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HEADER LUMINESCENT PROTEIN 21-MAY-21 7OMD
TITLE CRYSTAL STRUCTURE OF AZACOELENTERAZINE-BOUND RENILLA RENIFORMIS
TITLE 2 LUCIFERASE VARIANT RLUC8-D162A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COELENTERAZINE H 2-MONOOXYGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RENILLA-LUCIFERIN 2-MONOOXYGENASE,RENILLA-TYPE LUCIFERASE;
COMPND 5 EC: 1.13.12.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;
SOURCE 3 ORGANISM_COMMON: SEA PANSY;
SOURCE 4 ORGANISM_TAXID: 6136;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOLUMINSCENCE, LUMINESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHENKMAYEROVA,Y.L.JANIN,M.MAREK
REVDAT 1 01-JUN-22 7OMD 0
JRNL AUTH A.SCHENKMAYEROVA,M.MAREK,Y.JANIN
JRNL TITL STRUCTURAL AND CHEMICAL BASIS OF THE RENILLA-TYPE
JRNL TITL 2 BIOLUMINESCENCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14-3260-000
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 86694
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 4464
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.4010 - 4.9712 1.00 2828 145 0.1587 0.1739
REMARK 3 2 4.9712 - 3.9471 0.99 2791 117 0.1356 0.1682
REMARK 3 3 3.9471 - 3.4485 1.00 2783 120 0.1568 0.1626
REMARK 3 4 3.4485 - 3.1334 1.00 2788 140 0.1595 0.1882
REMARK 3 5 3.1334 - 2.9089 1.00 2722 163 0.1677 0.1885
REMARK 3 6 2.9089 - 2.7374 1.00 2720 181 0.1718 0.2103
REMARK 3 7 2.7374 - 2.6004 1.00 2714 173 0.1700 0.2334
REMARK 3 8 2.6004 - 2.4872 1.00 2780 141 0.1746 0.2196
REMARK 3 9 2.4872 - 2.3915 1.00 2786 113 0.1736 0.1980
REMARK 3 10 2.3915 - 2.3089 1.00 2757 140 0.1716 0.2170
REMARK 3 11 2.3089 - 2.2368 1.00 2720 133 0.1931 0.2292
REMARK 3 12 2.2368 - 2.1728 1.00 2768 149 0.1916 0.2270
REMARK 3 13 2.1728 - 2.1156 1.00 2720 151 0.1803 0.2360
REMARK 3 14 2.1156 - 2.0640 1.00 2748 137 0.1834 0.2483
REMARK 3 15 2.0640 - 2.0171 1.00 2741 178 0.1886 0.2380
REMARK 3 16 2.0171 - 1.9742 1.00 2721 150 0.1952 0.2309
REMARK 3 17 1.9742 - 1.9347 1.00 2711 153 0.1976 0.2340
REMARK 3 18 1.9347 - 1.8982 1.00 2740 159 0.2386 0.2712
REMARK 3 19 1.8982 - 1.8643 1.00 2732 173 0.2322 0.2492
REMARK 3 20 1.8643 - 1.8327 1.00 2720 149 0.2085 0.2716
REMARK 3 21 1.8327 - 1.8031 1.00 2753 162 0.2041 0.2405
REMARK 3 22 1.8031 - 1.7754 1.00 2722 150 0.2136 0.2893
REMARK 3 23 1.7754 - 1.7493 1.00 2734 163 0.2123 0.2512
REMARK 3 24 1.7493 - 1.7246 1.00 2677 156 0.2101 0.2114
REMARK 3 25 1.7246 - 1.7013 1.00 2786 131 0.2187 0.2212
REMARK 3 26 1.7013 - 1.6792 1.00 2695 147 0.2238 0.2877
REMARK 3 27 1.6792 - 1.6582 1.00 2769 147 0.2425 0.2763
REMARK 3 28 1.6582 - 1.6382 1.00 2731 164 0.2607 0.2835
REMARK 3 29 1.6382 - 1.6192 1.00 2721 137 0.2749 0.3619
REMARK 3 30 1.6192 - 1.6010 0.96 2652 142 0.3090 0.3476
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 2:310 OR RESID 401:403 OR
REMARK 3 RESID 501:854 ) ) OR ( CHAIN B AND ( RESID 404:404
REMARK 3 OR RESID 2:311 OR RESID 401:403 OR RESID 501:836 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.925 -5.640 18.453
REMARK 3 T TENSOR
REMARK 3 T11: 0.0886 T22: 0.1681
REMARK 3 T33: 0.1201 T12: -0.0438
REMARK 3 T13: -0.0253 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.4112 L22: 2.0175
REMARK 3 L33: 0.6080 L12: -0.5161
REMARK 3 L13: -0.0302 L23: -0.2460
REMARK 3 S TENSOR
REMARK 3 S11: 0.0156 S12: -0.0253 S13: -0.0637
REMARK 3 S21: 0.0226 S22: 0.0478 S23: 0.1368
REMARK 3 S31: 0.0321 S32: 0.0090 S33: -0.0470
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7OMD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1292116012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86744
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 43.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 1.05700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: 2PSJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, BIS-TRIS, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.5K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 42.02850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 MET A 1
REMARK 465 GLN A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 MET B 1
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
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 LEU A 30 -127.46 57.31
REMARK 500 SER A 32 -147.35 -149.16
REMARK 500 GLU A 40 -46.87 71.43
REMARK 500 ALA A 54 -17.21 77.20
REMARK 500 THR A 55 -163.86 -114.16
REMARK 500 ASP A 120 -133.05 57.91
REMARK 500 LYS A 227 91.61 -65.62
REMARK 500 SER A 257 -162.91 -119.82
REMARK 500 LEU A 284 -150.79 -110.58
REMARK 500 ALA A 291 51.90 -140.16
REMARK 500 LEU B 30 -123.37 49.60
REMARK 500 SER B 32 -145.10 -134.82
REMARK 500 GLU B 40 -52.41 71.92
REMARK 500 ALA B 54 -19.44 77.74
REMARK 500 THR B 55 -164.81 -114.31
REMARK 500 ASP B 120 -139.06 63.85
REMARK 500 SER B 257 -164.06 -110.19
REMARK 500 SER B 257 -163.72 -109.32
REMARK 500 LEU B 284 -147.75 -106.61
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 A 853 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 854 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH B 835 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B 836 DISTANCE = 6.69 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VK8 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VK8 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VK8 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VK8 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404
DBREF 7OMD A 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 7OMD B 1 311 UNP P27652 LUCI_RENRE 1 311
SEQADV 7OMD THR A 55 UNP P27652 ALA 55 CONFLICT
SEQADV 7OMD ALA A 124 UNP P27652 CYS 124 CONFLICT
SEQADV 7OMD ALA A 130 UNP P27652 SER 130 CONFLICT
SEQADV 7OMD ARG A 136 UNP P27652 LYS 136 CONFLICT
SEQADV 7OMD MET A 143 UNP P27652 ALA 143 CONFLICT
SEQADV 7OMD ALA A 162 UNP P27652 ASP 162 ENGINEERED MUTATION
SEQADV 7OMD VAL A 185 UNP P27652 MET 185 CONFLICT
SEQADV 7OMD LEU A 253 UNP P27652 MET 253 CONFLICT
SEQADV 7OMD LEU A 287 UNP P27652 SER 287 CONFLICT
SEQADV 7OMD HIS A 312 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS A 313 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS A 314 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS A 315 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS A 316 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS A 317 UNP P27652 EXPRESSION TAG
SEQADV 7OMD THR B 55 UNP P27652 ALA 55 CONFLICT
SEQADV 7OMD ALA B 124 UNP P27652 CYS 124 CONFLICT
SEQADV 7OMD ALA B 130 UNP P27652 SER 130 CONFLICT
SEQADV 7OMD ARG B 136 UNP P27652 LYS 136 CONFLICT
SEQADV 7OMD MET B 143 UNP P27652 ALA 143 CONFLICT
SEQADV 7OMD ALA B 162 UNP P27652 ASP 162 ENGINEERED MUTATION
SEQADV 7OMD VAL B 185 UNP P27652 MET 185 CONFLICT
SEQADV 7OMD LEU B 253 UNP P27652 MET 253 CONFLICT
SEQADV 7OMD LEU B 287 UNP P27652 SER 287 CONFLICT
SEQADV 7OMD HIS B 312 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS B 313 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS B 314 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS B 315 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS B 316 UNP P27652 EXPRESSION TAG
SEQADV 7OMD HIS B 317 UNP P27652 EXPRESSION TAG
SEQRES 1 A 317 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 A 317 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 A 317 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 A 317 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 A 317 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 A 317 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 A 317 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 A 317 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 A 317 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 A 317 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 A 317 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 A 317 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 A 317 PRO ASP ILE GLU GLU ALA ILE ALA LEU ILE LYS SER GLU
SEQRES 14 A 317 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 A 317 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 A 317 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 A 317 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 A 317 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 A 317 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 A 317 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 A 317 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 A 317 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 A 317 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 A 317 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN HIS
SEQRES 25 A 317 HIS HIS HIS HIS HIS
SEQRES 1 B 317 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 B 317 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 B 317 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 B 317 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 B 317 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 B 317 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 B 317 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 B 317 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 B 317 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 B 317 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 B 317 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 B 317 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 B 317 PRO ASP ILE GLU GLU ALA ILE ALA LEU ILE LYS SER GLU
SEQRES 14 B 317 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 B 317 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 B 317 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 B 317 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 B 317 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 B 317 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 B 317 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 B 317 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 B 317 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 B 317 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 B 317 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN HIS
SEQRES 25 B 317 HIS HIS HIS HIS HIS
HET VK8 A 401 32
HET DMS A 402 4
HET PEG A 403 7
HET VK8 B 401 32
HET VK8 B 402 32
HET VK8 B 403 32
HET CL B 404 1
HETNAM VK8 6-(4-HYDROXYPHENYL)-2-[(4-HYDROXYPHENYL)METHYL]-8-
HETNAM 2 VK8 (PHENYLMETHYL)-[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-3-ONE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
FORMUL 3 VK8 4(C25 H20 N4 O3)
FORMUL 4 DMS C2 H6 O S
FORMUL 5 PEG C4 H10 O3
FORMUL 9 CL CL 1-
FORMUL 10 HOH *690(H2 O)
HELIX 1 AA1 GLN A 10 MET A 14 5 5
HELIX 2 AA2 THR A 16 ARG A 23 1 8
HELIX 3 AA3 SER A 56 ARG A 61 5 6
HELIX 4 AA4 VAL A 63 ILE A 67 5 5
HELIX 5 AA5 ARG A 93 LEU A 107 1 15
HELIX 6 AA6 ASP A 120 HIS A 133 1 14
HELIX 7 AA7 GLU A 151 GLU A 155 5 5
HELIX 8 AA8 ASP A 158 SER A 168 1 11
HELIX 9 AA9 SER A 168 GLU A 177 1 10
HELIX 10 AB1 ASN A 179 THR A 184 1 6
HELIX 11 AB2 THR A 184 LYS A 189 1 6
HELIX 12 AB3 GLU A 195 GLU A 204 1 10
HELIX 13 AB4 PRO A 205 LYS A 207 5 3
HELIX 14 AB5 GLY A 210 VAL A 212 5 3
HELIX 15 AB6 ARG A 213 GLU A 222 1 10
HELIX 16 AB7 LYS A 230 ALA A 246 1 17
HELIX 17 AB8 PHE A 262 LYS A 271 1 10
HELIX 18 AB9 PHE A 286 ASP A 290 5 5
HELIX 19 AC1 ALA A 291 GLU A 310 1 20
HELIX 20 AC2 GLN B 10 MET B 14 5 5
HELIX 21 AC3 THR B 16 ARG B 23 1 8
HELIX 22 AC4 SER B 56 ARG B 61 5 6
HELIX 23 AC5 VAL B 63 ILE B 67 5 5
HELIX 24 AC6 ARG B 93 GLU B 106 1 14
HELIX 25 AC7 ASP B 120 HIS B 133 1 14
HELIX 26 AC8 ASP B 158 SER B 168 1 11
HELIX 27 AC9 SER B 168 GLU B 177 1 10
HELIX 28 AD1 ASN B 179 THR B 184 1 6
HELIX 29 AD2 THR B 184 LYS B 189 1 6
HELIX 30 AD3 GLU B 195 GLU B 204 1 10
HELIX 31 AD4 PRO B 205 LYS B 207 5 3
HELIX 32 AD5 GLY B 210 VAL B 212 5 3
HELIX 33 AD6 ARG B 213 TRP B 219 1 7
HELIX 34 AD7 PRO B 220 ILE B 223 5 4
HELIX 35 AD8 LYS B 230 ALA B 246 1 17
HELIX 36 AD9 PHE B 262 LYS B 272 1 11
HELIX 37 AE1 PHE B 286 ASP B 290 5 5
HELIX 38 AE2 ALA B 291 GLU B 310 1 20
SHEET 1 AA1 8 LYS A 25 VAL A 29 0
SHEET 2 AA1 8 SER A 32 ASP A 38 -1 O TYR A 36 N LYS A 25
SHEET 3 AA1 8 ARG A 72 PRO A 76 -1 O ILE A 75 N TYR A 37
SHEET 4 AA1 8 ALA A 46 LEU A 50 1 N VAL A 47 O ARG A 72
SHEET 5 AA1 8 ILE A 114 HIS A 119 1 O VAL A 117 N LEU A 50
SHEET 6 AA1 8 ILE A 137 MET A 143 1 O VAL A 141 N PHE A 116
SHEET 7 AA1 8 LYS A 252 GLU A 256 1 O LEU A 253 N HIS A 142
SHEET 8 AA1 8 THR A 276 LYS A 280 1 O VAL A 279 N GLU A 256
SHEET 1 AA2 8 LYS B 25 VAL B 29 0
SHEET 2 AA2 8 SER B 32 ASP B 38 -1 O TYR B 36 N LYS B 25
SHEET 3 AA2 8 ARG B 72 PRO B 76 -1 O ILE B 75 N TYR B 37
SHEET 4 AA2 8 ALA B 46 LEU B 50 1 N VAL B 47 O ARG B 72
SHEET 5 AA2 8 ILE B 114 HIS B 119 1 O VAL B 117 N LEU B 50
SHEET 6 AA2 8 ILE B 137 MET B 143 1 O VAL B 141 N PHE B 116
SHEET 7 AA2 8 LYS B 252 GLU B 256 1 O LEU B 253 N HIS B 142
SHEET 8 AA2 8 THR B 276 LYS B 280 1 O VAL B 279 N GLU B 256
SITE 1 AC1 19 ASP A 158 GLU A 161 ALA A 162 ILE A 163
SITE 2 AC1 19 ILE A 166 PHE A 180 PHE A 181 VAL A 185
SITE 3 AC1 19 PRO A 220 PHE A 261 PHE A 262 HIS A 285
SITE 4 AC1 19 HOH A 539 HOH A 653 GLU B 161 VK8 B 401
SITE 5 AC1 19 VK8 B 402 VK8 B 403 HOH B 503
SITE 1 AC2 4 TRP A 121 PRO A 220 PHE A 262 HOH A 624
SITE 1 AC3 9 ASP A 148 VAL A 149 GLU A 151 ASP A 154
SITE 2 AC3 9 ARG A 238 ASN A 241 HOH A 505 HOH A 514
SITE 3 AC3 9 HOH A 571
SITE 1 AC4 15 LEU A 165 PHE A 180 THR A 184 VK8 A 401
SITE 2 AC4 15 LEU B 165 ILE B 166 MET B 174 PHE B 180
SITE 3 AC4 15 PHE B 181 VAL B 185 HIS B 285 VK8 B 402
SITE 4 AC4 15 VK8 B 403 HOH B 516 HOH B 556
SITE 1 AC5 13 VK8 A 401 HOH A 667 TRP B 121 ILE B 150
SITE 2 AC5 13 TRP B 156 ILE B 159 GLU B 161 ALA B 162
SITE 3 AC5 13 PRO B 220 VK8 B 401 VK8 B 403 CL B 404
SITE 4 AC5 13 HOH B 693
SITE 1 AC6 17 ASP A 158 VK8 A 401 ASP B 120 GLU B 144
SITE 2 AC6 17 SER B 145 VAL B 146 VAL B 147 ASP B 148
SITE 3 AC6 17 ILE B 150 ILE B 223 PRO B 224 PHE B 262
SITE 4 AC6 17 HIS B 285 VK8 B 401 VK8 B 402 HOH B 607
SITE 5 AC6 17 HOH B 688
SITE 1 AC7 3 ASN B 53 TRP B 121 VK8 B 402
CRYST1 51.569 84.057 77.437 90.00 90.72 90.00 P 1 21 1 4
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 0.019391 0.000000 0.000244 0.00000
SCALE2 0.000000 0.011897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012915 0.00000
TER 2564 GLU A 310
TER 5125 GLN B 311
MASTER 339 0 7 38 16 0 23 6 5897 2 139 50
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