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HEADER HYDROLASE 13-NOV-08 3F98
TITLE CRYSTAL STRUCTURE OF HUMAN PLASMA PLATELET ACTIVATING FACTOR
TITLE 2 ACETYLHYDROLASE COVALENTLY INHIBITED BY TABUN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 47-429;
COMPND 5 SYNONYM: PAF ACETYLHYDROLASE, PAF 2-ACYLHYDROLASE, LDL-
COMPND 6 ASSOCIATED PHOSPHOLIPASE A2, LDL-PLA(2), 2-ACETYL-1-
COMPND 7 ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE, 1-ALKYL-2-
COMPND 8 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE;
COMPND 9 EC: 3.1.1.47;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLA2G7, PAFAH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PLASMA PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE, SECRETED
KEYWDS 2 PROTEIN, ALPHA/BETA-HYDROLASE-FOLD, LDL-BOUND; LIPOPROTEIN
KEYWDS 3 ASSOCIATED PHOSPHOLIPASE A2, LP-PLA2, GROUP VIIA PLA2,
KEYWDS 4 GLYCOPROTEIN, HYDROLASE, LIPID DEGRADATION, POLYMORPHISM,
KEYWDS 5 TABUN, DISEASE MUTATION, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR U.SAMANTA,B.J.BAHNSON
REVDAT 1 23-JUN-09 3F98 0
JRNL AUTH U.SAMANTA,S.D.KIRBY,P.SRINIVASAN,D.M.CERASOLI,
JRNL AUTH 2 B.J.BAHNSON
JRNL TITL CRYSTAL STRUCTURES OF HUMAN GROUP-VIIA
JRNL TITL 2 PHOSPHOLIPASE A2 INHIBITED BY ORGANOPHOSPHORUS
JRNL TITL 3 NERVE AGENTS EXHIBIT NON-AGED COMPLEXES.
JRNL REF BIOCHEM.PHARM. 2009
JRNL REFN ISSN 0006-2952
JRNL PMID 19394314
JRNL DOI 10.1016/J.BCP.2009.04.018
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 134355
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7097
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9769
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 497
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9351
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 1342
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.09000
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): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.692
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9772 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13072 ; 1.349 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1126 ; 6.500 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 472 ;36.830 ;23.941
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1737 ;14.629 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;16.931 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1425 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7204 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5137 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6633 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1135 ; 0.138 ; 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): 183 ; 0.235 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 75 ; 0.171 ; 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): 5995 ; 0.887 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9246 ; 1.456 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4267 ; 1.941 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3826 ; 2.945 ; 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 : 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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3F98 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0055
REMARK 200 MONOCHROMATOR : SI(111) 0.990
REMARK 200 OPTICS : ROSENBAUM-ROCK
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141507
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 10.000
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.0250
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 10.10
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.590
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP OF CCP4I, REFMAC5 OF CCP4I FOR REFINEMENT
REMARK 200 STARTING MODEL: NATIVE STRUCTURE, PDB ENTRY 3D59
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 126.92750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 126.92750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 38.49200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.66100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.49200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.66100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 126.92750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.49200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.66100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 126.92750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.49200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.66100
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
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 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1356 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 47
REMARK 465 ALA A 48
REMARK 465 ASN A 426
REMARK 465 GLN A 427
REMARK 465 HIS A 428
REMARK 465 ILE A 429
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 ASN B 426
REMARK 465 GLN B 427
REMARK 465 HIS B 428
REMARK 465 ILE B 429
REMARK 465 ALA C 47
REMARK 465 ALA C 48
REMARK 465 ASN C 426
REMARK 465 GLN C 427
REMARK 465 HIS C 428
REMARK 465 ILE C 429
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O1 FMT C 579 O HOH C 1817 2.16
REMARK 500 NE2 GLN B 287 O HOH B 1468 2.19
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 SER A 273 C SER A 273 O 0.189
REMARK 500 HIS A 272 C SER A 273 N 0.287
REMARK 500 SER B 273 C SER B 273 O 0.189
REMARK 500 HIS B 272 C SER B 273 N 0.287
REMARK 500 SER C 273 C SER C 273 O 0.187
REMARK 500 HIS C 272 C SER C 273 N 0.280
REMARK 500 SER C 273 C PHE C 274 N 0.148
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 SER A 273 CA - C - N ANGL. DEV. = 18.4 DEGREES
REMARK 500 SER A 273 O - C - N ANGL. DEV. = -14.6 DEGREES
REMARK 500 SER B 273 CA - C - N ANGL. DEV. = 18.4 DEGREES
REMARK 500 SER B 273 O - C - N ANGL. DEV. = -14.7 DEGREES
REMARK 500 SER C 273 CA - C - N ANGL. DEV. = 18.7 DEGREES
REMARK 500 SER C 273 O - C - N ANGL. DEV. = -16.8 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 GLN A 53 -60.87 -133.40
REMARK 500 PHE A 156 -177.11 -170.82
REMARK 500 HIS A 216 -31.78 -135.08
REMARK 500 SER A 273 -104.91 56.07
REMARK 500 HIS A 399 56.12 -102.81
REMARK 500 LYS A 400 -164.73 -116.98
REMARK 500 THR A 424 66.59 -150.72
REMARK 500 GLN B 53 -56.39 -132.75
REMARK 500 ASP B 73 -168.41 -71.59
REMARK 500 HIS B 216 -33.26 -137.40
REMARK 500 SER B 273 -104.89 56.10
REMARK 500 HIS B 399 58.01 -105.06
REMARK 500 LYS B 400 -163.14 -117.84
REMARK 500 THR B 424 63.66 -150.36
REMARK 500 GLN C 53 -57.10 -135.12
REMARK 500 ASP C 73 -168.80 -72.57
REMARK 500 HIS C 216 -32.98 -135.75
REMARK 500 SER C 273 -107.12 50.09
REMARK 500 HIS C 399 57.82 -105.58
REMARK 500 LYS C 400 -161.35 -118.90
REMARK 500 THR C 424 73.92 -151.17
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 ASP A 91 ARG A 92 -130.07
REMARK 500 ASP B 91 ARG B 92 -131.62
REMARK 500 ASP C 91 ARG C 92 -132.04
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 NTJ A 473
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 503
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 506
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 508
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 509
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 510
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 511
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 513
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 518
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 521
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 522
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 524
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 527
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 528
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 531
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 533
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 534
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 536
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 538
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 539
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 540
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 541
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 544
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 546
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 547
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 551
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 552
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 553
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 554
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 555
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 556
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 558
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NTJ B 473
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 501
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 502
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 504
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 505
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 507
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 512
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 514
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 515
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 516
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 517
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 520
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 523
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 525
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 526
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 529
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 530
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 532
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 535
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 537
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 542
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 543
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 545
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 548
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 549
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 550
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 557
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 586
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NTJ C 473
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 519
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 559
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 560
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 561
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 562
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 563
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 564
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 565
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 566
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 567
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 568
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 569
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 570
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 571
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 572
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 573
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 574
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 575
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 576
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 577
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 578
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 579
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 580
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 581
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 582
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 583
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 584
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 585
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D59 RELATED DB: PDB
REMARK 900 THE SAME WILD TYPE PROTEIN
REMARK 900 RELATED ID: 3D5E RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PARAOXON
REMARK 900 RELATED ID: 3F96 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SARIN
REMARK 900 RELATED ID: 3F97 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SOMAN
REMARK 900 RELATED ID: 3F98 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIISOPROPYLFLUOROPHOSPHATE
DBREF 3F98 A 47 429 UNP Q13093 PAFA_HUMAN 47 429
DBREF 3F98 B 47 429 UNP Q13093 PAFA_HUMAN 47 429
DBREF 3F98 C 47 429 UNP Q13093 PAFA_HUMAN 47 429
SEQRES 1 A 383 ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY
SEQRES 2 A 383 ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE
SEQRES 3 A 383 ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR
SEQRES 4 A 383 PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE
SEQRES 5 A 383 PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU
SEQRES 6 A 383 GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU
SEQRES 7 A 383 PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO
SEQRES 8 A 383 LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER
SEQRES 9 A 383 HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE
SEQRES 10 A 383 GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA
SEQRES 11 A 383 VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR
SEQRES 12 A 383 PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER
SEQRES 13 A 383 TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR
SEQRES 14 A 383 HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU
SEQRES 15 A 383 CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS
SEQRES 16 A 383 GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP
SEQRES 17 A 383 MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE
SEQRES 18 A 383 ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE
SEQRES 19 A 383 GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE
SEQRES 20 A 383 ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL
SEQRES 21 A 383 TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER
SEQRES 22 A 383 GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS
SEQRES 23 A 383 LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR
SEQRES 24 A 383 ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR
SEQRES 25 A 383 PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU
SEQRES 26 A 383 LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER
SEQRES 27 A 383 ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY
SEQRES 28 A 383 LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU
SEQRES 29 A 383 GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN
SEQRES 30 A 383 THR THR ASN GLN HIS ILE
SEQRES 1 B 383 ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY
SEQRES 2 B 383 ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE
SEQRES 3 B 383 ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR
SEQRES 4 B 383 PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE
SEQRES 5 B 383 PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU
SEQRES 6 B 383 GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU
SEQRES 7 B 383 PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO
SEQRES 8 B 383 LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER
SEQRES 9 B 383 HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE
SEQRES 10 B 383 GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA
SEQRES 11 B 383 VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR
SEQRES 12 B 383 PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER
SEQRES 13 B 383 TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR
SEQRES 14 B 383 HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU
SEQRES 15 B 383 CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS
SEQRES 16 B 383 GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP
SEQRES 17 B 383 MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE
SEQRES 18 B 383 ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE
SEQRES 19 B 383 GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE
SEQRES 20 B 383 ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL
SEQRES 21 B 383 TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER
SEQRES 22 B 383 GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS
SEQRES 23 B 383 LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR
SEQRES 24 B 383 ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR
SEQRES 25 B 383 PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU
SEQRES 26 B 383 LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER
SEQRES 27 B 383 ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY
SEQRES 28 B 383 LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU
SEQRES 29 B 383 GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN
SEQRES 30 B 383 THR THR ASN GLN HIS ILE
SEQRES 1 C 383 ALA ALA ALA SER PHE GLY GLN THR LYS ILE PRO ARG GLY
SEQRES 2 C 383 ASN GLY PRO TYR SER VAL GLY CYS THR ASP LEU MET PHE
SEQRES 3 C 383 ASP HIS THR ASN LYS GLY THR PHE LEU ARG LEU TYR TYR
SEQRES 4 C 383 PRO SER GLN ASP ASN ASP ARG LEU ASP THR LEU TRP ILE
SEQRES 5 C 383 PRO ASN LYS GLU TYR PHE TRP GLY LEU SER LYS PHE LEU
SEQRES 6 C 383 GLY THR HIS TRP LEU MET GLY ASN ILE LEU ARG LEU LEU
SEQRES 7 C 383 PHE GLY SER MET THR THR PRO ALA ASN TRP ASN SER PRO
SEQRES 8 C 383 LEU ARG PRO GLY GLU LYS TYR PRO LEU VAL VAL PHE SER
SEQRES 9 C 383 HIS GLY LEU GLY ALA PHE ARG THR LEU TYR SER ALA ILE
SEQRES 10 C 383 GLY ILE ASP LEU ALA SER HIS GLY PHE ILE VAL ALA ALA
SEQRES 11 C 383 VAL GLU HIS ARG ASP ARG SER ALA SER ALA THR TYR TYR
SEQRES 12 C 383 PHE LYS ASP GLN SER ALA ALA GLU ILE GLY ASP LYS SER
SEQRES 13 C 383 TRP LEU TYR LEU ARG THR LEU LYS GLN GLU GLU GLU THR
SEQRES 14 C 383 HIS ILE ARG ASN GLU GLN VAL ARG GLN ARG ALA LYS GLU
SEQRES 15 C 383 CYS SER GLN ALA LEU SER LEU ILE LEU ASP ILE ASP HIS
SEQRES 16 C 383 GLY LYS PRO VAL LYS ASN ALA LEU ASP LEU LYS PHE ASP
SEQRES 17 C 383 MET GLU GLN LEU LYS ASP SER ILE ASP ARG GLU LYS ILE
SEQRES 18 C 383 ALA VAL ILE GLY HIS SER PHE GLY GLY ALA THR VAL ILE
SEQRES 19 C 383 GLN THR LEU SER GLU ASP GLN ARG PHE ARG CYS GLY ILE
SEQRES 20 C 383 ALA LEU ASP ALA TRP MET PHE PRO LEU GLY ASP GLU VAL
SEQRES 21 C 383 TYR SER ARG ILE PRO GLN PRO LEU PHE PHE ILE ASN SER
SEQRES 22 C 383 GLU TYR PHE GLN TYR PRO ALA ASN ILE ILE LYS MET LYS
SEQRES 23 C 383 LYS CYS TYR SER PRO ASP LYS GLU ARG LYS MET ILE THR
SEQRES 24 C 383 ILE ARG GLY SER VAL HIS GLN ASN PHE ALA ASP PHE THR
SEQRES 25 C 383 PHE ALA THR GLY LYS ILE ILE GLY HIS MET LEU LYS LEU
SEQRES 26 C 383 LYS GLY ASP ILE ASP SER ASN VAL ALA ILE ASP LEU SER
SEQRES 27 C 383 ASN LYS ALA SER LEU ALA PHE LEU GLN LYS HIS LEU GLY
SEQRES 28 C 383 LEU HIS LYS ASP PHE ASP GLN TRP ASP CYS LEU ILE GLU
SEQRES 29 C 383 GLY ASP ASP GLU ASN LEU ILE PRO GLY THR ASN ILE ASN
SEQRES 30 C 383 THR THR ASN GLN HIS ILE
HET NTJ A 473 8
HET FMT A 503 3
HET FMT A 506 3
HET FMT A 508 3
HET FMT A 509 3
HET FMT A 510 3
HET FMT A 511 3
HET FMT A 513 3
HET FMT A 518 3
HET FMT A 521 3
HET FMT A 522 3
HET FMT A 524 3
HET FMT A 527 3
HET FMT A 528 3
HET FMT A 531 3
HET FMT A 533 3
HET FMT A 534 3
HET FMT A 536 3
HET FMT A 538 3
HET FMT A 539 3
HET FMT A 540 3
HET FMT A 541 3
HET FMT A 544 3
HET FMT A 546 3
HET FMT A 547 3
HET FMT A 551 3
HET FMT A 552 3
HET FMT A 553 3
HET FMT A 554 3
HET FMT A 555 3
HET FMT A 556 3
HET FMT A 558 3
HET NTJ B 473 8
HET FMT B 501 3
HET FMT B 502 3
HET FMT B 504 3
HET FMT B 505 3
HET FMT B 507 3
HET FMT B 512 3
HET FMT B 514 3
HET FMT B 515 3
HET FMT B 516 3
HET FMT B 517 3
HET FMT B 520 3
HET FMT B 523 3
HET FMT B 525 3
HET FMT B 526 3
HET FMT B 529 3
HET FMT B 530 3
HET FMT B 532 3
HET FMT B 535 3
HET FMT B 537 3
HET FMT B 542 3
HET FMT B 543 3
HET FMT B 545 3
HET FMT B 548 3
HET FMT B 549 3
HET FMT B 550 3
HET FMT B 557 3
HET FMT B 586 3
HET NTJ C 473 8
HET FMT C 519 3
HET FMT C 559 3
HET FMT C 560 3
HET FMT C 561 3
HET FMT C 562 3
HET FMT C 563 3
HET FMT C 564 3
HET FMT C 565 3
HET FMT C 566 3
HET FMT C 567 3
HET FMT C 568 3
HET FMT C 569 3
HET FMT C 570 3
HET FMT C 571 3
HET FMT C 572 3
HET FMT C 573 3
HET FMT C 574 3
HET FMT C 575 3
HET FMT C 576 3
HET FMT C 577 3
HET FMT C 578 3
HET FMT C 579 3
HET FMT C 580 3
HET FMT C 581 3
HET FMT C 582 3
HET FMT C 583 3
HET FMT C 584 3
HET FMT C 585 3
HETNAM NTJ R-ETHYL N,N-DIMETHYLPHOSPHONAMIDATE
HETNAM FMT FORMIC ACID
FORMUL 4 NTJ 3(C4 H12 N O2 P)
FORMUL 5 FMT 86(C H2 O2)
FORMUL 93 HOH *1084(H2 O)
HELIX 1 1 ASN A 100 GLY A 112 1 13
HELIX 2 2 TRP A 115 GLY A 126 1 12
HELIX 3 3 TYR A 160 HIS A 170 1 11
HELIX 4 4 ASP A 192 GLY A 199 1 8
HELIX 5 5 LYS A 210 HIS A 241 1 32
HELIX 6 6 ASP A 254 LYS A 259 5 6
HELIX 7 7 SER A 273 ASP A 286 1 14
HELIX 8 8 GLY A 303 ILE A 310 5 8
HELIX 9 9 TYR A 324 LYS A 333 1 10
HELIX 10 10 VAL A 350 ALA A 360 5 11
HELIX 11 11 GLY A 362 LEU A 369 1 8
HELIX 12 12 ASP A 376 GLY A 397 1 22
HELIX 13 13 ASP A 401 GLN A 404 5 4
HELIX 14 14 TRP A 405 GLU A 410 1 6
HELIX 15 15 ASN B 100 GLY B 112 1 13
HELIX 16 16 TRP B 115 GLY B 126 1 12
HELIX 17 17 TYR B 160 HIS B 170 1 11
HELIX 18 18 ASP B 192 GLY B 199 1 8
HELIX 19 19 LYS B 210 HIS B 241 1 32
HELIX 20 20 ASP B 254 LYS B 259 5 6
HELIX 21 21 SER B 273 ASP B 286 1 14
HELIX 22 22 GLY B 303 ILE B 310 5 8
HELIX 23 23 TYR B 324 LYS B 333 1 10
HELIX 24 24 VAL B 350 ALA B 360 5 11
HELIX 25 25 GLY B 362 LEU B 369 1 8
HELIX 26 26 ASP B 376 GLY B 397 1 22
HELIX 27 27 ASP B 401 GLN B 404 5 4
HELIX 28 28 TRP B 405 GLU B 410 1 6
HELIX 29 29 ASN C 100 GLY C 112 1 13
HELIX 30 30 TRP C 115 GLY C 126 1 12
HELIX 31 31 TYR C 160 HIS C 170 1 11
HELIX 32 32 ASP C 192 GLY C 199 1 8
HELIX 33 33 LYS C 210 HIS C 241 1 32
HELIX 34 34 ASP C 254 LYS C 259 5 6
HELIX 35 35 SER C 273 ASP C 286 1 14
HELIX 36 36 GLY C 303 ILE C 310 5 8
HELIX 37 37 TYR C 324 LYS C 333 1 10
HELIX 38 38 VAL C 350 ALA C 360 5 11
HELIX 39 39 GLY C 362 LEU C 369 1 8
HELIX 40 40 ASP C 376 GLY C 397 1 22
HELIX 41 41 ASP C 401 GLN C 404 5 4
HELIX 42 42 TRP C 405 GLU C 410 1 6
SHEET 1 A10 ASN A 133 TRP A 134 0
SHEET 2 A10 SER A 64 PHE A 72 1 N VAL A 65 O ASN A 133
SHEET 3 A10 THR A 79 SER A 87 -1 O LEU A 83 N THR A 68
SHEET 4 A10 ILE A 173 VAL A 177 -1 O ALA A 176 N ARG A 82
SHEET 5 A10 TYR A 144 SER A 150 1 N VAL A 147 O ALA A 175
SHEET 6 A10 ILE A 262 GLY A 271 1 O ASP A 263 N TYR A 144
SHEET 7 A10 CYS A 291 LEU A 295 1 O LEU A 295 N GLY A 271
SHEET 8 A10 LEU A 314 SER A 319 1 O PHE A 315 N ALA A 294
SHEET 9 A10 ARG A 341 ILE A 346 1 O LYS A 342 N PHE A 316
SHEET 10 A10 LEU A 416 PRO A 418 -1 O ILE A 417 N THR A 345
SHEET 1 B 2 THR A 95 LEU A 96 0
SHEET 2 B 2 THR A 129 THR A 130 -1 O THR A 130 N THR A 95
SHEET 1 C 2 ALA A 186 TYR A 189 0
SHEET 2 C 2 SER A 202 TYR A 205 -1 O SER A 202 N TYR A 189
SHEET 1 D10 ASN B 133 TRP B 134 0
SHEET 2 D10 SER B 64 PHE B 72 1 N VAL B 65 O ASN B 133
SHEET 3 D10 THR B 79 SER B 87 -1 O TYR B 85 N GLY B 66
SHEET 4 D10 ILE B 173 VAL B 177 -1 O ALA B 176 N ARG B 82
SHEET 5 D10 TYR B 144 SER B 150 1 N VAL B 147 O ALA B 175
SHEET 6 D10 ILE B 262 GLY B 271 1 O ASP B 263 N TYR B 144
SHEET 7 D10 CYS B 291 LEU B 295 1 O LEU B 295 N GLY B 271
SHEET 8 D10 LEU B 314 SER B 319 1 O PHE B 315 N ALA B 294
SHEET 9 D10 ARG B 341 ILE B 346 1 O LYS B 342 N PHE B 316
SHEET 10 D10 LEU B 416 PRO B 418 -1 O ILE B 417 N THR B 345
SHEET 1 E 2 THR B 95 LEU B 96 0
SHEET 2 E 2 THR B 129 THR B 130 -1 O THR B 130 N THR B 95
SHEET 1 F 2 ALA B 186 TYR B 189 0
SHEET 2 F 2 SER B 202 TYR B 205 -1 O SER B 202 N TYR B 189
SHEET 1 G10 ASN C 133 TRP C 134 0
SHEET 2 G10 SER C 64 PHE C 72 1 N VAL C 65 O ASN C 133
SHEET 3 G10 THR C 79 SER C 87 -1 O TYR C 85 N GLY C 66
SHEET 4 G10 ILE C 173 VAL C 177 -1 O ALA C 176 N ARG C 82
SHEET 5 G10 TYR C 144 SER C 150 1 N VAL C 147 O ALA C 175
SHEET 6 G10 ILE C 262 GLY C 271 1 O ASP C 263 N TYR C 144
SHEET 7 G10 CYS C 291 LEU C 295 1 O LEU C 295 N GLY C 271
SHEET 8 G10 LEU C 314 SER C 319 1 O PHE C 315 N ALA C 294
SHEET 9 G10 ARG C 341 ILE C 346 1 O LYS C 342 N PHE C 316
SHEET 10 G10 LEU C 416 PRO C 418 -1 O ILE C 417 N THR C 345
SHEET 1 H 2 THR C 95 LEU C 96 0
SHEET 2 H 2 THR C 129 THR C 130 -1 O THR C 130 N THR C 95
SHEET 1 I 2 ALA C 186 TYR C 189 0
SHEET 2 I 2 SER C 202 TYR C 205 -1 O SER C 202 N TYR C 189
LINK C HIS A 272 N SER A 273 1555 1555 1.62
LINK C SER A 273 N PHE A 274 1555 1555 1.44
LINK C HIS B 272 N SER B 273 1555 1555 1.62
LINK C SER B 273 N PHE B 274 1555 1555 1.44
LINK C HIS C 272 N SER C 273 1555 1555 1.62
LINK C SER C 273 N PHE C 274 1555 1555 1.48
LINK OG SER A 273 P1 NTJ A 473 1555 1555 1.63
LINK OG SER B 273 P1 NTJ B 473 1555 1555 1.61
LINK OG SER C 273 P1 NTJ C 473 1555 1555 1.63
CISPEP 1 PHE A 72 ASP A 73 0 -9.02
CISPEP 2 PHE B 72 ASP B 73 0 -9.90
CISPEP 3 PHE C 72 ASP C 73 0 -9.38
SITE 1 AC1 11 GLY A 152 LEU A 153 SER A 273 PHE A 274
SITE 2 AC1 11 TRP A 298 PHE A 322 HIS A 351 GLN A 352
SITE 3 AC1 11 HOH A1210 HOH A1392 PHE C 51
SITE 1 AC2 4 ILE A 98 ARG A 122 GLY A 126 PRO C 337
SITE 1 AC3 7 TYR A 335 ARG A 341 LYS A 342 MET A 343
SITE 2 AC3 7 FMT A 522 HOH A1641 ASN B 423
SITE 1 AC4 5 ASP A 374 ILE A 375 HOH A1049 HOH A1166
SITE 2 AC4 5 HOH A1631
SITE 1 AC5 4 PHE A 72 ASP A 73 GLY A 78 HOH A1288
SITE 1 AC6 4 ARG A 207 HIS A 216 HOH A1323 HOH A1628
SITE 1 AC7 7 ALA A 390 GLN A 393 LYS A 394 ASP A 403
SITE 2 AC7 7 ASP A 406 HOH A1176 HOH A1428
SITE 1 AC8 6 ARG A 182 LEU A 204 TYR A 205 HOH A1290
SITE 2 AC8 6 HOH A1367 HOH A1713
SITE 1 AC9 7 GLU A 320 ARG A 347 GLY A 348 HOH A1305
SITE 2 AC9 7 HOH A1362 HOH A1631 ASP B 412
SITE 1 BC1 5 ASN A 135 PRO A 137 PHE A 253 GLN A 257
SITE 2 BC1 5 HOH A1253
SITE 1 BC2 6 LYS A 339 GLU A 340 ARG A 341 FMT A 506
SITE 2 BC2 6 HOH A1130 HOH A1641
SITE 1 BC3 4 GLN A 88 ARG A 139 HOH A1307 HOH A1662
SITE 1 BC4 2 ASN A 119 HOH A1610
SITE 1 BC5 5 VAL A 245 ASN A 247 PHE A 253 MET A 255
SITE 2 BC5 5 HOH A1299
SITE 1 BC6 5 ASP A 181 ARG A 182 ARG A 207 FMT A 553
SITE 2 BC6 5 HOH A1485
SITE 1 BC7 8 HIS A 179 ASP A 181 ARG A 182 SER A 183
SITE 2 BC7 8 ALA A 184 THR A 187 LEU A 204 TYR A 205
SITE 1 BC8 4 PHE A 322 VAL A 350 HIS A 351 HOH A1684
SITE 1 BC9 2 LYS A 386 TRP A 405
SITE 1 CC1 6 TRP A 105 TRP A 203 TYR A 205 HOH A1074
SITE 2 CC1 6 HOH A1206 HOH A1727
SITE 1 CC2 3 LYS A 109 GLY A 112 THR A 113
SITE 1 CC3 4 ASP A 412 HOH A1271 HOH A1622 ARG B 92
SITE 1 CC4 5 ASP A 240 ASP A 260 ASP C 240 HIS C 241
SITE 2 CC4 5 ASP C 260
SITE 1 CC5 3 ASP A 406 CYS A 407 HOH A1622
SITE 1 CC6 7 ARG A 92 ASP A 94 ILE C 422 ASN C 423
SITE 2 CC6 7 FMT C 581 HOH C1749 HOH C1839
SITE 1 CC7 2 HIS A 367 ASP A 374
SITE 1 CC8 7 ASN A 100 TYR A 188 LYS A 201 HOH A1115
SITE 2 CC8 7 HOH A1198 HOH A1490 ASP C 338
SITE 1 CC9 5 PRO A 62 HIS A 170 LYS A 400 PHE A 402
SITE 2 CC9 5 HOH A1726
SITE 1 DC1 6 GLU A 220 GLN A 221 GLN A 224 FMT A 531
SITE 2 DC1 6 HOH A1410 HOH A1702
SITE 1 DC2 7 THR A 208 LEU A 209 GLU A 214 ARG A 218
SITE 2 DC2 7 HOH A1050 HOH A1624 SER C 50
SITE 1 DC3 8 LYS A 55 PRO A 57 ASN A 378 FMT A 556
SITE 2 DC3 8 HOH A1633 HOH A1657 THR C 215 HOH C1880
SITE 1 DC4 9 THR A 54 LYS A 55 FMT A 555 HOH A1633
SITE 2 DC4 9 THR C 215 PHE C 300 FMT C 582 HOH C1880
SITE 3 DC4 9 HOH C1909
SITE 1 DC5 5 GLU A 265 ARG A 290 HIS A 395 LEU A 396
SITE 2 DC5 5 HOH A1375
SITE 1 DC6 11 PHE B 51 GLY B 152 LEU B 153 SER B 273
SITE 2 DC6 11 PHE B 274 TRP B 298 PHE B 322 HIS B 351
SITE 3 DC6 11 GLN B 352 HOH B1112 HOH B1183
SITE 1 DC7 4 PHE B 72 ASP B 73 GLY B 78 HOH B1656
SITE 1 DC8 5 PHE B 322 VAL B 350 HIS B 351 HOH B1047
SITE 2 DC8 5 HOH B1595
SITE 1 DC9 4 ASP B 374 ILE B 375 FMT B 505 HOH B1637
SITE 1 EC1 5 ARG B 347 ASN B 415 FMT B 504 FMT B 515
SITE 2 EC1 5 HOH B1637
SITE 1 EC2 4 GLU B 142 LYS B 143 LYS B 259 HOH B1683
SITE 1 EC3 7 ASN A 423 TYR B 335 LYS B 342 MET B 343
SITE 2 EC3 7 GLY B 419 HOH B1453 HOH B1521
SITE 1 EC4 4 LYS B 55 PHE B 359 THR B 361 LYS B 372
SITE 1 EC5 8 ASP A 412 GLU B 320 TYR B 321 ARG B 347
SITE 2 EC5 8 GLY B 348 FMT B 505 HOH B1262 HOH B1301
SITE 1 EC6 6 PRO B 62 TYR B 63 HIS B 170 LYS B 400
SITE 2 EC6 6 PHE B 402 HOH B1400
SITE 1 EC7 5 GLU B 212 VAL B 379 HOH B1111 HOH B1182
SITE 2 EC7 5 HOH B1236
SITE 1 EC8 3 GLN B 393 LEU B 398 HOH B1629
SITE 1 EC9 6 TYR B 335 LYS B 339 GLU B 340 ARG B 341
SITE 2 EC9 6 HOH B1141 HOH B1536
SITE 1 FC1 3 ASN B 76 HOH B1533 HOH B1567
SITE 1 FC2 4 SER A 336 ARG B 122 FMT B 529 HOH B1325
SITE 1 FC3 9 SER A 336 PRO A 337 ASN B 100 LYS B 101
SITE 2 FC3 9 ARG B 122 FMT B 526 HOH B1048 HOH B1325
SITE 3 FC3 9 HOH B1482
SITE 1 FC4 6 LYS B 55 PRO B 57 GLN B 211 ASN B 378
SITE 2 FC4 6 HOH B1297 HOH B1572
SITE 1 FC5 7 THR B 54 LYS B 55 MET B 128 THR B 129
SITE 2 FC5 7 HOH B1132 HOH B1153 HOH B1189
SITE 1 FC6 8 HIS B 179 ASP B 181 ARG B 182 SER B 183
SITE 2 FC6 8 ALA B 184 THR B 187 LEU B 204 TYR B 205
SITE 1 FC7 3 ARG B 309 FMT B 549 HOH B1480
SITE 1 FC8 8 PRO B 57 ASN B 60 GLN B 211 ASN B 378
SITE 2 FC8 8 ILE B 381 ASP B 382 HOH B1101 HOH B1598
SITE 1 FC9 3 HOH B1632 PHE C 72 ASP C 73
SITE 1 GC1 6 PRO A 418 THR B 420 ILE B 422 ASN B 423
SITE 2 GC1 6 HOH B1099 HOH B1663
SITE 1 GC2 1 GLN B 257
SITE 1 GC3 5 GLU B 305 SER B 308 ARG B 309 FMT B 537
SITE 2 GC3 5 HOH B1157
SITE 1 GC4 7 ILE B 239 GLY B 242 LYS B 243 MET B 255
SITE 2 GC4 7 GLU B 256 LYS B 259 HOH B1486
SITE 1 GC5 4 GLU B 265 ARG B 290 HIS B 395 LEU B 396
SITE 1 GC6 8 ASN B 318 SER B 319 GLU B 320 GLN B 323
SITE 2 GC6 8 THR B 345 THR B 420 ASN B 421 ILE B 422
SITE 1 GC7 11 PHE A 51 GLY C 152 LEU C 153 SER C 273
SITE 2 GC7 11 PHE C 274 TRP C 298 PHE C 322 HIS C 351
SITE 3 GC7 11 GLN C 352 HOH C1842 HOH C1926
SITE 1 GC8 7 THR C 54 LYS C 55 MET C 128 THR C 129
SITE 2 GC8 7 HOH C1134 HOH C1195 HOH C1774
SITE 1 GC9 3 LYS C 386 TRP C 405 HOH C2047
SITE 1 HC1 3 ARG C 182 TYR C 205 FMT C 561
SITE 1 HC2 5 TRP C 203 TYR C 205 FMT C 560 HOH C1938
SITE 2 HC2 5 HOH C2031
SITE 1 HC3 3 GLU C 220 GLN C 224 HOH C1978
SITE 1 HC4 5 LYS C 363 LYS C 372 ASP C 376 SER C 377
SITE 2 HC4 5 HOH C1789
SITE 1 HC5 6 ASN C 135 SER C 136 PRO C 137 LYS C 252
SITE 2 HC5 6 GLN C 257 HOH C1822
SITE 1 HC6 6 GLU C 320 TYR C 321 ARG C 347 GLY C 348
SITE 2 HC6 6 ASP C 412 HOH C2034
SITE 1 HC7 4 ARG C 223 LYS C 227 GLU C 285 FMT C 573
SITE 1 HC8 4 TRP C 134 ASN C 135 LEU C 251 LYS C 252
SITE 1 HC9 6 THR C 420 ILE C 422 ASN C 423 HOH C1802
SITE 2 HC9 6 HOH C1897 HOH C2008
SITE 1 IC1 4 ASN C 415 HOH C1762 HOH C1779 HOH C2034
SITE 1 IC2 3 THR C 208 FMT C 571 HOH C2021
SITE 1 IC3 2 THR C 208 FMT C 570
SITE 1 IC4 4 PRO C 62 HIS C 170 LYS C 400 PHE C 402
SITE 1 IC5 3 ARG C 223 GLU C 285 FMT C 566
SITE 1 IC6 8 ASP A 91 HOH A1677 TYR C 321 PHE C 322
SITE 2 IC6 8 VAL C 350 HIS C 351 HOH C1875 HOH C2068
SITE 1 IC7 8 HIS C 179 ASP C 181 ARG C 182 SER C 183
SITE 2 IC7 8 ALA C 184 THR C 187 LEU C 204 TYR C 205
SITE 1 IC8 5 ASP C 181 ARG C 182 ARG C 207 GLN C 221
SITE 2 IC8 5 HOH C1981
SITE 1 IC9 3 LYS C 266 LEU C 396 GLY C 397
SITE 1 JC1 7 ILE C 239 GLY C 242 LYS C 243 MET C 255
SITE 2 JC1 7 GLU C 256 LYS C 259 HOH C1773
SITE 1 JC2 7 GLN A 211 PRO C 57 ASN C 60 ASN C 378
SITE 2 JC2 7 ILE C 381 ASP C 382 HOH C1817
SITE 1 JC3 5 LYS C 386 HOH C1456 HOH C1813 HOH C1949
SITE 2 JC3 5 HOH C2050
SITE 1 JC4 4 ARG A 92 FMT A 546 ASN C 421 ASN C 423
SITE 1 JC5 8 LYS A 55 FMT A 556 PHE C 300 LYS C 330
SITE 2 JC5 8 HOH C1857 HOH C1889 HOH C1909 HOH C1921
SITE 1 JC6 4 ARG C 309 HOH C1947 HOH C2063 HOH C2074
SITE 1 JC7 6 THR A 215 PHE A 300 THR C 54 LYS C 55
SITE 2 JC7 6 HOH C2016 HOH C2032
SITE 1 JC8 8 ASN C 318 SER C 319 GLU C 320 GLN C 323
SITE 2 JC8 8 THR C 345 THR C 420 ASN C 421 ILE C 422
CRYST1 76.984 133.322 253.855 90.00 90.00 90.00 C 2 2 21 24
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 0.012990 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003939 0.00000
TER 3113 THR A 425
TER 6239 THR B 425
TER 9354 THR C 425
MASTER 691 0 89 42 42 0 148 610717 3 297 90
END |