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HEADER HYDROLASE 04-JUL-08 3DOH
TITLE CRYSTAL STRUCTURE OF A THERMOSTABLE ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 16-395;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 STRAIN: MSB8;
SOURCE 5 GENE: TM_0033;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-24D
KEYWDS ALPHA-BETA HYDROLASE, BETA SHEET
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LEVISSON,L.SUN,S.HENDRIKS,B.W.DIJKSTRA,J.VAN DER OOST,
AUTHOR 2 S.W.M.KENGEN
REVDAT 1 17-FEB-09 3DOH 0
JRNL AUTH M.LEVISSON,L.SUN,S.HENDRIKS,P.SWINKELS,T.AKVELD,
JRNL AUTH 2 J.B.BULTEMA,A.BARENDREGT,R.H.H.VAN DEN HEUVEL,
JRNL AUTH 3 B.W.DIJKSTRA,J.VAN DER OOST,S.W.M.KENGEN
JRNL TITL CRYSTAL STRUCTURE AND BIOCHEMICAL PROPERTIES OF A
JRNL TITL 2 NOVEL THERMOSTABLE ESTERASE CONTAINING AN
JRNL TITL 3 IMMUNOGLOBULIN-LIKE DOMAIN.
JRNL REF J.MOL.BIOL. V. 385 949 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19013466
JRNL DOI 10.1016/J.JMB.2008.10.075
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 28373
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1506
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2092
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5982
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
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): 0.693
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.335
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.245
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.516
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6185 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8427 ; 1.887 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 745 ;10.304 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 286 ;35.953 ;24.476
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1011 ;20.566 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;19.916 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 918 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4719 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3016 ; 0.247 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4127 ; 0.329 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 323 ; 0.163 ; 0.200
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): 70 ; 0.285 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.077 ; 0.200
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): 3841 ; 0.931 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6111 ; 1.639 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2706 ; 2.007 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2316 ; 3.242 ; 4.500
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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3DOH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-08.
REMARK 100 THE RCSB ID CODE IS RCSB048291.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000, 0.9791, 0.9793, 0.9757
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31079
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 1M LITHIUM SULPHATE
REMARK 280 MONOHYDRATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 65.07850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 37.57309
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 102.06133
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 65.07850
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 37.57309
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 102.06133
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 65.07850
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 37.57309
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 102.06133
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 65.07850
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 37.57309
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 102.06133
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 65.07850
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 37.57309
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 102.06133
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 65.07850
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 37.57309
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 102.06133
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 75.14618
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 204.12267
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 75.14618
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 204.12267
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 75.14618
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 204.12267
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 75.14618
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 204.12267
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 75.14618
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 204.12267
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 75.14618
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 204.12267
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 GLN A 16
REMARK 465 GLU A 17
REMARK 465 ASP A 18
REMARK 465 VAL A 19
REMARK 465 THR A 20
REMARK 465 GLN B 16
REMARK 465 GLU B 17
REMARK 465 ASP B 18
REMARK 465 VAL B 19
REMARK 465 THR B 20
REMARK 465 ARG B 249
REMARK 465 GLU B 250
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 ARG A 395 O
REMARK 470 ARG B 395 O
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 THR A 64 102.89 -177.02
REMARK 500 HIS A 106 59.91 -91.81
REMARK 500 MET A 121 106.56 1.46
REMARK 500 ASP A 150 137.53 -179.33
REMARK 500 ILE A 155 -34.26 108.59
REMARK 500 VAL A 171 127.35 -28.25
REMARK 500 TYR A 206 -52.26 -125.61
REMARK 500 CYS A 229 117.79 173.06
REMARK 500 SER A 240 -146.05 -137.97
REMARK 500 SER A 241 155.79 166.08
REMARK 500 THR A 244 57.76 -63.44
REMARK 500 ASP A 248 127.72 165.72
REMARK 500 ARG A 249 70.61 -102.31
REMARK 500 GLU A 250 -61.90 -145.58
REMARK 500 PRO A 252 49.11 -76.27
REMARK 500 ARG A 279 54.21 -141.63
REMARK 500 SER A 286 -112.19 68.19
REMARK 500 PHE A 299 57.09 -143.18
REMARK 500 CYS A 310 78.96 35.55
REMARK 500 ASP B 66 -25.92 172.39
REMARK 500 TYR B 77 -163.50 -179.71
REMARK 500 ASN B 79 167.60 179.16
REMARK 500 SER B 81 -86.56 -112.46
REMARK 500 LEU B 84 34.39 -94.40
REMARK 500 PRO B 114 49.62 -86.09
REMARK 500 ASN B 115 -138.97 -140.06
REMARK 500 PHE B 116 56.17 -109.49
REMARK 500 ILE B 155 7.05 55.98
REMARK 500 GLU B 168 -67.65 -23.97
REMARK 500 THR B 169 141.81 157.95
REMARK 500 ASN B 184 126.41 -35.20
REMARK 500 ASP B 186 42.02 -100.21
REMARK 500 THR B 203 -6.77 -145.38
REMARK 500 TYR B 206 -53.53 -132.44
REMARK 500 PRO B 238 150.72 -48.42
REMARK 500 ASN B 239 -9.17 67.39
REMARK 500 THR B 244 41.66 -71.90
REMARK 500 SER B 286 -106.93 58.23
REMARK 500 HIS B 330 139.93 -170.32
REMARK 500 LYS B 355 47.16 76.36
REMARK 500 PRO B 373 6.07 -65.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 120 MET A 121 138.10
REMARK 500 MET A 121 LYS A 122 143.06
REMARK 500 ASP A 137 GLY A 138 -43.22
REMARK 500 PRO A 228 CYS A 229 -114.19
REMARK 500 CYS A 236 PRO A 237 -148.52
REMARK 500 PRO A 237 PRO A 238 -132.23
REMARK 500 GLY A 312 GLY A 313 -125.58
REMARK 500 GLY A 353 GLY A 354 129.79
REMARK 500 THR B 64 GLY B 65 -53.00
REMARK 500 TYR B 77 ALA B 78 -149.74
REMARK 500 GLY B 82 GLY B 83 142.32
REMARK 500 GLY B 113 PRO B 114 -142.30
REMARK 500 LYS B 181 ASP B 182 -65.53
REMARK 500 ASP B 182 VAL B 183 -147.75
REMARK 500 HIS B 196 GLY B 197 77.75
REMARK 500 GLY B 353 GLY B 354 135.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN B 90 21.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 400
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 500
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DOI RELATED DB: PDB
DBREF 3DOH A 16 395 UNP Q9WXP0 Q9WXP0_THEMA 16 395
DBREF 3DOH B 16 395 UNP Q9WXP0 Q9WXP0_THEMA 16 395
SEQRES 1 A 380 GLN GLU ASP VAL THR VAL LYS SER VAL THR LEU ILE THR
SEQRES 2 A 380 LYS VAL PHE PRO GLU GLY GLU LYS VAL CYS ALA VAL VAL
SEQRES 3 A 380 ILE GLU TYR PRO VAL GLU ILE ASP GLY GLN LYS LEU SER
SEQRES 4 A 380 PRO ASP GLN PHE SER VAL LYS VAL LYS THR GLY ASP THR
SEQRES 5 A 380 TYR SER SER ARG THR ILE THR LYS VAL TYR ALA ASN ASN
SEQRES 6 A 380 SER GLY GLY LEU SER PHE SER ILE PHE ASN ASN ARG GLY
SEQRES 7 A 380 LYS TYR VAL VAL LEU GLU LEU SER THR GLU ASP LEU HIS
SEQRES 8 A 380 SER ASN THR ILE VAL PHE GLY PRO ASN PHE LEU ASN THR
SEQRES 9 A 380 ARG MET LYS LEU ASP TYR ILE VAL SER GLN LEU VAL PRO
SEQRES 10 A 380 ILE PHE ASP VAL ASP GLY ASN GLU VAL GLU PRO PHE THR
SEQRES 11 A 380 SER LYS GLN THR ASP GLU LYS HIS LEU ILE ILE ASP ASP
SEQRES 12 A 380 PHE LEU ALA PHE THR PHE LYS ASP PRO GLU THR GLY VAL
SEQRES 13 A 380 GLU ILE PRO TYR ARG LEU PHE VAL PRO LYS ASP VAL ASN
SEQRES 14 A 380 PRO ASP ARG LYS TYR PRO LEU VAL VAL PHE LEU HIS GLY
SEQRES 15 A 380 ALA GLY GLU ARG GLY THR ASP ASN TYR LEU GLN VAL ALA
SEQRES 16 A 380 GLY ASN ARG GLY ALA VAL VAL TRP ALA GLN PRO ARG TYR
SEQRES 17 A 380 GLN VAL VAL HIS PRO CYS PHE VAL LEU ALA PRO GLN CYS
SEQRES 18 A 380 PRO PRO ASN SER SER TRP SER THR LEU PHE THR ASP ARG
SEQRES 19 A 380 GLU ASN PRO PHE ASN PRO GLU LYS PRO LEU LEU ALA VAL
SEQRES 20 A 380 ILE LYS ILE ILE ARG LYS LEU LEU ASP GLU TYR ASN ILE
SEQRES 21 A 380 ASP GLU ASN ARG ILE TYR ILE THR GLY LEU SER MET GLY
SEQRES 22 A 380 GLY TYR GLY THR TRP THR ALA ILE MET GLU PHE PRO GLU
SEQRES 23 A 380 LEU PHE ALA ALA ALA ILE PRO ILE CYS GLY GLY GLY ASP
SEQRES 24 A 380 VAL SER LYS VAL GLU ARG ILE LYS ASP ILE PRO ILE TRP
SEQRES 25 A 380 VAL PHE HIS ALA GLU ASP ASP PRO VAL VAL PRO VAL GLU
SEQRES 26 A 380 ASN SER ARG VAL LEU VAL LYS LYS LEU ALA GLU ILE GLY
SEQRES 27 A 380 GLY LYS VAL ARG TYR THR GLU TYR GLU LYS GLY PHE MET
SEQRES 28 A 380 GLU LYS HIS GLY TRP ASP PRO HIS GLY SER TRP ILE PRO
SEQRES 29 A 380 THR TYR GLU ASN GLN GLU ALA ILE GLU TRP LEU PHE GLU
SEQRES 30 A 380 GLN SER ARG
SEQRES 1 B 380 GLN GLU ASP VAL THR VAL LYS SER VAL THR LEU ILE THR
SEQRES 2 B 380 LYS VAL PHE PRO GLU GLY GLU LYS VAL CYS ALA VAL VAL
SEQRES 3 B 380 ILE GLU TYR PRO VAL GLU ILE ASP GLY GLN LYS LEU SER
SEQRES 4 B 380 PRO ASP GLN PHE SER VAL LYS VAL LYS THR GLY ASP THR
SEQRES 5 B 380 TYR SER SER ARG THR ILE THR LYS VAL TYR ALA ASN ASN
SEQRES 6 B 380 SER GLY GLY LEU SER PHE SER ILE PHE ASN ASN ARG GLY
SEQRES 7 B 380 LYS TYR VAL VAL LEU GLU LEU SER THR GLU ASP LEU HIS
SEQRES 8 B 380 SER ASN THR ILE VAL PHE GLY PRO ASN PHE LEU ASN THR
SEQRES 9 B 380 ARG MET LYS LEU ASP TYR ILE VAL SER GLN LEU VAL PRO
SEQRES 10 B 380 ILE PHE ASP VAL ASP GLY ASN GLU VAL GLU PRO PHE THR
SEQRES 11 B 380 SER LYS GLN THR ASP GLU LYS HIS LEU ILE ILE ASP ASP
SEQRES 12 B 380 PHE LEU ALA PHE THR PHE LYS ASP PRO GLU THR GLY VAL
SEQRES 13 B 380 GLU ILE PRO TYR ARG LEU PHE VAL PRO LYS ASP VAL ASN
SEQRES 14 B 380 PRO ASP ARG LYS TYR PRO LEU VAL VAL PHE LEU HIS GLY
SEQRES 15 B 380 ALA GLY GLU ARG GLY THR ASP ASN TYR LEU GLN VAL ALA
SEQRES 16 B 380 GLY ASN ARG GLY ALA VAL VAL TRP ALA GLN PRO ARG TYR
SEQRES 17 B 380 GLN VAL VAL HIS PRO CYS PHE VAL LEU ALA PRO GLN CYS
SEQRES 18 B 380 PRO PRO ASN SER SER TRP SER THR LEU PHE THR ASP ARG
SEQRES 19 B 380 GLU ASN PRO PHE ASN PRO GLU LYS PRO LEU LEU ALA VAL
SEQRES 20 B 380 ILE LYS ILE ILE ARG LYS LEU LEU ASP GLU TYR ASN ILE
SEQRES 21 B 380 ASP GLU ASN ARG ILE TYR ILE THR GLY LEU SER MET GLY
SEQRES 22 B 380 GLY TYR GLY THR TRP THR ALA ILE MET GLU PHE PRO GLU
SEQRES 23 B 380 LEU PHE ALA ALA ALA ILE PRO ILE CYS GLY GLY GLY ASP
SEQRES 24 B 380 VAL SER LYS VAL GLU ARG ILE LYS ASP ILE PRO ILE TRP
SEQRES 25 B 380 VAL PHE HIS ALA GLU ASP ASP PRO VAL VAL PRO VAL GLU
SEQRES 26 B 380 ASN SER ARG VAL LEU VAL LYS LYS LEU ALA GLU ILE GLY
SEQRES 27 B 380 GLY LYS VAL ARG TYR THR GLU TYR GLU LYS GLY PHE MET
SEQRES 28 B 380 GLU LYS HIS GLY TRP ASP PRO HIS GLY SER TRP ILE PRO
SEQRES 29 B 380 THR TYR GLU ASN GLN GLU ALA ILE GLU TRP LEU PHE GLU
SEQRES 30 B 380 GLN SER ARG
HET SO4 A 400 5
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 502 5
HET SO4 B 500 5
HET SO4 B 501 5
HET SO4 B 503 5
HET SO4 B 504 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 10(O4 S 2-)
FORMUL 13 HOH *156(H2 O)
HELIX 1 1 GLN A 51 LEU A 53 5 3
HELIX 2 2 SER A 54 ASP A 56 5 3
HELIX 3 3 ASP A 104 ASN A 108 5 5
HELIX 4 4 ILE A 155 ASP A 157 5 3
HELIX 5 5 GLY A 197 ARG A 201 5 5
HELIX 6 6 TYR A 206 GLY A 211 1 6
HELIX 7 7 VAL A 216 ALA A 219 5 4
HELIX 8 8 GLN A 220 VAL A 225 1 6
HELIX 9 9 GLU A 256 TYR A 273 1 18
HELIX 10 10 SER A 286 PHE A 299 1 14
HELIX 11 11 ASP A 314 LYS A 322 5 9
HELIX 12 12 VAL A 339 ILE A 352 1 14
HELIX 13 13 GLY A 364 HIS A 369 1 6
HELIX 14 14 SER A 376 GLU A 382 1 7
HELIX 15 15 ASN A 383 GLU A 392 1 10
HELIX 16 16 ASP B 49 LEU B 53 5 5
HELIX 17 17 SER B 54 ASP B 56 5 3
HELIX 18 18 ASP B 104 ASN B 108 5 5
HELIX 19 19 TYR B 206 GLY B 211 1 6
HELIX 20 20 VAL B 216 ALA B 219 5 4
HELIX 21 21 GLN B 220 VAL B 225 1 6
HELIX 22 22 GLU B 256 TYR B 273 1 18
HELIX 23 23 SER B 286 PHE B 299 1 14
HELIX 24 24 ASP B 314 LYS B 322 5 9
HELIX 25 25 VAL B 339 ILE B 352 1 14
HELIX 26 26 GLY B 364 HIS B 369 1 6
HELIX 27 27 SER B 376 GLU B 382 1 7
HELIX 28 28 ASN B 383 GLU B 392 1 10
SHEET 1 A 5 ILE A 73 ASN A 79 0
SHEET 2 A 5 ARG A 92 LEU A 100 -1 O VAL A 97 N TYR A 77
SHEET 3 A 5 GLY A 34 ASP A 49 -1 N ILE A 42 O VAL A 96
SHEET 4 A 5 SER A 23 PHE A 31 -1 N ILE A 27 O ALA A 39
SHEET 5 A 5 ASP A 150 LEU A 154 1 O ASP A 150 N LEU A 26
SHEET 1 B 4 TYR A 68 ARG A 71 0
SHEET 2 B 4 PHE A 58 LYS A 63 -1 N VAL A 60 O ARG A 71
SHEET 3 B 4 TYR A 125 GLN A 129 -1 O SER A 128 N SER A 59
SHEET 4 B 4 PHE A 144 LYS A 147 -1 O SER A 146 N VAL A 127
SHEET 1 C 6 PHE A 159 LYS A 165 0
SHEET 2 C 6 GLU A 172 PHE A 178 -1 O TYR A 175 N PHE A 162
SHEET 3 C 6 PHE A 230 PRO A 234 -1 O ALA A 233 N ARG A 176
SHEET 4 C 6 TYR A 189 LEU A 195 1 N VAL A 192 O PHE A 230
SHEET 5 C 6 ILE A 275 LEU A 285 1 O TYR A 281 N LEU A 191
SHEET 6 C 6 ALA A 305 ILE A 309 1 O ILE A 309 N GLY A 284
SHEET 1 D 2 ILE A 326 ALA A 331 0
SHEET 2 D 2 VAL A 356 TYR A 361 1 O ARG A 357 N ILE A 326
SHEET 1 E 5 ILE B 73 ASN B 79 0
SHEET 2 E 5 TYR B 95 LEU B 100 -1 O VAL B 97 N TYR B 77
SHEET 3 E 5 GLY B 34 GLU B 43 -1 N VAL B 40 O LEU B 98
SHEET 4 E 5 SER B 23 PHE B 31 -1 N PHE B 31 O GLY B 34
SHEET 5 E 5 ASP B 150 HIS B 153 1 O ASP B 150 N LEU B 26
SHEET 1 F 4 THR B 67 ARG B 71 0
SHEET 2 F 4 PHE B 58 THR B 64 -1 N THR B 64 O THR B 67
SHEET 3 F 4 TYR B 125 GLN B 129 -1 O ILE B 126 N LYS B 61
SHEET 4 F 4 PHE B 144 LYS B 147 -1 O SER B 146 N VAL B 127
SHEET 1 G 2 ILE B 110 VAL B 111 0
SHEET 2 G 2 THR B 119 ARG B 120 -1 O THR B 119 N VAL B 111
SHEET 1 H 2 ILE B 133 PHE B 134 0
SHEET 2 H 2 GLU B 140 VAL B 141 -1 O VAL B 141 N ILE B 133
SHEET 1 I 6 LEU B 160 LYS B 165 0
SHEET 2 I 6 GLU B 172 PHE B 178 -1 O ILE B 173 N PHE B 164
SHEET 3 I 6 PHE B 230 PRO B 234 -1 O ALA B 233 N ARG B 176
SHEET 4 I 6 TYR B 189 LEU B 195 1 N VAL B 192 O PHE B 230
SHEET 5 I 6 ILE B 275 LEU B 285 1 O TYR B 281 N LEU B 191
SHEET 6 I 6 ALA B 305 ILE B 309 1 O ILE B 309 N GLY B 284
SHEET 1 J 2 ILE B 326 ALA B 331 0
SHEET 2 J 2 VAL B 356 TYR B 361 1 O ARG B 357 N ILE B 326
CISPEP 1 THR A 64 GLY A 65 0 3.01
CISPEP 2 PRO A 114 ASN A 115 0 -22.00
CISPEP 3 GLY A 138 ASN A 139 0 -22.59
CISPEP 4 ARG B 92 GLY B 93 0 -7.68
CISPEP 5 PRO B 167 GLU B 168 0 14.03
CISPEP 6 THR B 169 GLY B 170 0 5.83
SITE 1 AC1 7 PHE A 116 GLY A 197 ALA A 198 GLY A 199
SITE 2 AC1 7 SER A 286 MET A 287 HIS A 374
SITE 1 AC2 5 LYS A 29 ARG A 222 GLU A 332 GLU A 362
SITE 2 AC2 5 LYS A 363
SITE 1 AC3 4 LYS A 61 SER A 69 SER A 70 ASP B 56
SITE 1 AC4 5 LYS A 152 LEU A 154 ILE A 155 ASP A 157
SITE 2 AC4 5 ASP A 158
SITE 1 AC5 4 HIS A 153 ASP A 157 ARG A 176 TYR A 206
SITE 1 AC6 7 PHE B 116 GLY B 197 ALA B 198 GLY B 199
SITE 2 AC6 7 SER B 286 MET B 287 HIS B 374
SITE 1 AC7 5 LYS B 29 ARG B 222 GLU B 332 GLU B 362
SITE 2 AC7 5 LYS B 363
SITE 1 AC8 3 ASP A 56 SER B 69 SER B 70
SITE 1 AC9 5 LYS B 152 LEU B 154 ILE B 155 ASP B 157
SITE 2 AC9 5 ASP B 158
SITE 1 BC1 4 HIS B 153 ILE B 156 ASP B 157 ARG B 176
CRYST1 130.157 130.157 306.184 90.00 90.00 120.00 H 3 2 36
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 0.007683 0.004436 0.000000 0.00000
SCALE2 0.000000 0.008872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003266 0.00000
TER 3002 ARG A 395
TER 5984 ARG B 395
MASTER 470 0 10 28 38 0 16 6 6188 2 50 60
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