -4.561 -5.515 51.124 1.00 30.68 C
ATOM 218 NE2 HIS A 28 -4.151 -6.489 51.916 1.00 31.85 N
ATOM 219 N VAL A 29 -8.460 -2.825 55.599 1.00 28.37 N
ATOM 220 CA VAL A 29 -9.059 -1.980 56.609 1.00 29.76 C
ATOM 221 C VAL A 29 -9.625 -2.916 57.680 1.00 31.09 C
ATOM 222 O VAL A 29 -10.011 -4.049 57.379 1.00 32.52 O
ATOM 223 CB VAL A 29 -10.171 -1.116 55.965 1.00 30.58 C
ATOM 224 CG1 VAL A 29 -11.315 -0.911 56.925 1.00 31.39 C
ATOM 225 CG2 VAL A 29 -9.585 0.222 55.531 1.00 23.89 C
ATOM 226 N PRO A 30 -9.660 -2.467 58.945 1.00 31.39 N
ATOM 227 CA PRO A 30 -10.185 -3.286 60.042 1.00 31.63 C
ATOM 228 C PRO A 30 -11.638 -3.681 59.789 1.00 32.29 C
ATOM 229 O PRO A 30 -12.304 -3.108 58.927 1.00 31.39 O
ATOM 230 CB PRO A 30 -10.058 -2.364 61.256 1.00 31.55 C
ATOM 231 CG PRO A 30 -8.909 -1.482 60.903 1.00 31.00 C
ATOM 232 CD PRO A 30 -9.163 -1.177 59.451 1.00 31.31 C
ATOM 233 N PRO A 31 -12.144 -4.675 60.534 1.00 32.87 N
ATOM 234 CA PRO A 31 -13.531 -5.124 60.372 1.00 34.20 C
ATOM 235 C PRO A 31 -14.481 -3.977 60.712 1.00 34.53 C
ATOM 236 O PRO A 31 -14.231 -3.222 61.647 1.00 34.29 O
ATOM 237 CB PRO A 31 -13.644 -6.270 61.376 1.00 33.57 C
ATOM 238 CG PRO A 31 -12.249 -6.806 61.439 1.00 34.85 C
ATOM 239 CD PRO A 31 -11.414 -5.548 61.468 1.00 34.26 C
ATOM 240 N ALA A 32 -15.569 -3.856 59.960 1.00 35.63 N
ATOM 241 CA ALA A 32 -16.538 -2.790 60.186 1.00 36.76 C
ATOM 242 C ALA A 32 -17.150 -2.792 61.586 1.00 38.81 C
ATOM 243 O ALA A 32 -17.439 -1.730 62.138 1.00 39.84 O
ATOM 244 CB ALA A 32 -17.640 -2.859 59.137 1.00 34.18 C
ATOM 245 N ASP A 33 -17.359 -3.970 62.166 1.00 41.37 N
ATOM 246 CA ASP A 33 -17.949 -4.028 63.502 1.00 42.89 C
ATOM 247 C ASP A 33 -16.977 -3.515 64.556 1.00 41.25 C
ATOM 248 O ASP A 33 -17.365 -3.220 65.683 1.00 42.54 O
ATOM 249 CB ASP A 33 -18.403 -5.455 63.834 1.00 45.64 C
ATOM 250 CG ASP A 33 -17.354 -6.492 63.508 1.00 50.83 C
ATOM 251 OD1 ASP A 33 -16.246 -6.412 64.077 1.00 52.60 O
ATOM 252 OD2 ASP A 33 -17.640 -7.388 62.681 1.00 52.77 O
ATOM 253 N GLU A 34 -15.711 -3.395 64.182 1.00 40.12 N
ATOM 254 CA GLU A 34 -14.697 -2.899 65.097 1.00 38.64 C
ATOM 255 C GLU A 34 -14.463 -1.403 64.927 1.00 38.83 C
ATOM 256 O GLU A 34 -14.472 -0.651 65.903 1.00 38.87 O
ATOM 257 CB GLU A 34 -13.381 -3.631 64.874 1.00 38.42 C
ATOM 258 CG GLU A 34 -13.236 -4.903 65.663 1.00 41.21 C
ATOM 259 CD GLU A 34 -11.884 -5.539 65.452 1.00 41.98 C
ATOM 260 OE1 GLU A 34 -10.870 -4.822 65.589 1.00 43.05 O
ATOM 261 OE2 GLU A 34 -11.837 -6.750 65.149 1.00 44.04 O
ATOM 262 N VAL A 35 -14.250 -0.981 63.683 1.00 37.23 N
ATOM 263 CA VAL A 35 -13.994 0.423 63.375 1.00 36.23 C
ATOM 264 C VAL A 35 -14.634 0.853 62.063 1.00 35.11 C
ATOM 265 O VAL A 35 -14.652 0.105 61.087 1.00 35.75 O
ATOM 266 CB VAL A 35 -12.477 0.712 63.250 1.00 35.79 C
ATOM 267 CG1 VAL A 35 -12.250 2.191 62.962 1.00 32.71 C
ATOM 268 CG2 VAL A 35 -11.756 0.298 64.515 1.00 38.79 C
ATOM 269 N ILE A 36 -15.159 2.067 62.044 1.00 31.96 N
ATOM 270 CA ILE A 36 -15.753 2.591 60.832 1.00 29.22 C
ATOM 271 C ILE A 36 -14.656 3.360 60.109 1.00 28.40 C
ATOM 272 O ILE A 36 -14.163 4.381 60.603 1.00 27.54 O
ATOM 273 CB ILE A 36 -16.931 3.523 61.145 1.00 31.03 C
ATOM 274 CG1 ILE A 36 -18.154 2.695 61.539 1.00 26.60 C
ATOM 275 CG2 ILE A 36 -17.242 4.384 59.940 1.00 35.76 C
ATOM 276 CD1 ILE A 36 -19.289 3.515 62.035 1.00 26.87 C
ATOM 277 N SER A 37 -14.258 2.842 58.949 1.00 25.62 N
ATOM 278 CA SER A 37 -13.214 3.458 58.144 1.00 23.24 C
ATOM 279 C SER A 37 -13.857 4.211 56.996 1.00 21.44 C
ATOM 280 O SER A 37 -14.521 3.619 56.143 1.00 19.36 O
ATOM 281 CB SER A 37 -12.268 2.389 57.608 1.00 24.48 C
ATOM 282 OG SER A 37 -11.746 1.617 58.672 1.00 25.64 O
ATOM 283 N VAL A 38 -13.648 5.521 56.971 1.00 21.11 N
ATOM 284 CA VAL A 38 -14.248 6.348 55.943 1.00 20.16 C
ATOM 285 C VAL A 38 -13.261 7.193 55.164 1.00 20.57 C
ATOM 286 O VAL A 38 -12.309 7.741 55.724 1.00 21.26 O
ATOM 287 CB VAL A 38 -15.299 7.293 56.556 1.00 21.74 C
ATOM 288 CG1 VAL A 38 -16.010 8.073 55.453 1.00 19.16 C
ATOM 289 CG2 VAL A 38 -16.291 6.490 57.395 1.00 19.51 C
ATOM 290 N VAL A 39 -13.511 7.293 53.862 1.00 19.83 N
ATOM 291 CA VAL A 39 -12.696 8.096 52.966 1.00 19.82 C
ATOM 292 C VAL A 39 -13.597 9.100 52.258 1.00 17.71 C
ATOM 293 O VAL A 39 -14.501 8.720 51.519 1.00 18.82 O
ATOM 294 CB VAL A 39 -11.987 7.229 51.900 1.00 22.66 C
ATOM 295 CG1 VAL A 39 -11.490 8.107 50.764 1.00 24.94 C
ATOM 296 CG2 VAL A 39 -10.809 6.504 52.527 1.00 24.65 C
ATOM 297 N CYS A 40 -13.349 10.381 52.498 1.00 16.17 N
ATOM 298 CA CYS A 40 -14.123 11.441 51.873 1.00 16.60 C
ATOM 299 C CYS A 40 -13.276 12.042 50.757 1.00 16.32 C
ATOM 300 O CYS A 40 -12.316 12.771 51.002 1.00 15.35 O
ATOM 301 CB CYS A 40 -14.492 12.490 52.915 1.00 17.95 C
ATOM 302 SG CYS A 40 -15.330 11.749 54.334 1.00 19.69 S
ATOM 303 N ALA A 41 -13.642 11.713 49.524 1.00 17.48 N
ATOM 304 CA ALA A 41 -12.907 12.167 48.354 1.00 16.66 C
ATOM 305 C ALA A 41 -13.638 13.224 47.542 1.00 16.43 C
ATOM 306 O ALA A 41 -14.827 13.462 47.738 1.00 18.00 O
ATOM 307 CB ALA A 41 -12.599 10.966 47.467 1.00 13.52 C
ATOM 308 N PRO A 42 -12.920 13.888 46.624 1.00 17.15 N
ATOM 309 CA PRO A 42 -13.512 14.920 45.770 1.00 18.23 C
ATOM 310 C PRO A 42 -14.688 14.320 44.996 1.00 18.87 C
ATOM 311 O PRO A 42 -14.671 13.135 44.648 1.00 19.12 O
ATOM 312 CB PRO A 42 -12.357 15.302 44.845 1.00 17.37 C
ATOM 313 CG PRO A 42 -11.163 15.148 45.741 1.00 17.75 C
ATOM 314 CD PRO A 42 -11.456 13.832 46.441 1.00 16.82 C
ATOM 315 N PHE A 43 -15.699 15.137 44.723 1.00 17.22 N
ATOM 316 CA PHE A 43 -16.880 14.682 44.002 1.00 19.20 C
ATOM 317 C PHE A 43 -16.559 13.876 42.749 1.00 19.13 C
ATOM 318 O PHE A 43 -17.186 12.854 42.482 1.00 18.46 O
ATOM 319 CB PHE A 43 -17.751 15.873 43.600 1.00 20.68 C
ATOM 320 CG PHE A 43 -18.395 16.575 44.751 1.00 19.37 C
ATOM 321 CD1 PHE A 43 -19.191 15.879 45.647 1.00 21.38 C
ATOM 322 CD2 PHE A 43 -18.242 17.946 44.913 1.00 20.76 C
ATOM 323 CE1 PHE A 43 -19.835 16.538 46.689 1.00 22.29 C
ATOM 324 CE2 PHE A 43 -18.880 18.615 45.949 1.00 22.32 C
ATOM 325 CZ PHE A 43 -19.679 17.909 46.839 1.00 21.37 C
ATOM 326 N LEU A 44 -15.591 14.359 41.980 1.00 19.42 N
ATOM 327 CA LEU A 44 -15.183 13.717 40.739 1.00 20.24 C
ATOM 328 C LEU A 44 -14.858 12.233 40.846 1.00 20.66 C
ATOM 329 O LEU A 44 -15.139 11.469 39.923 1.00 21.48 O
ATOM 330 CB LEU A 44 -13.966 14.444 40.161 1.00 22.37 C
ATOM 331 CG LEU A 44 -14.157 15.506 39.074 1.00 26.24 C
ATOM 332 CD1 LEU A 44 -15.362 16.379 39.372 1.00 27.93 C
ATOM 333 CD2 LEU A 44 -12.882 16.343 38.976 1.00 24.96 C
ATOM 334 N PHE A 45 -14.281 11.817 41.969 1.00 20.02 N
ATOM 335 CA PHE A 45 -13.874 10.417 42.130 1.00 19.73 C
ATOM 336 C PHE A 45 -14.862 9.455 42.780 1.00 19.04 C
ATOM 337 O PHE A 45 -14.689 8.241 42.687 1.00 19.63 O
ATOM 338 CB PHE A 45 -12.569 10.343 42.926 1.00 17.23 C
ATOM 339 CG PHE A 45 -11.562 11.391 42.554 1.00 18.38 C
ATOM 340 CD1 PHE A 45 -11.442 11.831 41.241 1.00 18.89 C
ATOM 341 CD2 PHE A 45 -10.705 11.912 43.516 1.00 17.30 C
ATOM 342 CE1 PHE A 45 -10.480 12.774 40.890 1.00 21.13 C
ATOM 343 CE2 PHE A 45 -9.736 12.855 43.174 1.00 20.58 C
ATOM 344 CZ PHE A 45 -9.625 13.287 41.862 1.00 17.97 C
ATOM 345 N LEU A 46 -15.885 9.987 43.437 1.00 18.07 N
ATOM 346 CA LEU A 46 -16.846 9.156 44.147 1.00 19.99 C
ATOM 347 C LEU A 46 -17.369 7.936 43.401 1.00 21.28 C
ATOM 348 O LEU A 46 -17.313 6.818 43.913 1.00 20.81 O
ATOM 349 CB LEU A 46 -18.002 10.024 44.650 1.00 19.65 C
ATOM 350 CG LEU A 46 -17.527 11.104 45.637 1.00 21.02 C
ATOM 351 CD1 LEU A 46 -18.695 11.961 46.105 1.00 19.91 C
ATOM 352 CD2 LEU A 46 -16.843 10.439 46.829 1.00 19.84 C
ATOM 353 N ASP A 47 -17.868 8.147 42.192 1.00 24.15 N
ATOM 354 CA ASP A 47 -18.404 7.058 41.386 1.00 24.40 C
ATOM 355 C ASP A 47 -17.506 5.812 41.363 1.00 24.98 C
ATOM 356 O ASP A 47 -17.910 4.734 41.814 1.00 25.48 O
ATOM 357 CB ASP A 47 -18.648 7.557 39.962 1.00 26.18 C
ATOM 358 CG ASP A 47 -19.300 6.514 39.086 1.00 26.96 C
ATOM 359 OD1 ASP A 47 -19.927 5.585 39.634 1.00 27.30 O
ATOM 360 OD2 ASP A 47 -19.200 6.635 37.850 1.00 29.05 O
ATOM 361 N ARG A 48 -16.291 5.959 40.846 1.00 23.41 N
ATOM 362 CA ARG A 48 -15.364 4.837 40.764 1.00 22.24 C
ATOM 363 C ARG A 48 -14.975 4.287 42.118 1.00 21.78 C
ATOM 364 O ARG A 48 -14.768 3.083 42.271 1.00 25.06 O
ATOM 365 CB ARG A 48 -14.101 5.233 40.010 1.00 22.27 C
ATOM 366 CG ARG A 48 -14.372 5.621 38.586 1.00 27.56 C
ATOM 367 CD ARG A 48 -13.211 5.268 37.689 1.00 28.13 C
ATOM 368 NE ARG A 48 -13.370 5.856 36.364 1.00 27.94 N
ATOM 369 CZ ARG A 48 -12.555 5.625 35.342 1.00 31.41 C
ATOM 370 NH1 ARG A 48 -11.518 4.807 35.486 1.00 30.64 N
ATOM 371 NH2 ARG A 48 -12.762 6.231 34.182 1.00 31.35 N
ATOM 372 N LEU A 49 -14.870 5.168 43.102 1.00 19.39 N
ATOM 373 CA LEU A 49 -14.505 4.743 44.440 1.00 18.85 C
ATOM 374 C LEU A 49 -15.580 3.868 45.046 1.00 17.77 C
ATOM 375 O LEU A 49 -15.283 2.834 45.641 1.00 20.48 O
ATOM 376 CB LEU A 49 -14.240 5.964 45.330 1.00 18.53 C
ATOM 377 CG LEU A 49 -12.777 6.427 45.403 1.00 20.22 C
ATOM 378 CD1 LEU A 49 -12.072 6.238 44.065 1.00 14.94 C
ATOM 379 CD2 LEU A 49 -12.739 7.879 45.842 1.00 18.38 C
ATOM 380 N VAL A 50 -16.832 4.280 44.899 1.00 18.51 N
ATOM 381 CA VAL A 50 -17.935 3.505 45.443 1.00 19.63 C
ATOM 382 C VAL A 50 -17.937 2.108 44.834 1.00 19.91 C
ATOM 383 O VAL A 50 -18.083 1.118 45.548 1.00 19.68 O
ATOM 384 CB VAL A 50 -19.302 4.189 45.176 1.00 20.76 C
ATOM 385 CG1 VAL A 50 -20.442 3.221 45.479 1.00 17.61 C
ATOM 386 CG2 VAL A 50 -19.428 5.437 46.036 1.00 15.89 C
ATOM 387 N GLN A 51 -17.762 2.036 43.517 1.00 21.46 N
ATOM 388 CA GLN A 51 -17.739 0.757 42.815 1.00 23.66 C
ATOM 389 C GLN A 51 -16.579 -0.109 43.293 1.00 22.47 C
ATOM 390 O GLN A 51 -16.741 -1.307 43.518 1.00 25.49 O
ATOM 391 CB GLN A 51 -17.603 0.966 41.306 1.00 24.74 C
ATOM 392 CG GLN A 51 -18.671 1.840 40.691 1.00 33.26 C
ATOM 393 CD GLN A 51 -18.495 1.990 39.191 1.00 39.55 C
ATOM 394 OE1 GLN A 51 -18.655 3.084 38.640 1.00 42.81 O
ATOM 395 NE2 GLN A 51 -18.169 0.885 38.518 1.00 41.57 N
ATOM 396 N ALA A 52 -15.411 0.503 43.445 1.00 20.31 N
ATOM 397 CA ALA A 52 -14.226 -0.218 43.880 1.00 20.31 C
ATOM 398 C ALA A 52 -14.310 -0.680 45.327 1.00 21.92 C
ATOM 399 O ALA A 52 -13.863 -1.778 45.656 1.00 23.69 O
ATOM 400 CB ALA A 52 -12.995 0.647 43.688 1.00 19.58 C
ATOM 401 N ALA A 53 -14.894 0.146 46.189 1.00 21.20 N
ATOM 402 CA ALA A 53 -14.999 -0.198 47.605 1.00 21.83 C
ATOM 403 C ALA A 53 -16.180 -1.102 47.927 1.00 22.14 C
ATOM 404 O ALA A 53 -16.281 -1.639 49.029 1.00 20.09 O
ATOM 405 CB ALA A 53 -15.074 1.075 48.446 1.00 19.00 C
ATOM 406 N ASP A 54 -17.073 -1.281 46.966 1.00 24.04 N
ATOM 407 CA ASP A 54 -18.236 -2.120 47.204 1.00 23.69 C
ATOM 408 C ASP A 54 -17.845 -3.509 47.707 1.00 24.12 C
ATOM 409 O ASP A 54 -16.931 -4.144 47.175 1.00 22.58 O
ATOM 410 CB ASP A 54 -19.060 -2.259 45.929 1.00 23.11 C
ATOM 411 CG ASP A 54 -20.347 -3.015 46.161 1.00 25.48 C
ATOM 412 OD1 ASP A 54 -21.177 -2.524 46.954 1.00 23.87 O
ATOM 413 OD2 ASP A 54 -20.529 -4.097 45.562 1.00 24.35 O
ATOM 414 N GLY A 55 -18.540 -3.971 48.742 1.00 24.23 N
ATOM 415 CA GLY A 55 -18.266 -5.285 49.292 1.00 22.10 C
ATOM 416 C GLY A 55 -17.150 -5.335 50.314 1.00 21.44 C
ATOM 417 O GLY A 55 -16.760 -6.418 50.751 1.00 23.54 O
ATOM 418 N THR A 56 -16.630 -4.174 50.698 1.00 21.05 N
ATOM 419 CA THR A 56 -15.551 -4.116 51.679 1.00 20.47 C
ATOM 420 C THR A 56 -15.992 -3.256 52.854 1.00 21.57 C
ATOM 421 O THR A 56 -17.094 -2.717 52.849 1.00 21.01 O
ATOM 422 CB THR A 56 -14.280 -3.503 51.071 1.00 20.72 C
ATOM 423 OG1 THR A 56 -14.482 -2.100 50.853 1.00 18.85 O
ATOM 424 CG2 THR A 56 -13.957 -4.170 49.748 1.00 14.84 C
ATOM 425 N ASP A 57 -15.136 -3.124 53.860 1.00 23.28 N
ATOM 426 CA ASP A 57 -15.480 -2.318 55.023 1.00 25.49 C
ATOM 427 C ASP A 57 -15.055 -0.868 54.863 1.00 26.73 C
ATOM 428 O ASP A 57 -15.236 -0.052 55.765 1.00 28.53 O
ATOM 429 CB ASP A 57 -14.841 -2.898 56.281 1.00 27.37 C
ATOM 430 CG ASP A 57 -15.345 -4.288 56.591 1.00 29.90 C
ATOM 431 OD1 ASP A 57 -16.555 -4.524 56.398 1.00 29.42 O
ATOM 432 OD2 ASP A 57 -14.538 -5.135 57.036 1.00 32.02 O
ATOM 433 N LEU A 58 -14.481 -0.543 53.714 1.00 27.49 N
ATOM 434 CA LEU A 58 -14.044 0.821 53.472 1.00 27.14 C
ATOM 435 C LEU A 58 -15.247 1.601 52.965 1.00 26.30 C
ATOM 436 O LEU A 58 -15.777 1.306 51.898 1.00 25.29 O
ATOM 437 CB LEU A 58 -12.909 0.836 52.443 1.00 24.38 C
ATOM 438 CG LEU A 58 -12.146 2.133 52.155 1.00 24.34 C
ATOM 439 CD1 LEU A 58 -12.832 2.903 51.057 1.00 25.51 C
ATOM 440 CD2 LEU A 58 -12.025 2.960 53.429 1.00 22.81 C
ATOM 441 N LYS A 59 -15.698 2.572 53.752 1.00 24.91 N
ATOM 442 CA LYS A 59 -16.834 3.377 53.347 1.00 25.57 C
ATOM 443 C LYS A 59 -16.378 4.663 52.664 1.00 24.54 C
ATOM 444 O LYS A 59 -15.318 5.211 52.971 1.00 24.58 O
ATOM 445 CB LYS A 59 -17.742 3.673 54.547 1.00 27.94 C
ATOM 446 CG LYS A 59 -18.869 2.638 54.721 1.00 32.46 C
ATOM 447 CD LYS A 59 -18.517 1.499 55.671 1.00 34.48 C
ATOM 448 CE LYS A 59 -18.698 1.932 57.141 1.00 42.74 C
ATOM 449 NZ LYS A 59 -18.441 0.847 58.156 1.00 38.64 N
ATOM 450 N ILE A 60 -17.186 5.128 51.720 1.00 23.42 N
ATOM 451 CA ILE A 60 -16.880 6.321 50.953 1.00 22.31 C
ATOM 452 C ILE A 60 -17.766 7.505 51.323 1.00 22.89 C
ATOM 453 O ILE A 60 -18.990 7.377 51.382 1.00 22.94 O
ATOM 454 CB ILE A 60 -17.054 6.050 49.447 1.00 20.73 C
ATOM 455 CG1 ILE A 60 -16.210 4.842 49.028 1.00 20.15 C
ATOM 456 CG2 ILE A 60 -16.680 7.285 48.654 1.00 22.78 C
ATOM 457 CD1 ILE A 60 -14.733 4.953 49.380 1.00 18.29 C
ATOM 458 N GLY A 61 -17.142 8.658 51.558 1.00 20.43 N
ATOM 459 CA GLY A 61 -17.895 9.852 51.895 1.00 18.21 C
ATOM 460 C GLY A 61 -17.625 11.024 50.960 1.00 18.22 C
ATOM 461 O GLY A 61 -16.669 11.020 50.181 1.00 17.17 O
ATOM 462 N ALA A 62 -18.487 12.028 51.025 1.00 17.80 N
ATOM 463 CA ALA A 62 -18.330 13.224 50.214 1.00 18.61 C
ATOM 464 C ALA A 62 -17.807 14.300 51.162 1.00 20.70 C
ATOM 465 O ALA A 62 -17.945 14.179 52.388 1.00 20.99 O
ATOM 466 CB ALA A 62 -19.666 13.642 49.620 1.00 16.83 C
ATOM 467 N GLN A 63 -17.217 15.349 50.601 1.00 19.81 N
ATOM 468 CA GLN A 63 -16.659 16.422 51.411 1.00 19.82 C
ATOM 469 C GLN A 63 -17.651 17.535 51.714 1.00 21.63 C
ATOM 470 O GLN A 63 -17.387 18.402 52.550 1.00 20.45 O
ATOM 471 CB GLN A 63 -15.405 16.969 50.732 1.00 21.09 C
ATOM 472 CG GLN A 63 -14.225 15.999 50.834 1.00 20.47 C
ATOM 473 CD GLN A 63 -13.014 16.434 50.034 1.00 19.79 C
ATOM 474 OE1 GLN A 63 -12.859 17.612 49.711 1.00 19.64 O
ATOM 475 NE2 GLN A 63 -12.136 15.481 49.725 1.00 19.68 N
ATOM 476 N THR A 64 -18.798 17.493 51.040 1.00 20.16 N
ATOM 477 CA THR A 64 -19.859 18.470 51.257 1.00 18.22 C
ATOM 478 C THR A 64 -21.025 18.150 50.330 1.00 19.76 C
ATOM 479 O THR A 64 -20.970 17.199 49.549 1.00 19.16 O
ATOM 480 CB THR A 64 -19.378 19.926 50.979 1.00 16.35 C
ATOM 481 OG1 THR A 64 -20.377 20.855 51.423 1.00 11.96 O
ATOM 482 CG2 THR A 64 -19.132 20.140 49.490 1.00 11.42 C
ATOM 483 N MET A 65 -22.081 18.945 50.433 1.00 16.95 N
ATOM 484 CA MET A 65 -23.254 18.779 49.591 1.00 20.11 C
ATOM 485 C MET A 65 -24.141 19.976 49.840 1.00 18.43 C
ATOM 486 O MET A 65 -23.914 20.737 50.774 1.00 18.11 O
ATOM 487 CB MET A 65 -24.034 17.512 49.952 1.00 20.51 C
ATOM 488 CG MET A 65 -24.575 17.522 51.368 1.00 24.97 C
ATOM 489 SD MET A 65 -25.740 16.199 51.711 1.00 29.59 S
ATOM 490 CE MET A 65 -24.713 14.851 51.554 1.00 34.29 C
ATOM 491 N HIS A 66 -25.141 20.145 48.990 1.00 17.70 N
ATOM 492 CA HIS A 66 -26.090 21.223 49.154 1.00 20.77 C
ATOM 493 C HIS A 66 -27.233 20.607 49.966 1.00 22.45 C
ATOM 494 O HIS A 66 -27.227 19.403 50.229 1.00 21.88 O
ATOM 495 CB HIS A 66 -26.578 21.706 47.791 1.00 21.22 C
ATOM 496 CG HIS A 66 -27.353 22.981 47.854 1.00 24.32 C
ATOM 497 ND1 HIS A 66 -28.725 23.013 47.978 1.00 23.03 N
ATOM 498 CD2 HIS A 66 -26.940 24.271 47.871 1.00 20.83 C
ATOM 499 CE1 HIS A 66 -29.124 24.269 48.069 1.00 22.64 C
ATOM 500 NE2 HIS A 66 -28.061 25.051 48.006 1.00 21.77 N
ATOM 501 N PHE A 67 -28.203 21.411 50.378 1.00 24.52 N
ATOM 502 CA PHE A 67 -29.308 20.870 51.164 1.00 26.28 C
ATOM 503 C PHE A 67 -30.537 20.503 50.335 1.00 25.87 C
ATOM 504 O PHE A 67 -31.353 19.687 50.762 1.00 28.83 O
ATOM 505 CB PHE A 67 -29.689 21.851 52.283 1.00 25.88 C
ATOM 506 CG PHE A 67 -29.964 23.245 51.805 1.00 28.10 C
ATOM 507 CD1 PHE A 67 -31.177 23.564 51.197 1.00 28.04 C
ATOM 508 CD2 PHE A 67 -29.007 24.244 51.955 1.00 26.23 C
ATOM 509 CE1 PHE A 67 -31.431 24.861 50.746 1.00 27.26 C
ATOM 510 CE2 PHE A 67 -29.251 25.543 51.507 1.00 27.47 C
ATOM 511 CZ PHE A 67 -30.465 25.851 50.902 1.00 26.78 C
ATOM 512 N ALA A 68 -30.665 21.091 49.150 1.00 25.21 N
ATOM 513 CA ALA A 68 -31.809 20.805 48.287 1.00 24.95 C
ATOM 514 C ALA A 68 -31.585 19.524 47.490 1.00 24.45 C
ATOM 515 O ALA A 68 -30.441 19.144 47.226 1.00 24.28 O
ATOM 516 CB ALA A 68 -32.062 21.977 47.337 1.00 20.46 C
ATOM 517 N ASP A 69 -32.678 18.866 47.109 1.00 23.78 N
ATOM 518 CA ASP A 69 -32.609 17.626 46.342 1.00 25.53 C
ATOM 519 C ASP A 69 -32.205 17.886 44.897 1.00 24.00 C
ATOM 520 O ASP A 69 -31.627 17.023 44.237 1.00 25.39 O
ATOM 521 CB ASP A 69 -33.964 16.910 46.348 1.00 29.70 C
ATOM 522 CG ASP A 69 -34.387 16.472 47.727 1.00 33.86 C
ATOM 523 OD1 ASP A 69 -33.517 16.018 48.499 1.00 38.10 O
ATOM 524 OD2 ASP A 69 -35.595 16.565 48.034 1.00 37.97 O
ATOM 525 N GLN A 70 -32.532 19.078 44.413 1.00 22.68 N
ATOM 526 CA GLN A 70 -32.225 19.485 43.048 1.00 23.73 C
ATOM 527 C GLN A 70 -32.569 20.960 42.937 1.00 19.62 C
ATOM 528 O GLN A 70 -33.161 21.524 43.851 1.00 17.22 O
ATOM 529 CB GLN A 70 -33.080 18.696 42.063 1.00 27.02 C
ATOM 530 CG GLN A 70 -34.560 19.018 42.177 1.00 37.56 C
ATOM 531 CD GLN A 70 -35.427 17.908 41.637 1.00 44.91 C
ATOM 532 OE1 GLN A 70 -35.448 16.801 42.187 1.00 48.66 O
ATOM 533 NE2 GLN A 70 -36.150 18.189 40.552 1.00 47.90 N
ATOM 534 N GLY A 71 -32.202 21.582 41.823 1.00 18.01 N
ATOM 535 CA GLY A 71 -32.515 22.989 41.651 1.00 18.32 C
ATOM 536 C GLY A 71 -31.443 23.830 40.988 1.00 18.41 C
ATOM 537 O GLY A 71 -30.405 23.328 40.554 1.00 20.01 O
ATOM 538 N ALA A 72 -31.708 25.130 40.929 1.00 19.49 N
ATOM 539 CA ALA A 72 -30.812 26.094 40.309 1.00 20.13 C
ATOM 540 C ALA A 72 -29.655 26.477 41.219 1.00 19.79 C
ATOM 541 O ALA A 72 -29.589 27.600 41.714 1.00 20.68 O
ATOM 542 CB ALA A 72 -31.595 27.339 39.908 1.00 20.32 C
ATOM 543 N TYR A 73 -28.747 25.533 41.436 1.00 18.64 N
ATOM 544 CA TYR A 73 -27.581 25.761 42.274 1.00 19.68 C
ATOM 545 C TYR A 73 -26.388 25.262 41.481 1.00 21.63 C
ATOM 546 O TYR A 73 -25.834 24.189 41.756 1.00 22.44 O
ATOM 547 CB TYR A 73 -27.711 24.984 43.583 1.00 19.15 C