HEADER HYDROLASE/HYDROLASE INHIBITOR 10-NOV-16 5PAS
TITLE CRYSTAL STRUCTURE OF FACTOR VIIA IN COMPLEX WITH (2S)-2-HYDROXY-N-[[3-
TITLE 2 [5-HYDROXY-4-(1H-PYRROLO[3,2-C]PYRIDIN-2-YL)PYRAZOL-1-
TITLE 3 YL]PHENYL]METHYL]-3-PHENYLPROPANAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR VII LIGHT CHAIN;
COMPND 3 CHAIN: A;
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 HEAVY CHAIN;
COMPND 9 CHAIN: C;
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 5PAS 1 REMARK
REVDAT 3 17-NOV-21 5PAS 1 LINK
REVDAT 2 21-FEB-18 5PAS 1 REMARK
REVDAT 1 21-JUN-17 5PAS 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. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
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) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 83985
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) : 0.200
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4440
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) : 1.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5932
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 289
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2376
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 381
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.92
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : 0.27000
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): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.058
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.075
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2626 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1792 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3594 ; 1.472 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4340 ; 2.628 ; 3.007
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 339 ; 6.008 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;26.980 ;22.743
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 425 ;14.918 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;18.020 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 388 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2953 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 536 ; 0.002 ; 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): 1590 ; 0.507 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 651 ; 0.060 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2587 ; 0.952 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1036 ; 1.090 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 995 ; 1.825 ; 4.500
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 : 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: THE NUMBERING FOLLOWS THAT OF THE
REMARK 3 UNPROCESSED PRECURSOR. UNUSUAL PLACEMENT OF TERMINAL ARYL GROUP
REMARK 3 IN S2 POCKET. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 5PAS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1001400429.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.984000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88673
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 39.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.940
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.490
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
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 58.42000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.51500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.51500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.21000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.51500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.51500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 87.63000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.51500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.51500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.21000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.51500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.51500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 87.63000
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 58.42000
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: A, 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 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 SER A 207
REMARK 465 LYS A 208
REMARK 465 PRO A 209
REMARK 465 GLN A 210
REMARK 465 GLY A 211
REMARK 465 ARG A 212
REMARK 465 LYS C 376
REMARK 465 VAL C 377
REMARK 465 GLY C 378
REMARK 465 ASP C 379
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 C 375 CG CD NE CZ NH1 NH2
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 O HOH A 420 O HOH A 430 2.03
REMARK 500 O HOH A 421 O HOH A 462 2.12
REMARK 500 O HOH A 430 O HOH C 736 2.16
REMARK 500 O HOH C 656 O HOH C 658 2.16
REMARK 500 O HOH C 747 O HOH C 859 2.18
REMARK 500 O HOH C 720 O HOH C 881 2.18
REMARK 500 O HOH C 758 O HOH C 832 2.19
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 160 -108.46 -123.10
REMARK 500 THR A 168 40.91 -87.39
REMARK 500 HIS C 271 -70.86 -143.87
REMARK 500 THR C 332 -58.78 -120.47
REMARK 500 SER C 423 -80.33 -122.20
REMARK 500
REMARK 500 REMARK: NULL
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 C 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 270 OE1
REMARK 620 2 ASP C 272 O 88.2
REMARK 620 3 GLU C 275 O 138.1 77.6
REMARK 620 4 GLU C 280 OE2 106.5 165.1 89.4
REMARK 620 5 HOH C 673 O 80.4 98.9 63.6 81.6
REMARK 620 6 HOH C 803 O 92.9 87.5 125.1 94.0 170.4
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7ZD C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 504
DBREF 5PAS A 149 212 UNP P08709 FA7_HUMAN 149 212
DBREF 5PAS C 213 466 UNP P08709 FA7_HUMAN 213 466
SEQRES 1 A 64 LEU ILE CYS VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR
SEQRES 2 A 64 CYS SER ASP HIS THR GLY THR LYS ARG SER CYS ARG CYS
SEQRES 3 A 64 HIS GLU GLY TYR SER LEU LEU ALA ASP GLY VAL SER CYS
SEQRES 4 A 64 THR PRO THR VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE
SEQRES 5 A 64 LEU GLU LYS ARG ASN ALA SER LYS PRO GLN GLY ARG
SEQRES 1 C 254 ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO
SEQRES 2 C 254 TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS
SEQRES 3 C 254 GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA
SEQRES 4 C 254 ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU
SEQRES 5 C 254 ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP
SEQRES 6 C 254 GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE
SEQRES 7 C 254 PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE
SEQRES 8 C 254 ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP
SEQRES 9 C 254 HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER
SEQRES 10 C 254 GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER
SEQRES 11 C 254 GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU
SEQRES 12 C 254 GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN
SEQRES 13 C 254 ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO
SEQRES 14 C 254 ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP
SEQRES 15 C 254 GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO
SEQRES 16 C 254 HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY
SEQRES 17 C 254 ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS
SEQRES 18 C 254 PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP
SEQRES 19 C 254 LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL
SEQRES 20 C 254 LEU LEU ARG ALA PRO PHE PRO
HET GOL A 301 12
HET GOL A 302 6
HET 7ZD C 501 34
HET CA C 502 1
HET CL C 503 1
HET SO4 C 504 5
HETNAM GOL GLYCEROL
HETNAM 7ZD (2S)-2-HYDROXY-N-[[3-[5-HYDROXY-4-(1H-PYRROLO[3,2-
HETNAM 2 7ZD C]PYRIDIN-2-YL)PYRAZOL-1-YL]PHENYL]METHYL]-3-
HETNAM 3 7ZD PHENYLPROPANAMIDE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 7ZD C26 H23 N5 O3
FORMUL 6 CA CA 2+
FORMUL 7 CL CL 1-
FORMUL 8 SO4 O4 S 2-
FORMUL 9 HOH *381(H2 O)
HELIX 1 AA1 ASN A 153 CYS A 158 5 6
HELIX 2 AA2 ILE A 198 ASN A 205 1 8
HELIX 3 AA3 ALA C 251 ASP C 256 5 6
HELIX 4 AA4 ASN C 260 ARG C 262 5 3
HELIX 5 AA5 GLU C 325 THR C 332 1 8
HELIX 6 AA6 LEU C 333 VAL C 336 5 4
HELIX 7 AA7 MET C 366 SER C 374 1 9
HELIX 8 AA8 TYR C 443 ARG C 452 1 10
SHEET 1 AA1 2 TYR A 161 HIS A 165 0
SHEET 2 AA1 2 LYS A 169 ARG A 173 -1 O SER A 171 N SER A 163
SHEET 1 AA2 2 TYR A 178 LEU A 180 0
SHEET 2 AA2 2 CYS A 187 PRO A 189 -1 O THR A 188 N SER A 179
SHEET 1 AA3 8 LYS C 217 VAL C 218 0
SHEET 2 AA3 8 MET C 358 LEU C 365 -1 O VAL C 359 N LYS C 217
SHEET 3 AA3 8 MET C 387 ALA C 390 -1 O CYS C 389 N LEU C 365
SHEET 4 AA3 8 GLY C 435 ARG C 439 -1 O TYR C 437 N PHE C 388
SHEET 5 AA3 8 THR C 415 TRP C 424 -1 N TRP C 424 O VAL C 436
SHEET 6 AA3 8 PRO C 407 TYR C 412 -1 N THR C 410 O TYR C 417
SHEET 7 AA3 8 PHE C 338 GLY C 343 -1 N LEU C 340 O ALA C 409
SHEET 8 AA3 8 MET C 358 LEU C 365 -1 O VAL C 362 N SER C 339
SHEET 1 AA4 8 LEU C 460 ALA C 463 0
SHEET 2 AA4 8 GLN C 281 PRO C 291 1 N VAL C 288 O LEU C 461
SHEET 3 AA4 8 ALA C 304 LEU C 308 -1 O LEU C 305 N ILE C 289
SHEET 4 AA4 8 TRP C 247 SER C 250 -1 N VAL C 248 O LEU C 306
SHEET 5 AA4 8 ALA C 235 LEU C 242 -1 N THR C 241 O VAL C 249
SHEET 6 AA4 8 GLN C 227 VAL C 232 -1 N LEU C 230 O CYS C 238
SHEET 7 AA4 8 LEU C 264 LEU C 268 -1 O ILE C 265 N LEU C 231
SHEET 8 AA4 8 GLN C 281 PRO C 291 -1 O ARG C 283 N ALA C 266
SSBOND 1 CYS A 151 CYS A 162 1555 1555 2.03
SSBOND 2 CYS A 158 CYS A 172 1555 1555 2.03
SSBOND 3 CYS A 174 CYS A 187 1555 1555 2.04
SSBOND 4 CYS A 195 CYS C 322 1555 1555 2.04
SSBOND 5 CYS C 219 CYS C 224 1555 1555 2.04
SSBOND 6 CYS C 238 CYS C 254 1555 1555 2.04
SSBOND 7 CYS C 370 CYS C 389 1555 1555 2.04
SSBOND 8 CYS C 400 CYS C 428 1555 1555 2.03
LINK ND1BHIS C 309 CL CL C 503 1555 1555 1.58
LINK OE1 GLU C 270 CA CA C 502 1555 1555 2.35
LINK O ASP C 272 CA CA C 502 1555 1555 2.51
LINK O GLU C 275 CA CA C 502 1555 1555 2.31
LINK OE2 GLU C 280 CA CA C 502 1555 1555 2.61
LINK CA CA C 502 O HOH C 673 1555 1555 2.80
LINK CA CA C 502 O HOH C 803 1555 1555 2.40
CISPEP 1 PHE C 465 PRO C 466 0 2.30
SITE 1 AC1 7 GLY A 196 LYS A 197 ILE A 198 LEU A 201
SITE 2 AC1 7 GLU A 202 GLY C 414 TRP C 416
SITE 1 AC2 8 ARG A 173 CYS A 174 SER A 179 LEU A 180
SITE 2 AC2 8 HOH A 409 HOH A 416 HOH A 431 HOH A 436
SITE 1 AC3 16 LEU C 237 CYS C 238 HIS C 253 ASP C 256
SITE 2 AC3 16 LYS C 257 TYR C 294 SER C 399 LYS C 401
SITE 3 AC3 16 SER C 404 SER C 423 GLY C 425 GLY C 427
SITE 4 AC3 16 HOH C 605 HOH C 624 HOH C 692 HOH C 745
SITE 1 AC4 6 GLU C 270 ASP C 272 GLU C 275 GLU C 280
SITE 2 AC4 6 HOH C 673 HOH C 803
SITE 1 AC5 2 ARG C 284 HIS C 309
SITE 1 AC6 7 MET C 366 THR C 367 ARG C 439 HOH C 651
SITE 2 AC6 7 HOH C 670 HOH C 679 HOH C 797
CRYST1 95.030 95.030 116.840 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 0.010523 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008559 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
