HEADER HYDROLASE/HYDROLASE INHIBITOR 10-NOV-16 5PAB
TITLE CRYSTAL STRUCTURE OF FACTOR VIIA IN COMPLEX WITH 1-[[3-[2-HYDROXY-3-
TITLE 2 (1H-PYRROLO[3,2-C]PYRIDIN-2-YL)PHENYL]PHENYL]METHYL]-3-PHENYLUREA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR VII HEAVY CHAIN;
COMPND 3 CHAIN: H;
COMPND 4 SYNONYM: PROCONVERTIN,SERUM PROTHROMBIN CONVERSION ACCELERATOR,SPCA;
COMPND 5 EC: 3.4.21.21;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: COAGULATION FACTOR VII LIGHT CHAIN;
COMPND 9 CHAIN: L;
COMPND 10 SYNONYM: PROCONVERTIN,SERUM PROTHROMBIN CONVERSION ACCELERATOR,SPCA;
COMPND 11 EC: 3.4.21.21;
COMPND 12 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: F7;
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 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: F7;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS GLYCOPROTEIN, HYDROLASE, SERINE PROTEASE, PLASMA, BLOOD COAGULATION
KEYWDS 2 FACTOR, PROTEIN INHIBITOR COMPLEX, CALCIUM-BINDING, HYDROLASE-
KEYWDS 3 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.STIHLE,A.MAYWEG,S.ROEVER,M.G.RUDOLPH
REVDAT 4 03-APR-24 5PAB 1 REMARK
REVDAT 3 17-NOV-21 5PAB 1 REMARK
REVDAT 2 21-FEB-18 5PAB 1 REMARK
REVDAT 1 21-JUN-17 5PAB 0
JRNL AUTH A.MAYWEG,S.ROEVER,M.G.RUDOLPH
JRNL TITL CRYSTAL STRUCTURE OF A FACTOR VIIA COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 35332
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1864
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) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.04
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2416
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2346
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 71
REMARK 3 SOLVENT ATOMS : 288
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.61000
REMARK 3 B22 (A**2) : -0.61000
REMARK 3 B33 (A**2) : 1.23000
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): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.279
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2575 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2431 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3520 ; 1.718 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5602 ; 0.982 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 6.701 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;29.709 ;22.991
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 416 ;13.733 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;21.046 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 392 ; 0.261 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2898 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 607 ; 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): 1249 ; 1.999 ; 2.429
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1248 ; 1.999 ; 2.426
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1564 ; 3.215 ; 3.618
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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: MAIN-CHAIN H213-H215 IN 2
REMARK 3 CONFORMATIONS, WEAK DENSITY. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5PAB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1001400416.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54190
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37285
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.71600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: INHOUSE MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 MG/ML PROTEIN IN 20MM TRIS/HCL PH
REMARK 280 8.4, 5 MM BENZAMIDINE, 0.1 M NACL, 50 MM CACL2 MIXED 1+1 WITH 32-
REMARK 280 35% AMMONIUM SULPHATE, 2% PEG 4000, 0.1 M BICINE-NAOH PH 8.5, 15%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 58.09850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.60850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.60850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.04925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.60850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.60850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 87.14775
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.60850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.60850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.04925
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.60850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.60850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 87.14775
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 58.09850
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
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 H 628 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 LYS H 164
REMARK 465 VAL H 165
REMARK 465 GLY H 166
REMARK 465 ASP H 167
REMARK 465 SER H 168
REMARK 465 PRO H 169
REMARK 465 ARG L 144
REMARK 465 ASN L 145
REMARK 465 ALA L 146
REMARK 465 SER L 147
REMARK 465 LYS L 148
REMARK 465 PRO L 149
REMARK 465 GLN L 150
REMARK 465 GLY L 151
REMARK 465 ARG L 152
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 H 227 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG L 110 NE - CZ - NH1 ANGL. DEV. = 3.0 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 HIS H 59 -68.34 -146.96
REMARK 500 THR H 120 -53.41 -126.19
REMARK 500 SER H 211 -126.72 -104.50
REMARK 500 CYS H 216 92.91 168.92
REMARK 500 GLN L 100 -106.03 -123.19
REMARK 500 THR L 106 108.55 -56.64
REMARK 500 THR L 108 43.99 -91.53
REMARK 500 VAL L 125 -32.93 -130.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH H 638 DISTANCE = 6.01 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 306 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU H 58 OE1
REMARK 620 2 ASP H 60 O 82.7
REMARK 620 3 GLU H 63 O 130.5 76.0
REMARK 620 4 GLU H 68 OE2 112.6 161.3 85.6
REMARK 620 5 HOH H 432 O 77.6 93.7 60.2 79.9
REMARK 620 6 HOH H 564 O 102.0 81.1 117.7 104.9 174.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XD H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 202
DBREF 5PAB H 1 254 UNP P08709 FA7_HUMAN 213 466
DBREF 5PAB L 89 152 UNP P08709 FA7_HUMAN 149 212
SEQRES 1 H 254 ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO
SEQRES 2 H 254 TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS
SEQRES 3 H 254 GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA
SEQRES 4 H 254 ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU
SEQRES 5 H 254 ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP
SEQRES 6 H 254 GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE
SEQRES 7 H 254 PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE
SEQRES 8 H 254 ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP
SEQRES 9 H 254 HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER
SEQRES 10 H 254 GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER
SEQRES 11 H 254 GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU
SEQRES 12 H 254 GLU LEU MHO VAL LEU ASN VAL PRO ARG LEU MET THR GLN
SEQRES 13 H 254 ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO
SEQRES 14 H 254 ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP
SEQRES 15 H 254 GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO
SEQRES 16 H 254 HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY
SEQRES 17 H 254 ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS
SEQRES 18 H 254 PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP
SEQRES 19 H 254 LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL
SEQRES 20 H 254 LEU LEU ARG ALA PRO PHE PRO
SEQRES 1 L 64 LEU ILE CYS VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR
SEQRES 2 L 64 CYS SER ASP HIS THR GLY THR LYS ARG SER CYS ARG CYS
SEQRES 3 L 64 HIS GLU GLY TYR SER LEU LEU ALA ASP GLY VAL SER CYS
SEQRES 4 L 64 THR PRO THR VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE
SEQRES 5 L 64 LEU GLU LYS ARG ASN ALA SER LYS PRO GLN GLY ARG
MODRES 5PAB MHO H 146 MET MODIFIED RESIDUE
HET MHO H 146 9
HET 7XD H 301 33
HET CL H 302 1
HET GOL H 303 6
HET GOL H 304 6
HET GOL H 305 6
HET CA H 306 1
HET CL H 307 1
HET CL H 308 1
HET SO4 H 309 5
HET GOL L 201 6
HET SO4 L 202 5
HETNAM MHO S-OXYMETHIONINE
HETNAM 7XD 1-[[3-[2-OXIDANYL-3-(1~{H}-PYRROLO[3,2-C]PYRIDIN-2-YL)
HETNAM 2 7XD PHENYL]PHENYL]METHYL]-3-PHENYL-UREA
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MHO C5 H11 N O3 S
FORMUL 3 7XD C27 H22 N4 O2
FORMUL 4 CL 3(CL 1-)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 8 CA CA 2+
FORMUL 11 SO4 2(O4 S 2-)
FORMUL 14 HOH *288(H2 O)
HELIX 1 AA1 ALA H 39 ASP H 44 5 6
HELIX 2 AA2 ASN H 48 ARG H 50 5 3
HELIX 3 AA3 GLU H 113 THR H 120 1 8
HELIX 4 AA4 LEU H 121 VAL H 124 5 4
HELIX 5 AA5 MET H 154 SER H 162 1 9
HELIX 6 AA6 TYR H 231 ARG H 240 1 10
HELIX 7 AA7 ASN L 93 CYS L 98 5 6
HELIX 8 AA8 ILE L 138 LYS L 143 1 6
SHEET 1 AA1 8 LYS H 5 VAL H 6 0
SHEET 2 AA1 8 MHO H 146 LEU H 153 -1 O VAL H 147 N LYS H 5
SHEET 3 AA1 8 MET H 175 ALA H 178 -1 O CYS H 177 N LEU H 153
SHEET 4 AA1 8 GLY H 223 ARG H 227 -1 O TYR H 225 N PHE H 176
SHEET 5 AA1 8 THR H 203 VAL H 210 -1 N ILE H 209 O THR H 226
SHEET 6 AA1 8 PRO H 195 TYR H 200 -1 N TYR H 200 O THR H 203
SHEET 7 AA1 8 PHE H 126 GLY H 131 -1 N LEU H 128 O ALA H 197
SHEET 8 AA1 8 MHO H 146 LEU H 153 -1 O VAL H 150 N SER H 127
SHEET 1 AA2 8 LEU H 248 ALA H 251 0
SHEET 2 AA2 8 GLN H 69 PRO H 79 1 N VAL H 76 O LEU H 249
SHEET 3 AA2 8 ALA H 92 LEU H 96 -1 O LEU H 93 N ILE H 77
SHEET 4 AA2 8 TRP H 35 SER H 38 -1 N VAL H 36 O LEU H 94
SHEET 5 AA2 8 ALA H 23 ASN H 32 -1 N THR H 29 O VAL H 37
SHEET 6 AA2 8 GLN H 15 VAL H 20 -1 N LEU H 18 O CYS H 26
SHEET 7 AA2 8 LEU H 52 LEU H 56 -1 O ILE H 53 N LEU H 19
SHEET 8 AA2 8 GLN H 69 PRO H 79 -1 O GLN H 69 N LEU H 56
SHEET 1 AA3 2 TYR L 101 HIS L 105 0
SHEET 2 AA3 2 LYS L 109 ARG L 113 -1 O SER L 111 N SER L 103
SHEET 1 AA4 2 TYR L 118 LEU L 120 0
SHEET 2 AA4 2 CYS L 127 PRO L 129 -1 O THR L 128 N SER L 119
SSBOND 1 CYS H 7 CYS H 12 1555 1555 2.07
SSBOND 2 CYS H 26 CYS H 42 1555 1555 2.04
SSBOND 3 CYS H 110 CYS L 135 1555 1555 2.03
SSBOND 4 CYS H 158 CYS H 177 1555 1555 2.09
SSBOND 5 CYS H 188 CYS H 216 1555 1555 2.07
SSBOND 6 CYS L 91 CYS L 102 1555 1555 2.06
SSBOND 7 CYS L 98 CYS L 112 1555 1555 2.03
SSBOND 8 CYS L 114 CYS L 127 1555 1555 2.04
LINK C LEU H 145 N MHO H 146 1555 1555 1.33
LINK C MHO H 146 N VAL H 147 1555 1555 1.33
LINK OE1 GLU H 58 CA CA H 306 1555 1555 2.46
LINK O ASP H 60 CA CA H 306 1555 1555 2.73
LINK O GLU H 63 CA CA H 306 1555 1555 2.58
LINK OE2 GLU H 68 CA CA H 306 1555 1555 2.52
LINK CA CA H 306 O HOH H 432 1555 1555 2.89
LINK CA CA H 306 O HOH H 564 1555 1555 2.77
CISPEP 1 PHE H 253 PRO H 254 0 1.49
SITE 1 AC1 17 LEU H 25 HIS H 41 CYS H 42 ASP H 44
SITE 2 AC1 17 LYS H 45 GLY H 85 SER H 187 CYS H 188
SITE 3 AC1 17 LYS H 189 SER H 192 SER H 211 TRP H 212
SITE 4 AC1 17 GLY H 213 GLY H 215 GOL H 304 HOH H 415
SITE 5 AC1 17 HOH H 519
SITE 1 AC2 2 ARG H 72 HIS H 97
SITE 1 AC3 5 PHE H 43 ASP H 44 ARG H 138 HOH H 451
SITE 2 AC3 5 HOH H 475
SITE 1 AC4 8 GLN H 24 LEU H 25 LYS H 189 GLY H 190
SITE 2 AC4 8 7XD H 301 HOH H 407 HOH H 413 HOH H 415
SITE 1 AC5 1 HOH H 547
SITE 1 AC6 6 GLU H 58 ASP H 60 GLU H 63 GLU H 68
SITE 2 AC6 6 HOH H 432 HOH H 564
SITE 1 AC7 1 ARG H 240
SITE 1 AC8 2 GLU H 242 GOL L 201
SITE 1 AC9 5 MET H 154 THR H 155 ARG H 227 HOH H 409
SITE 2 AC9 5 HOH H 481
SITE 1 AD1 6 GLU H 242 CL H 308 CYS L 114 SER L 119
SITE 2 AD1 6 LEU L 120 HOH L 308
SITE 1 AD2 5 ARG H 119 CYS L 102 SER L 103 ASP L 104
SITE 2 AD2 5 HOH L 314
CRYST1 95.217 95.217 116.197 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010502 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010502 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008606 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
