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HEADER HYDROLASE 21-AUG-24 9J8I
TITLE MUTANT OF A DEEP SEA BACTERIAL PET HYDROLASE MTCUT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENGINEERED PET HYDROLASE MTCUTM9;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MARINACTINOSPORA THERMOTOLERANS DSM 45154;
SOURCE 3 ORGANISM_TAXID: 1122192;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SHANSHAN,L.WEI,L.LIJUAN,J.YANG
REVDAT 1 03-SEP-25 9J8I 0
JRNL AUTH L.SHANSHAN,L.WEI,L.LIJUAN,J.YANG
JRNL TITL MUTANT OF A DEEP SEA BACTERIAL PET HYDROLASE MTCUT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 60541
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 + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3229
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4388
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3640
REMARK 3 BIN FREE R VALUE SET COUNT : 242
REMARK 3 BIN FREE R VALUE : 0.3930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.76000
REMARK 3 B22 (A**2) : -2.76000
REMARK 3 B33 (A**2) : 5.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.279
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.191
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.005
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8212 ; 0.007 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 7396 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11212 ; 1.805 ; 1.812
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17060 ; 0.618 ; 1.745
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1032 ; 7.217 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 72 ; 9.127 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1204 ;14.217 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1216 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9968 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1968 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4140 ; 4.697 ; 6.124
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4140 ; 4.696 ; 6.124
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5168 ; 6.477 ;11.014
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5169 ; 6.478 ;11.015
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4072 ; 5.148 ; 6.335
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4073 ; 5.148 ; 6.336
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6045 ; 7.106 ;11.556
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8799 ; 8.396 ;57.450
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8795 ; 8.397 ;57.460
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 9J8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-24.
REMARK 100 THE DEPOSITION ID IS D_1300050545.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-24
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 : SSRF
REMARK 200 BEAMLINE : BL10U2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : STFC LARGE PIXEL DETECTOR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63825
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.720
REMARK 200 RESOLUTION RANGE LOW (A) : 32.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 42.40
REMARK 200 R MERGE (I) : 0.32800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 45.20
REMARK 200 R MERGE FOR SHELL (I) : 3.44800
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 800 MM (NH4)2SO4, 100 MM SODIUM
REMARK 280 CITRATE/CITRIC ACID PH4.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 93.97000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 93.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.01000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 93.97000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 93.97000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.01000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 93.97000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 93.97000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 66.01000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 93.97000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.97000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.01000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 HIS A 309
REMARK 465 THR A 310
REMARK 465 THR A 311
REMARK 465 LEU A 312
REMARK 465 GLU A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS B 309
REMARK 465 THR B 310
REMARK 465 THR B 311
REMARK 465 LEU B 312
REMARK 465 GLU B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS C 309
REMARK 465 THR C 310
REMARK 465 THR C 311
REMARK 465 LEU C 312
REMARK 465 GLU C 313
REMARK 465 HIS C 314
REMARK 465 HIS C 315
REMARK 465 HIS C 316
REMARK 465 HIS C 317
REMARK 465 HIS C 318
REMARK 465 HIS C 319
REMARK 465 HIS D 309
REMARK 465 THR D 310
REMARK 465 THR D 311
REMARK 465 LEU D 312
REMARK 465 GLU D 313
REMARK 465 HIS D 314
REMARK 465 HIS D 315
REMARK 465 HIS D 316
REMARK 465 HIS D 317
REMARK 465 HIS D 318
REMARK 465 HIS D 319
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP A 293 OD1 ASP A 293 2555 1.63
REMARK 500 OH TYR D 110 OH TYR D 110 8556 1.81
REMARK 500 CZ TYR D 110 OH TYR D 110 8556 2.06
REMARK 500 CZ TYR C 110 CZ TYR C 110 8556 2.10
REMARK 500 CZ TYR D 110 CZ TYR D 110 8556 2.11
REMARK 500 OH TYR C 110 OH TYR C 110 8556 2.12
REMARK 500 CZ TYR C 110 OH TYR C 110 8556 2.15
REMARK 500 CE1 TYR C 110 OH TYR C 110 8556 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG C 148 NE ARG C 148 CZ 0.130
REMARK 500 ARG D 148 NE ARG D 148 CZ 0.119
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 CYS A 178 CB - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG B 68 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 CYS B 178 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 TYR C 110 CA - CB - CG ANGL. DEV. = -11.8 DEGREES
REMARK 500 ARG C 148 CA - CB - CG ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG C 148 CG - CD - NE ANGL. DEV. = 23.6 DEGREES
REMARK 500 ARG C 148 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG C 148 NH1 - CZ - NH2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 ARG C 148 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG C 148 NE - CZ - NH2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP C 165 CB - CA - C ANGL. DEV. = -14.2 DEGREES
REMARK 500 CYS C 178 CB - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 TYR D 110 CA - CB - CG ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG D 146 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 148 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG D 148 CG - CD - NE ANGL. DEV. = 20.4 DEGREES
REMARK 500 ARG D 148 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG D 148 NH1 - CZ - NH2 ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG D 148 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG D 148 NE - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 CYS D 178 CB - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 178 -128.39 65.80
REMARK 500 ARG A 191 77.84 -115.58
REMARK 500 HIS A 232 -92.87 -117.67
REMARK 500 PHE B 85 -163.65 -161.84
REMARK 500 CYS B 178 -126.63 63.77
REMARK 500 ARG B 191 76.36 -118.85
REMARK 500 HIS B 232 -93.73 -122.54
REMARK 500 PRO C 57 157.27 -49.35
REMARK 500 PHE C 85 -178.98 -171.94
REMARK 500 THR C 111 -3.63 71.74
REMARK 500 PRO C 162 -5.72 -57.68
REMARK 500 CYS C 178 -124.66 62.22
REMARK 500 HIS C 204 138.25 -174.90
REMARK 500 HIS C 232 -92.53 -122.76
REMARK 500 THR D 111 -8.34 78.09
REMARK 500 THR D 113 -169.96 -119.98
REMARK 500 PRO D 162 -7.82 -55.97
REMARK 500 CYS D 178 -125.41 64.84
REMARK 500 HIS D 204 136.76 -176.33
REMARK 500 ASN D 223 46.90 -108.16
REMARK 500 HIS D 232 -85.75 -119.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 146 0.09 SIDE CHAIN
REMARK 500 ARG B 146 0.11 SIDE CHAIN
REMARK 500 ARG C 148 0.14 SIDE CHAIN
REMARK 500 ARG C 213 0.07 SIDE CHAIN
REMARK 500 ARG C 261 0.09 SIDE CHAIN
REMARK 500 ARG C 276 0.11 SIDE CHAIN
REMARK 500 ARG D 146 0.09 SIDE CHAIN
REMARK 500 ARG D 148 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8XHO RELATED DB: PDB
DBREF 9J8I A 50 319 PDB 9J8I 9J8I 50 319
DBREF 9J8I B 50 319 PDB 9J8I 9J8I 50 319
DBREF 9J8I C 50 319 PDB 9J8I 9J8I 50 319
DBREF 9J8I D 50 319 PDB 9J8I 9J8I 50 319
SEQRES 1 A 270 SER ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 A 270 SER VAL THR ALA SER ARG GLY PRO PHE ALA THR THR THR
SEQRES 3 A 270 ASP SER VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY
SEQRES 4 A 270 THR ILE TYR TYR PRO THR ASP THR SER GLU GLY THR PHE
SEQRES 5 A 270 GLY GLY VAL VAL ILE ALA PRO GLY TYR THR ALA THR GLN
SEQRES 6 A 270 SER SER ILE ALA TRP MET GLY HIS ARG ILE ALA SER GLN
SEQRES 7 A 270 GLY PHE VAL VAL PHE THR ILE ASP THR ASN THR ARG TYR
SEQRES 8 A 270 ASP GLN PRO ASP SER ARG GLY ARG GLN ILE LEU ALA ALA
SEQRES 9 A 270 LEU ASP TYR LEU THR GLN GLN SER PRO VAL ARG ASP ARG
SEQRES 10 A 270 VAL ASP PRO ASN ARG LEU ALA VAL MET GLY HIS CYS MET
SEQRES 11 A 270 GLY GLY GLY GLY THR LEU ARG ALA ALA GLU ASN ARG PRO
SEQRES 12 A 270 SER LEU LYS ALA ALA ILE PRO LEU ALA PRO TRP HIS LEU
SEQRES 13 A 270 GLN LYS ASP TRP SER ASN VAL ARG VAL PRO THR MET ILE
SEQRES 14 A 270 ILE GLY CYS GLU ASN ASP THR VAL ALA SER VAL SER THR
SEQRES 15 A 270 HIS ALA ILE ARG PHE TYR GLU SER LEU PRO SER SER LEU
SEQRES 16 A 270 PRO LYS ALA TYR LEU GLU LEU ARG GLY ALA ASP HIS PHE
SEQRES 17 A 270 ALA PRO ASN ARG PRO ASN THR THR ILE ALA LYS TYR VAL
SEQRES 18 A 270 ILE ALA TRP LEU LYS ARG PHE VAL ASP GLU ASP GLU ARG
SEQRES 19 A 270 TYR GLU GLN PHE LEU CYS PRO PRO PRO ASP THR GLY LEU
SEQRES 20 A 270 PHE SER ASP PHE SER ASP TYR ARG ASP SER CYS PRO HIS
SEQRES 21 A 270 THR THR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 270 SER ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 B 270 SER VAL THR ALA SER ARG GLY PRO PHE ALA THR THR THR
SEQRES 3 B 270 ASP SER VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY
SEQRES 4 B 270 THR ILE TYR TYR PRO THR ASP THR SER GLU GLY THR PHE
SEQRES 5 B 270 GLY GLY VAL VAL ILE ALA PRO GLY TYR THR ALA THR GLN
SEQRES 6 B 270 SER SER ILE ALA TRP MET GLY HIS ARG ILE ALA SER GLN
SEQRES 7 B 270 GLY PHE VAL VAL PHE THR ILE ASP THR ASN THR ARG TYR
SEQRES 8 B 270 ASP GLN PRO ASP SER ARG GLY ARG GLN ILE LEU ALA ALA
SEQRES 9 B 270 LEU ASP TYR LEU THR GLN GLN SER PRO VAL ARG ASP ARG
SEQRES 10 B 270 VAL ASP PRO ASN ARG LEU ALA VAL MET GLY HIS CYS MET
SEQRES 11 B 270 GLY GLY GLY GLY THR LEU ARG ALA ALA GLU ASN ARG PRO
SEQRES 12 B 270 SER LEU LYS ALA ALA ILE PRO LEU ALA PRO TRP HIS LEU
SEQRES 13 B 270 GLN LYS ASP TRP SER ASN VAL ARG VAL PRO THR MET ILE
SEQRES 14 B 270 ILE GLY CYS GLU ASN ASP THR VAL ALA SER VAL SER THR
SEQRES 15 B 270 HIS ALA ILE ARG PHE TYR GLU SER LEU PRO SER SER LEU
SEQRES 16 B 270 PRO LYS ALA TYR LEU GLU LEU ARG GLY ALA ASP HIS PHE
SEQRES 17 B 270 ALA PRO ASN ARG PRO ASN THR THR ILE ALA LYS TYR VAL
SEQRES 18 B 270 ILE ALA TRP LEU LYS ARG PHE VAL ASP GLU ASP GLU ARG
SEQRES 19 B 270 TYR GLU GLN PHE LEU CYS PRO PRO PRO ASP THR GLY LEU
SEQRES 20 B 270 PHE SER ASP PHE SER ASP TYR ARG ASP SER CYS PRO HIS
SEQRES 21 B 270 THR THR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 270 SER ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 C 270 SER VAL THR ALA SER ARG GLY PRO PHE ALA THR THR THR
SEQRES 3 C 270 ASP SER VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY
SEQRES 4 C 270 THR ILE TYR TYR PRO THR ASP THR SER GLU GLY THR PHE
SEQRES 5 C 270 GLY GLY VAL VAL ILE ALA PRO GLY TYR THR ALA THR GLN
SEQRES 6 C 270 SER SER ILE ALA TRP MET GLY HIS ARG ILE ALA SER GLN
SEQRES 7 C 270 GLY PHE VAL VAL PHE THR ILE ASP THR ASN THR ARG TYR
SEQRES 8 C 270 ASP GLN PRO ASP SER ARG GLY ARG GLN ILE LEU ALA ALA
SEQRES 9 C 270 LEU ASP TYR LEU THR GLN GLN SER PRO VAL ARG ASP ARG
SEQRES 10 C 270 VAL ASP PRO ASN ARG LEU ALA VAL MET GLY HIS CYS MET
SEQRES 11 C 270 GLY GLY GLY GLY THR LEU ARG ALA ALA GLU ASN ARG PRO
SEQRES 12 C 270 SER LEU LYS ALA ALA ILE PRO LEU ALA PRO TRP HIS LEU
SEQRES 13 C 270 GLN LYS ASP TRP SER ASN VAL ARG VAL PRO THR MET ILE
SEQRES 14 C 270 ILE GLY CYS GLU ASN ASP THR VAL ALA SER VAL SER THR
SEQRES 15 C 270 HIS ALA ILE ARG PHE TYR GLU SER LEU PRO SER SER LEU
SEQRES 16 C 270 PRO LYS ALA TYR LEU GLU LEU ARG GLY ALA ASP HIS PHE
SEQRES 17 C 270 ALA PRO ASN ARG PRO ASN THR THR ILE ALA LYS TYR VAL
SEQRES 18 C 270 ILE ALA TRP LEU LYS ARG PHE VAL ASP GLU ASP GLU ARG
SEQRES 19 C 270 TYR GLU GLN PHE LEU CYS PRO PRO PRO ASP THR GLY LEU
SEQRES 20 C 270 PHE SER ASP PHE SER ASP TYR ARG ASP SER CYS PRO HIS
SEQRES 21 C 270 THR THR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 270 SER ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 D 270 SER VAL THR ALA SER ARG GLY PRO PHE ALA THR THR THR
SEQRES 3 D 270 ASP SER VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY
SEQRES 4 D 270 THR ILE TYR TYR PRO THR ASP THR SER GLU GLY THR PHE
SEQRES 5 D 270 GLY GLY VAL VAL ILE ALA PRO GLY TYR THR ALA THR GLN
SEQRES 6 D 270 SER SER ILE ALA TRP MET GLY HIS ARG ILE ALA SER GLN
SEQRES 7 D 270 GLY PHE VAL VAL PHE THR ILE ASP THR ASN THR ARG TYR
SEQRES 8 D 270 ASP GLN PRO ASP SER ARG GLY ARG GLN ILE LEU ALA ALA
SEQRES 9 D 270 LEU ASP TYR LEU THR GLN GLN SER PRO VAL ARG ASP ARG
SEQRES 10 D 270 VAL ASP PRO ASN ARG LEU ALA VAL MET GLY HIS CYS MET
SEQRES 11 D 270 GLY GLY GLY GLY THR LEU ARG ALA ALA GLU ASN ARG PRO
SEQRES 12 D 270 SER LEU LYS ALA ALA ILE PRO LEU ALA PRO TRP HIS LEU
SEQRES 13 D 270 GLN LYS ASP TRP SER ASN VAL ARG VAL PRO THR MET ILE
SEQRES 14 D 270 ILE GLY CYS GLU ASN ASP THR VAL ALA SER VAL SER THR
SEQRES 15 D 270 HIS ALA ILE ARG PHE TYR GLU SER LEU PRO SER SER LEU
SEQRES 16 D 270 PRO LYS ALA TYR LEU GLU LEU ARG GLY ALA ASP HIS PHE
SEQRES 17 D 270 ALA PRO ASN ARG PRO ASN THR THR ILE ALA LYS TYR VAL
SEQRES 18 D 270 ILE ALA TRP LEU LYS ARG PHE VAL ASP GLU ASP GLU ARG
SEQRES 19 D 270 TYR GLU GLN PHE LEU CYS PRO PRO PRO ASP THR GLY LEU
SEQRES 20 D 270 PHE SER ASP PHE SER ASP TYR ARG ASP SER CYS PRO HIS
SEQRES 21 D 270 THR THR LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *73(H2 O)
HELIX 1 AA1 THR A 60 THR A 65 1 6
HELIX 2 AA2 THR A 113 ILE A 117 5 5
HELIX 3 AA3 ALA A 118 SER A 126 1 9
HELIX 4 AA4 GLN A 142 GLN A 160 1 19
HELIX 5 AA5 VAL A 163 ASP A 165 5 3
HELIX 6 AA6 MET A 179 ARG A 191 1 13
HELIX 7 AA7 HIS A 232 LEU A 240 1 9
HELIX 8 AA8 PHE A 257 ARG A 261 5 5
HELIX 9 AA9 ASN A 263 ASP A 279 1 17
HELIX 10 AB1 ASP A 281 LEU A 288 5 8
HELIX 11 AB2 THR B 60 ALA B 66 1 7
HELIX 12 AB3 THR B 113 ALA B 118 5 6
HELIX 13 AB4 TRP B 119 SER B 126 1 8
HELIX 14 AB5 GLN B 142 GLN B 160 1 19
HELIX 15 AB6 VAL B 163 ASP B 165 5 3
HELIX 16 AB7 MET B 179 ARG B 191 1 13
HELIX 17 AB8 HIS B 232 LEU B 240 1 9
HELIX 18 AB9 PHE B 257 ARG B 261 5 5
HELIX 19 AC1 ASN B 263 ASP B 279 1 17
HELIX 20 AC2 ASP B 281 ARG B 283 5 3
HELIX 21 AC3 TYR B 284 CYS B 289 1 6
HELIX 22 AC4 THR C 60 THR C 65 1 6
HELIX 23 AC5 THR C 113 ALA C 118 5 6
HELIX 24 AC6 TRP C 119 SER C 126 1 8
HELIX 25 AC7 GLN C 142 GLN C 160 1 19
HELIX 26 AC8 VAL C 163 ASP C 165 5 3
HELIX 27 AC9 MET C 179 ARG C 191 1 13
HELIX 28 AD1 HIS C 232 LEU C 240 1 9
HELIX 29 AD2 PHE C 257 ARG C 261 5 5
HELIX 30 AD3 ASN C 263 ASP C 279 1 17
HELIX 31 AD4 ASP C 281 ARG C 283 5 3
HELIX 32 AD5 TYR C 284 CYS C 289 1 6
HELIX 33 AD6 THR D 60 ALA D 66 1 7
HELIX 34 AD7 THR D 113 ALA D 118 5 6
HELIX 35 AD8 TRP D 119 SER D 126 1 8
HELIX 36 AD9 ASP D 144 GLN D 160 1 17
HELIX 37 AE1 VAL D 163 ASP D 165 5 3
HELIX 38 AE2 CYS D 178 ARG D 191 1 14
HELIX 39 AE3 HIS D 232 SER D 239 1 8
HELIX 40 AE4 PHE D 257 ARG D 261 5 5
HELIX 41 AE5 ASN D 263 VAL D 278 1 16
HELIX 42 AE6 ASP D 281 LEU D 288 5 8
SHEET 1 AA1 6 THR A 73 VAL A 78 0
SHEET 2 AA1 6 GLY A 88 PRO A 93 -1 O ILE A 90 N ASP A 76
SHEET 3 AA1 6 VAL A 130 ILE A 134 -1 O VAL A 131 N TYR A 91
SHEET 4 AA1 6 PHE A 101 ALA A 107 1 N VAL A 104 O PHE A 132
SHEET 5 AA1 6 VAL A 167 CYS A 178 1 O ASP A 168 N PHE A 101
SHEET 6 AA1 6 ALA A 196 PRO A 202 1 O LEU A 200 N GLY A 176
SHEET 1 AA2 3 THR A 216 CYS A 221 0
SHEET 2 AA2 3 LYS A 246 LEU A 251 1 O LEU A 249 N GLY A 220
SHEET 3 AA2 3 PHE A 300 ASP A 305 -1 O SER A 301 N GLU A 250
SHEET 1 AA3 6 THR B 73 VAL B 78 0
SHEET 2 AA3 6 GLY B 88 PRO B 93 -1 O GLY B 88 N VAL B 78
SHEET 3 AA3 6 VAL B 130 ILE B 134 -1 O VAL B 131 N TYR B 91
SHEET 4 AA3 6 PHE B 101 ALA B 107 1 N VAL B 104 O PHE B 132
SHEET 5 AA3 6 VAL B 167 HIS B 177 1 O ALA B 173 N GLY B 103
SHEET 6 AA3 6 ALA B 196 LEU B 200 1 O LEU B 200 N GLY B 176
SHEET 1 AA4 3 THR B 216 CYS B 221 0
SHEET 2 AA4 3 LYS B 246 LEU B 251 1 O ALA B 247 N ILE B 218
SHEET 3 AA4 3 PHE B 300 ASP B 305 -1 O SER B 301 N GLU B 250
SHEET 1 AA5 6 THR C 73 VAL C 78 0
SHEET 2 AA5 6 GLY C 88 PRO C 93 -1 O ILE C 90 N ASP C 76
SHEET 3 AA5 6 VAL C 130 ILE C 134 -1 O VAL C 131 N TYR C 91
SHEET 4 AA5 6 PHE C 101 ALA C 107 1 N VAL C 104 O PHE C 132
SHEET 5 AA5 6 VAL C 167 HIS C 177 1 O ALA C 173 N GLY C 103
SHEET 6 AA5 6 ALA C 196 LEU C 200 1 O LEU C 200 N GLY C 176
SHEET 1 AA6 3 THR C 216 CYS C 221 0
SHEET 2 AA6 3 LYS C 246 LEU C 251 1 O LEU C 249 N GLY C 220
SHEET 3 AA6 3 PHE C 300 ASP C 305 -1 O SER C 301 N GLU C 250
SHEET 1 AA7 6 THR D 73 VAL D 78 0
SHEET 2 AA7 6 GLY D 88 PRO D 93 -1 O ILE D 90 N ASP D 76
SHEET 3 AA7 6 VAL D 130 ILE D 134 -1 O VAL D 131 N TYR D 91
SHEET 4 AA7 6 PHE D 101 ALA D 107 1 N VAL D 104 O VAL D 130
SHEET 5 AA7 6 VAL D 167 HIS D 177 1 O ALA D 173 N GLY D 103
SHEET 6 AA7 6 ALA D 196 LEU D 200 1 O LEU D 200 N GLY D 176
SHEET 1 AA8 3 THR D 216 CYS D 221 0
SHEET 2 AA8 3 LYS D 246 LEU D 251 1 O LEU D 249 N GLY D 220
SHEET 3 AA8 3 PHE D 300 ASP D 305 -1 O ARG D 304 N TYR D 248
SSBOND 1 CYS A 289 CYS A 307 1555 1555 2.16
SSBOND 2 CYS B 289 CYS B 307 1555 1555 2.27
SSBOND 3 CYS C 289 CYS C 307 1555 1555 2.34
SSBOND 4 CYS D 289 CYS D 307 1555 1555 2.39
CISPEP 1 CYS A 289 PRO A 290 0 15.32
CISPEP 2 CYS A 307 PRO A 308 0 5.77
CISPEP 3 CYS B 289 PRO B 290 0 15.34
CISPEP 4 CYS B 307 PRO B 308 0 0.81
CISPEP 5 CYS C 289 PRO C 290 0 10.30
CISPEP 6 CYS D 289 PRO D 290 0 5.22
CRYST1 187.940 187.940 132.020 90.00 90.00 90.00 P 42 21 2 32
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 0.005321 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007575 0.00000
TER 1999 PRO A 308
TER 3998 PRO B 308
TER 5997 PRO C 308
TER 7996 PRO D 308
MASTER 473 0 0 42 36 0 0 6 8065 4 8 84
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