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Chemical substance (4) PDB-CCD (4) Chemical reaction (1) KEGG ENZYME (1) Gene (1) KEGG GENES (1) Protein sequence (4) UniProt (1) SWISS-PROT (1) PDBSTR (2) DNA sequence (1) EMBL (1) Protein domain (11) InterPro (7) PROSITE (4) Literature (1) PubMed (1) All databases (23)
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HEADER HYDROLASE/HYDROLASE INHIBITOR 08-DEC-16 5U6J
TITLE FACTOR VIIA IN COMPLEX WITH THE INHIBITOR 3-{[(2R)-17-ETHYL-4-METHYL-
TITLE 2 3,12-DIOXO-7-[(PROPAN-2-YL)SULFONYL]-13-OXA-4,11-
TITLE 3 DIAZATRICYCLO[14.2.2.1~6,10~]HENICOSA-1(18),6(21),7,9,16,19-HEXAEN-2-
TITLE 4 YL]AMINO}BENZAMIDE
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: CRICETINAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10026;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: F7;
SOURCE 13 EXPRESSION_SYSTEM: CRICETINAE;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10026
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 A.WEI
REVDAT 4 04-OCT-23 5U6J 1 REMARK
REVDAT 3 07-JUN-17 5U6J 1 JRNL
REVDAT 2 17-MAY-17 5U6J 1 JRNL
REVDAT 1 10-MAY-17 5U6J 0
JRNL AUTH N.R.WURTZ,B.L.PARKHURST,I.DELUCCA,P.W.GLUNZ,W.JIANG,X.ZHANG,
JRNL AUTH 2 D.L.CHENEY,J.M.BOZARTH,A.R.RENDINA,A.WEI,T.HARPER,
JRNL AUTH 3 J.M.LUETTGEN,Y.WU,P.C.WONG,D.A.SEIFFERT,R.R.WEXLER,
JRNL AUTH 4 E.S.PRIESTLEY
JRNL TITL NEUTRAL MACROCYCLIC FACTOR VIIA INHIBITORS.
JRNL REF BIOORG. MED. CHEM. LETT. V. 27 2650 2017
JRNL REFN ESSN 1464-3405
JRNL PMID 28460818
JRNL DOI 10.1016/J.BMCL.2017.04.008
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 22985
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.860
REMARK 3 FREE R VALUE TEST SET COUNT : 2267
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.81
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2603
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2283
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2346
REMARK 3 BIN R VALUE (WORKING SET) : 0.2248
REMARK 3 BIN FREE R VALUE : 0.2586
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.87
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 257
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2347
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 219
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.91330
REMARK 3 B22 (A**2) : 2.91330
REMARK 3 B33 (A**2) : -5.82660
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.253
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.222
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.183
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.204
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.176
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2555 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3523 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 853 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 51 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 416 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2555 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 318 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : 6 ; 1.000 ; HARMONIC
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2960 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.70
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.22
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5U6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225408.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000 (DENZO), HKL
REMARK 200 -2000 (DENZO), HKL-2000 (DENZO)
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000 (SCALEPACK),
REMARK 200 HKL-2000 (SCALEPACK), HKL-2000
REMARK 200 (SCALEPACK)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24829
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1DAN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, PH 6.0, 20 MM CACL2,
REMARK 280 17.5%(W/V) PEG 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 58.83500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.71500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.71500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.41750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.71500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.71500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 88.25250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.71500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.71500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.41750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.71500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.71500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 88.25250
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 58.83500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
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 574 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 170D
REMARK 465 VAL H 170E
REMARK 465 GLY H 170F
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 H 84 NE CZ NH1 NH2
REMARK 470 GLN H 166 CG CD OE1 NE2
REMARK 470 GLN H 170 CD OE1 NE2
REMARK 470 ARG H 170C CG CD NE CZ NH1 NH2
REMARK 470 THR L 106 OG1 CG2
REMARK 470 LYS L 143 CG CD CE NZ
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 ASN H 48 -167.52 -164.89
REMARK 500 HIS H 71 -64.86 -142.11
REMARK 500 SER H 195 131.11 -39.35
REMARK 500 SER H 214 -71.56 -115.19
REMARK 500 GLN H 217 58.88 -100.41
REMARK 500 GLN L 100 -106.86 -123.00
REMARK 500 THR L 106 99.98 -60.15
REMARK 500 THR L 108 45.30 -96.62
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 H 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU H 70 OE1
REMARK 620 2 ASP H 72 O 81.2
REMARK 620 3 GLU H 75 O 160.9 85.5
REMARK 620 4 GLU H 80 OE1 101.1 170.6 94.2
REMARK 620 5 HOH H 445 O 85.0 102.1 84.4 87.2
REMARK 620 6 HOH H 493 O 82.5 86.2 110.4 85.1 163.7
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 82J H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 308
DBREF 5U6J H 16 257 UNP P08709 FA7_HUMAN 213 466
DBREF 5U6J L 90 144 UNP P08709 FA7_HUMAN 150 204
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 MET 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 55 ILE CYS VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS
SEQRES 2 L 55 SER ASP HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS
SEQRES 3 L 55 GLU GLY TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR
SEQRES 4 L 55 PRO THR VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU
SEQRES 5 L 55 GLU LYS ARG
HET 82J H 301 78
HET CA H 302 1
HET SO4 H 303 5
HET SO4 H 304 5
HET SO4 H 305 5
HET SO4 H 306 5
HET GOL H 307 6
HET GOL H 308 6
HETNAM 82J 3-{[(2R)-17-ETHYL-4-METHYL-3,12-DIOXO-7-[(PROPAN-2-YL)
HETNAM 2 82J SULFONYL]-13-OXA-4,11-DIAZATRICYCLO[14.2.2.1~6,
HETNAM 3 82J 10~]HENICOSA-1(18),6(21),7,9,16,19-HEXAEN-2-
HETNAM 4 82J YL]AMINO}BENZAMIDE
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 82J C31 H36 N4 O6 S
FORMUL 4 CA CA 2+
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 11 HOH *219(H2 O)
HELIX 1 AA1 ALA H 55 ASP H 60 5 6
HELIX 2 AA2 ASN H 60D ARG H 62 5 3
HELIX 3 AA3 GLU H 125 THR H 129C 1 8
HELIX 4 AA4 LEU H 129D VAL H 129G 5 4
HELIX 5 AA5 MET H 164 SER H 170B 1 9
HELIX 6 AA6 CYS H 191 SER H 195 5 5
HELIX 7 AA7 TYR H 234 ARG H 243 1 10
HELIX 8 AA8 ASN L 93 CYS L 98 5 6
HELIX 9 AA9 ILE L 138 LYS L 143 1 6
SHEET 1 AA1 7 LYS H 20 VAL H 21 0
SHEET 2 AA1 7 MET H 156 PRO H 161 -1 O VAL H 157 N LYS H 20
SHEET 3 AA1 7 PHE H 135 GLY H 140 -1 N SER H 136 O VAL H 160
SHEET 4 AA1 7 PRO H 198 TYR H 203 -1 O ALA H 200 N LEU H 137
SHEET 5 AA1 7 THR H 206 TRP H 215 -1 O THR H 206 N TYR H 203
SHEET 6 AA1 7 GLY H 226 ARG H 230 -1 O VAL H 227 N TRP H 215
SHEET 7 AA1 7 MET H 180 ALA H 183 -1 N PHE H 181 O TYR H 228
SHEET 1 AA2 8 LEU H 251 ALA H 254 0
SHEET 2 AA2 8 GLN H 81 PRO H 91 1 N VAL H 88 O LEU H 252
SHEET 3 AA2 8 ALA H 104 LEU H 108 -1 O LEU H 105 N ILE H 89
SHEET 4 AA2 8 TRP H 51 SER H 54 -1 N VAL H 52 O LEU H 106
SHEET 5 AA2 8 ALA H 39 LEU H 46 -1 N THR H 45 O VAL H 53
SHEET 6 AA2 8 GLN H 30 VAL H 35 -1 N LEU H 33 O CYS H 42
SHEET 7 AA2 8 LEU H 64 LEU H 68 -1 O ILE H 65 N LEU H 34
SHEET 8 AA2 8 GLN H 81 PRO H 91 -1 O ARG H 83 N ALA H 66
SHEET 1 AA3 2 TYR L 101 ASP L 104 0
SHEET 2 AA3 2 ARG L 110 ARG L 113 -1 O ARG L 113 N TYR L 101
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 22 CYS H 27 1555 1555 2.04
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.04
SSBOND 3 CYS H 122 CYS L 135 1555 1555 2.03
SSBOND 4 CYS H 168 CYS H 182 1555 1555 2.06
SSBOND 5 CYS H 191 CYS H 220 1555 1555 2.03
SSBOND 6 CYS L 91 CYS L 102 1555 1555 2.04
SSBOND 7 CYS L 98 CYS L 112 1555 1555 2.03
SSBOND 8 CYS L 114 CYS L 127 1555 1555 2.09
LINK OE1 GLU H 70 CA CA H 302 1555 1555 2.36
LINK O ASP H 72 CA CA H 302 1555 1555 2.28
LINK O GLU H 75 CA CA H 302 1555 1555 2.11
LINK OE1 GLU H 80 CA CA H 302 1555 1555 2.27
LINK CA CA H 302 O HOH H 445 1555 1555 2.34
LINK CA CA H 302 O HOH H 493 1555 1555 2.52
CISPEP 1 PHE H 256 PRO H 257 0 2.95
SITE 1 AC1 21 LEU H 41 HIS H 57 CYS H 58 ASP H 60
SITE 2 AC1 21 LYS H 60A GLY H 97 THR H 98 THR H 99
SITE 3 AC1 21 ASP H 102 ASP H 189 SER H 190 CYS H 191
SITE 4 AC1 21 LYS H 192 SER H 195 VAL H 213 SER H 214
SITE 5 AC1 21 TRP H 215 GLY H 216 GLY H 219 CYS H 220
SITE 6 AC1 21 HOH H 443
SITE 1 AC2 6 GLU H 70 ASP H 72 GLU H 75 GLU H 80
SITE 2 AC2 6 HOH H 445 HOH H 493
SITE 1 AC3 4 ARG H 83 ARG H 84 HIS H 109 GLN H 110
SITE 1 AC4 5 VAL H 35 ASN H 37 ILE H 60B LYS H 60C
SITE 2 AC4 5 ASN H 60D
SITE 1 AC5 6 CYS H 168 SER H 170B ILE H 176 HIS H 224
SITE 2 AC5 6 PHE H 225 VAL H 227
SITE 1 AC6 7 ILE H 47 ASN H 48 GLN H 239 MET H 242
SITE 2 AC6 7 HOH H 436 HOH H 447 HIS L 115
SITE 1 AC7 6 PHE H 59 ILE H 60B TRP H 61 ARG H 147
SITE 2 AC7 6 HOH H 402 HOH H 456
SITE 1 AC8 5 GLU H 26 CYS H 27 LEU H 137 HOH H 539
SITE 2 AC8 5 ILE L 138
CRYST1 95.430 95.430 117.670 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 0.010479 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008498 0.00000
(ATOM LINES ARE NOT SHOWN.)
END