HEADER TRANSFERASE 28-SEP-16 5LYH
TITLE HUMAN PARP14 (ARTD8), CATALYTIC FRAGMENT IN COMPLEX WITH INHIBITOR H10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 14;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PARP-14,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 8,
COMPND 5 ARTD8,B AGGRESSIVE LYMPHOMA PROTEIN 2;
COMPND 6 EC: 2.4.2.30;
COMPND 7 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: PARP14, BAL2, KIAA1268;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS ADP-RIBOSYLATION, INHIBITOR COMPLEX, TRANSFERASE DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KARLBERG,A.G.THORSELL,H.SCHULER
REVDAT 4 17-JAN-24 5LYH 1 REMARK
REVDAT 3 24-JAN-18 5LYH 1 SOURCE REMARK
REVDAT 2 11-JAN-17 5LYH 1 JRNL
REVDAT 1 21-DEC-16 5LYH 0
JRNL AUTH B.PENG,A.G.THORSELL,T.KARLBERG,H.SCHULER,S.Q.YAO
JRNL TITL SMALL MOLECULE MICROARRAY BASED DISCOVERY OF PARP14
JRNL TITL 2 INHIBITORS.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 248 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 27918638
JRNL DOI 10.1002/ANIE.201609655
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 24403
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.22
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1711
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.4320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2987
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -31.74000
REMARK 3 B22 (A**2) : -31.74000
REMARK 3 B33 (A**2) : 63.49000
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): 0.046
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.036
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.206
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
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): 3161 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2833 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4297 ; 1.751 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6498 ; 1.271 ; 3.007
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 365 ; 7.753 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 168 ;33.279 ;24.226
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 481 ;16.829 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;23.782 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 435 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3664 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 824 ; 0.005 ; 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): 1466 ; 5.162 ; 5.944
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1465 ; 5.157 ; 5.943
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1826 ; 7.377 ; 8.902
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1827 ; 7.375 ; 8.903
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1692 ; 4.945 ; 6.366
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1693 ; 4.944 ; 6.364
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2469 ; 7.341 ; 9.433
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3404 ;10.628 ;47.368
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3404 ;10.627 ;47.365
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1613 1801 B 1613 1801 20500 0.10 0.05
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.658
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.342
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5LYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001597.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26408
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 46.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : 1.13000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 4F1L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG3350, 0.225M SODIUM MALONATE,
REMARK 280 PH 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.69333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.38667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.38667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.69333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 1609
REMARK 465 MET A 1610
REMARK 465 ASP A 1611
REMARK 465 TYR A 1701
REMARK 465 ALA A 1702
REMARK 465 GLY A 1703
REMARK 465 LYS A 1704
REMARK 465 ASN A 1705
REMARK 465 SER B 1609
REMARK 465 MET B 1610
REMARK 465 ASP B 1611
REMARK 465 MET B 1612
REMARK 465 ALA B 1702
REMARK 465 GLY B 1703
REMARK 465 LYS B 1704
REMARK 465 ASN B 1705
REMARK 465 ALA B 1706
REMARK 465 VAL B 1707
REMARK 465 ALA B 1708
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 LYS A1613 145.55 84.51
REMARK 500 ASN A1698 137.75 -3.56
REMARK 500 LYS A1711 72.73 -102.39
REMARK 500 TYR A1727 -65.95 -103.97
REMARK 500 PRO A1793 69.09 -69.87
REMARK 500 GLN B1614 -49.06 81.20
REMARK 500 GLN B1614 -47.64 80.47
REMARK 500 ASN B1698 -168.05 -71.60
REMARK 500 ARG B1699 -105.76 54.93
REMARK 500 LYS B1711 70.46 -102.61
REMARK 500 TYR B1727 -66.03 -104.31
REMARK 500 ASN B1752 -94.89 -130.25
REMARK 500 HIS B1753 -43.58 168.99
REMARK 500 ASN B1776 108.56 -160.49
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 MET A 1612 LYS A 1613 -136.10
REMARK 500 ARG B 1699 SER B 1700 -30.41
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 7B8 A 1901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7B8 B 1901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5LXP RELATED DB: PDB
REMARK 900 5LXP CONTAINS THE SAME PROTEIN COMPLEXED WITH INHIBITOR H5
DBREF 5LYH A 1611 1801 UNP Q460N5 PAR14_HUMAN 1530 1720
DBREF 5LYH B 1611 1801 UNP Q460N5 PAR14_HUMAN 1530 1720
SEQADV 5LYH SER A 1609 UNP Q460N5 EXPRESSION TAG
SEQADV 5LYH MET A 1610 UNP Q460N5 EXPRESSION TAG
SEQADV 5LYH SER B 1609 UNP Q460N5 EXPRESSION TAG
SEQADV 5LYH MET B 1610 UNP Q460N5 EXPRESSION TAG
SEQRES 1 A 193 SER MET ASP MET LYS GLN GLN ASN PHE CYS VAL VAL GLU
SEQRES 2 A 193 LEU LEU PRO SER ASP PRO GLU TYR ASN THR VAL ALA SER
SEQRES 3 A 193 LYS PHE ASN GLN THR CYS SER HIS PHE ARG ILE GLU LYS
SEQRES 4 A 193 ILE GLU ARG ILE GLN ASN PRO ASP LEU TRP ASN SER TYR
SEQRES 5 A 193 GLN ALA LYS LYS LYS THR MET ASP ALA LYS ASN GLY GLN
SEQRES 6 A 193 THR MET ASN GLU LYS GLN LEU PHE HIS GLY THR ASP ALA
SEQRES 7 A 193 GLY SER VAL PRO HIS VAL ASN ARG ASN GLY PHE ASN ARG
SEQRES 8 A 193 SER TYR ALA GLY LYS ASN ALA VAL ALA TYR GLY LYS GLY
SEQRES 9 A 193 THR TYR PHE ALA VAL ASN ALA ASN TYR SER ALA ASN ASP
SEQRES 10 A 193 THR TYR SER ARG PRO ASP ALA ASN GLY ARG LYS HIS VAL
SEQRES 11 A 193 TYR TYR VAL ARG VAL LEU THR GLY ILE TYR THR HIS GLY
SEQRES 12 A 193 ASN HIS SER LEU ILE VAL PRO PRO SER LYS ASN PRO GLN
SEQRES 13 A 193 ASN PRO THR ASP LEU TYR ASP THR VAL THR ASP ASN VAL
SEQRES 14 A 193 HIS HIS PRO SER LEU PHE VAL ALA PHE TYR ASP TYR GLN
SEQRES 15 A 193 ALA TYR PRO GLU TYR LEU ILE THR PHE ARG LYS
SEQRES 1 B 193 SER MET ASP MET LYS GLN GLN ASN PHE CYS VAL VAL GLU
SEQRES 2 B 193 LEU LEU PRO SER ASP PRO GLU TYR ASN THR VAL ALA SER
SEQRES 3 B 193 LYS PHE ASN GLN THR CYS SER HIS PHE ARG ILE GLU LYS
SEQRES 4 B 193 ILE GLU ARG ILE GLN ASN PRO ASP LEU TRP ASN SER TYR
SEQRES 5 B 193 GLN ALA LYS LYS LYS THR MET ASP ALA LYS ASN GLY GLN
SEQRES 6 B 193 THR MET ASN GLU LYS GLN LEU PHE HIS GLY THR ASP ALA
SEQRES 7 B 193 GLY SER VAL PRO HIS VAL ASN ARG ASN GLY PHE ASN ARG
SEQRES 8 B 193 SER TYR ALA GLY LYS ASN ALA VAL ALA TYR GLY LYS GLY
SEQRES 9 B 193 THR TYR PHE ALA VAL ASN ALA ASN TYR SER ALA ASN ASP
SEQRES 10 B 193 THR TYR SER ARG PRO ASP ALA ASN GLY ARG LYS HIS VAL
SEQRES 11 B 193 TYR TYR VAL ARG VAL LEU THR GLY ILE TYR THR HIS GLY
SEQRES 12 B 193 ASN HIS SER LEU ILE VAL PRO PRO SER LYS ASN PRO GLN
SEQRES 13 B 193 ASN PRO THR ASP LEU TYR ASP THR VAL THR ASP ASN VAL
SEQRES 14 B 193 HIS HIS PRO SER LEU PHE VAL ALA PHE TYR ASP TYR GLN
SEQRES 15 B 193 ALA TYR PRO GLU TYR LEU ILE THR PHE ARG LYS
HET 7B8 A1901 39
HET 7B8 B1901 39
HETNAM 7B8 3-[2-[4-[2-[[4-[(3-AMINOCARBONYLPHENYL)AMINO]-4-
HETNAM 2 7B8 OXIDANYLIDENE-BUTANOYL]AMINO]ETHYL]-1,2,3-TRIAZOL-1-
HETNAM 3 7B8 YL]ETHYLSULFAMOYL]BENZOIC ACID
FORMUL 3 7B8 2(C24 H27 N7 O7 S)
FORMUL 5 HOH *19(H2 O)
HELIX 1 AA1 ASP A 1626 SER A 1641 1 16
HELIX 2 AA2 ASN A 1653 GLY A 1672 1 20
HELIX 3 AA3 SER A 1688 GLY A 1696 1 9
HELIX 4 AA4 ASN A 1718 ASN A 1724 1 7
HELIX 5 AA5 ASP B 1626 SER B 1641 1 16
HELIX 6 AA6 ASN B 1653 GLY B 1672 1 20
HELIX 7 AA7 SER B 1688 GLY B 1696 1 9
HELIX 8 AA8 ASN B 1718 ASN B 1724 1 7
SHEET 1 AA1 5 CYS A1618 GLU A1621 0
SHEET 2 AA1 5 ARG A1644 GLN A1652 -1 O ARG A1650 N VAL A1620
SHEET 3 AA1 5 ALA A1791 ARG A1800 -1 O ARG A1800 N ARG A1644
SHEET 4 AA1 5 LYS A1736 LEU A1744 -1 N VAL A1738 O ILE A1797
SHEET 5 AA1 5 GLU A1677 THR A1684 -1 N LEU A1680 O VAL A1741
SHEET 1 AA2 4 THR A1713 ALA A1716 0
SHEET 2 AA2 4 LEU A1782 ALA A1785 -1 O ALA A1785 N THR A1713
SHEET 3 AA2 4 THR A1772 THR A1774 -1 N VAL A1773 O VAL A1784
SHEET 4 AA2 4 TYR A1748 HIS A1750 1 N THR A1749 O THR A1774
SHEET 1 AA3 5 CYS B1618 GLU B1621 0
SHEET 2 AA3 5 ARG B1644 GLN B1652 -1 O GLN B1652 N CYS B1618
SHEET 3 AA3 5 ALA B1791 ARG B1800 -1 O GLU B1794 N ILE B1651
SHEET 4 AA3 5 LYS B1736 LEU B1744 -1 N VAL B1738 O ILE B1797
SHEET 5 AA3 5 GLU B1677 THR B1684 -1 N LEU B1680 O VAL B1741
SHEET 1 AA4 4 THR B1713 ALA B1716 0
SHEET 2 AA4 4 LEU B1782 ALA B1785 -1 O ALA B1785 N THR B1713
SHEET 3 AA4 4 THR B1772 THR B1774 -1 N VAL B1773 O VAL B1784
SHEET 4 AA4 4 TYR B1748 THR B1749 1 N THR B1749 O THR B1774
SSBOND 1 CYS A 1618 CYS A 1618 1555 6765 2.19
SSBOND 2 CYS B 1618 CYS B 1618 1555 6765 2.07
SITE 1 AC1 18 HIS A1682 GLY A1683 THR A1684 SER A1688
SITE 2 AC1 18 HIS A1691 PHE A1697 ASN A1698 SER A1700
SITE 3 AC1 18 VAL A1707 GLY A1712 THR A1713 TYR A1714
SITE 4 AC1 18 PHE A1715 ALA A1716 TYR A1721 SER A1722
SITE 5 AC1 18 TYR A1727 ASN B1724
SITE 1 AC2 15 ASN A1724 HOH A2007 HIS B1682 GLY B1683
SITE 2 AC2 15 THR B1684 SER B1688 HIS B1691 VAL B1692
SITE 3 AC2 15 SER B1700 GLY B1712 TYR B1714 TYR B1721
SITE 4 AC2 15 SER B1722 TYR B1727 HOH B2002
CRYST1 83.032 83.032 122.080 90.00 90.00 120.00 P 31 2 1 12
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 0.012044 0.006953 0.000000 0.00000
SCALE2 0.000000 0.013907 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008191 0.00000
(ATOM LINES ARE NOT SHOWN.)
END