HEADER HYDROLASE/HYDROLASE INHIBITOR 14-NOV-14 4WXP
TITLE X-RAY CRYSTAL STRUCTURE OF NS3 HELICASE FROM HCV WITH A BOUND FRAGMENT
TITLE 2 INHIBITOR AT 2.08 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NS3-4 PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 180-630;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_TAXID: 11103;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HELICASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.DAVIES
REVDAT 2 27-SEP-23 4WXP 1 REMARK LINK
REVDAT 1 23-DEC-15 4WXP 0
JRNL AUTH B.O.BUCKMAN,K.KOSSEN,S.MISIALEK,S.STEVENS,R.RAJAGOPALAN,
JRNL AUTH 2 D.RUHMUND,L.HOOI,N.SNARSKAYA,V.SEREBRYANY,G.WANG,
JRNL AUTH 3 A.STOYCHEVA,J.B.NICHOLAS,D.R.DAVIES,S.BRUNTON,C.MONTALBETTI,
JRNL AUTH 4 D.WEDDELL,C.GOODWIN,D.SCHONFELD,O.MATHER,R.CHENG,L.BLATT,
JRNL AUTH 5 L.BEIGELMAN
JRNL TITL CRYSTAL STRUCTURE OF NS3 HELICASE FROM HCV WITH A BOUND
JRNL TITL 2 FRAGMENT INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1779)
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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 31227
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1574
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 34.5711 - 4.6213 0.98 2818 139 0.1455 0.1855
REMARK 3 2 4.6213 - 3.6694 0.99 2740 137 0.1400 0.1695
REMARK 3 3 3.6694 - 3.2059 1.00 2713 145 0.1775 0.2320
REMARK 3 4 3.2059 - 2.9130 1.00 2686 164 0.1976 0.2537
REMARK 3 5 2.9130 - 2.7043 1.00 2703 157 0.2068 0.2592
REMARK 3 6 2.7043 - 2.5449 1.00 2657 159 0.2123 0.2686
REMARK 3 7 2.5449 - 2.4175 1.00 2703 122 0.2226 0.3152
REMARK 3 8 2.4175 - 2.3122 1.00 2649 141 0.2120 0.2918
REMARK 3 9 2.3122 - 2.2232 1.00 2711 136 0.2167 0.3179
REMARK 3 10 2.2232 - 2.1465 1.00 2643 139 0.2373 0.2716
REMARK 3 11 2.1465 - 2.0800 0.98 2630 135 0.2749 0.3277
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 3397
REMARK 3 ANGLE : 1.127 4651
REMARK 3 CHIRALITY : 0.043 546
REMARK 3 PLANARITY : 0.006 599
REMARK 3 DIHEDRAL : 13.110 1190
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 186 THROUGH 322 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6455 -14.6450 25.7141
REMARK 3 T TENSOR
REMARK 3 T11: 0.2671 T22: 0.2118
REMARK 3 T33: 0.2054 T12: -0.0146
REMARK 3 T13: -0.0254 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 1.6567 L22: 2.0510
REMARK 3 L33: 2.2855 L12: 0.3242
REMARK 3 L13: -0.4192 L23: 0.0165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: -0.0423 S13: -0.1684
REMARK 3 S21: 0.2604 S22: -0.0139 S23: -0.1218
REMARK 3 S31: -0.1193 S32: 0.1870 S33: 0.0020
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 323 THROUGH 475 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0488 -13.5622 0.1192
REMARK 3 T TENSOR
REMARK 3 T11: 0.3192 T22: 0.3743
REMARK 3 T33: 0.6068 T12: 0.0087
REMARK 3 T13: -0.0183 T23: 0.1293
REMARK 3 L TENSOR
REMARK 3 L11: 1.7184 L22: 0.6734
REMARK 3 L33: 0.6187 L12: 1.9832
REMARK 3 L13: -0.6235 L23: 0.1511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: 0.3562 S13: 0.9022
REMARK 3 S21: -0.0671 S22: 0.1600 S23: 0.5187
REMARK 3 S31: -0.1077 S32: -0.1926 S33: -0.1350
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 476 THROUGH 630 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8789 2.9271 1.6718
REMARK 3 T TENSOR
REMARK 3 T11: 0.2390 T22: 0.2834
REMARK 3 T33: 0.2343 T12: -0.0363
REMARK 3 T13: 0.0237 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 0.8034 L22: 2.5649
REMARK 3 L33: 1.3586 L12: 0.1165
REMARK 3 L13: 0.1479 L23: -0.8032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0641 S12: 0.0638 S13: 0.1229
REMARK 3 S21: -0.0036 S22: 0.0153 S23: -0.0018
REMARK 3 S31: -0.1288 S32: 0.0028 S33: 0.0494
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 4WXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
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 : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31271
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.66900
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: MOLREP
REMARK 200 STARTING MODEL: 1HEI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS (PH 8.5), 0.8 M SODIUM
REMARK 280 CITRATE, 200 MM NACL, 2.5% PEG 4000, 20% EG CRYOPROTECTANT,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 289K, PH 8.50, VAPOR DIFFUSION,
REMARK 280 SITTING DROP
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 34.71100
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 69.42200
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 69.42200
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 34.71100
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: 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 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 A 811 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 ARG A 180
REMARK 465 SER A 181
REMARK 465 PRO A 182
REMARK 465 VAL A 183
REMARK 465 PHE A 184
REMARK 465 THR A 185
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 ASP A 186 CG OD1 OD2
REMARK 470 GLN A 195 CG CD OE1 NE2
REMARK 470 SER A 280 OG
REMARK 470 GLU A 357 CG CD OE1 OE2
REMARK 470 LYS A 371 CG CD CE NZ
REMARK 470 LYS A 372 CG CD CE NZ
REMARK 470 ARG A 393 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 545 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 552 CG CD OE1 NE2
REMARK 470 ASP A 555 CG OD1 OD2
REMARK 470 GLN A 580 CG CD OE1 NE2
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 OD2 ASP A 396 OG SER A 398 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NA NA A 701 NA NA A 701 4555 1.32
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 THR A 212 -71.52 -137.61
REMARK 500 SER A 342 -162.86 -109.20
REMARK 500 LYS A 352 -165.31 -117.10
REMARK 500 THR A 443 -91.10 -126.58
REMARK 500 ASP A 579 153.03 -48.56
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 GLU A 480 ARG A 481 145.81
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 NA A 701 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 387 OD1
REMARK 620 2 ASN A 387 OD1 0.0
REMARK 620 3 HOH A 802 O 96.7 96.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3VY A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WXR RELATED DB: PDB
DBREF 4WXP A 180 630 UNP K7XFN2 K7XFN2_9HEPC 180 630
SEQADV 4WXP SER A 196 UNP K7XFN2 THR 196 CONFLICT
SEQADV 4WXP ILE A 248 UNP K7XFN2 VAL 248 CONFLICT
SEQADV 4WXP ALA A 258 UNP K7XFN2 THR 258 CONFLICT
SEQADV 4WXP GLY A 263 UNP K7XFN2 ALA 263 CONFLICT
SEQADV 4WXP SER A 332 UNP K7XFN2 PRO 332 CONFLICT
SEQADV 4WXP VAL A 358 UNP K7XFN2 THR 358 CONFLICT
SEQADV 4WXP ARG A 360 UNP K7XFN2 LYS 360 CONFLICT
SEQADV 4WXP ALA A 383 UNP K7XFN2 GLY 383 CONFLICT
SEQADV 4WXP ASP A 447 UNP K7XFN2 GLU 447 CONFLICT
SEQADV 4WXP ARG A 470 UNP K7XFN2 GLY 470 CONFLICT
SEQADV 4WXP SER A 584 UNP K7XFN2 CYS 584 CONFLICT
SEQADV 4WXP THR A 586 UNP K7XFN2 ILE 586 CONFLICT
SEQADV 4WXP LEU A 593 UNP K7XFN2 HIS 593 CONFLICT
SEQADV 4WXP PRO A 595 UNP K7XFN2 SER 595 CONFLICT
SEQADV 4WXP LEU A 605 UNP K7XFN2 VAL 605 CONFLICT
SEQRES 1 A 451 ARG SER PRO VAL PHE THR ASP ASN SER SER PRO PRO ALA
SEQRES 2 A 451 VAL PRO GLN SER PHE GLN VAL ALA HIS LEU HIS ALA PRO
SEQRES 3 A 451 THR GLY SER GLY LYS SER THR LYS VAL PRO ALA ALA TYR
SEQRES 4 A 451 ALA ALA GLN GLY TYR LYS VAL LEU VAL LEU ASN PRO SER
SEQRES 5 A 451 VAL ALA ALA THR LEU GLY PHE GLY VAL TYR MET SER LYS
SEQRES 6 A 451 ALA HIS GLY ILE ASP PRO ASN ILE ARG THR GLY VAL ARG
SEQRES 7 A 451 ALA ILE THR THR GLY GLY PRO ILE THR TYR SER THR TYR
SEQRES 8 A 451 GLY LYS PHE LEU ALA ASP GLY GLY CYS SER GLY GLY ALA
SEQRES 9 A 451 TYR ASP ILE ILE ILE CYS ASP GLU CYS HIS SER THR ASP
SEQRES 10 A 451 SER THR SER ILE LEU GLY ILE GLY THR VAL LEU ASP GLN
SEQRES 11 A 451 ALA GLU THR ALA GLY ALA ARG LEU VAL VAL LEU ALA THR
SEQRES 12 A 451 ALA THR PRO PRO GLY SER VAL THR VAL SER HIS PRO ASN
SEQRES 13 A 451 ILE GLU GLU VAL ALA LEU SER ASN THR GLY GLU ILE PRO
SEQRES 14 A 451 PHE TYR GLY LYS ALA ILE PRO ILE GLU VAL ILE ARG GLY
SEQRES 15 A 451 GLY ARG HIS LEU ILE PHE CYS HIS SER LYS LYS LYS CYS
SEQRES 16 A 451 ASP GLU LEU ALA ALA LYS LEU SER ALA LEU GLY LEU ASN
SEQRES 17 A 451 ALA VAL ALA TYR TYR ARG GLY LEU ASP VAL SER VAL ILE
SEQRES 18 A 451 PRO THR SER GLY ASP VAL VAL VAL VAL ALA THR ASP ALA
SEQRES 19 A 451 LEU MET THR GLY TYR THR GLY ASP PHE ASP SER VAL ILE
SEQRES 20 A 451 ASP CYS ASN THR CYS VAL THR GLN THR VAL ASP PHE SER
SEQRES 21 A 451 LEU ASP PRO THR PHE THR ILE ASP THR THR THR VAL PRO
SEQRES 22 A 451 GLN ASP ALA VAL SER ARG SER GLN ARG ARG GLY ARG THR
SEQRES 23 A 451 GLY ARG GLY ARG ARG GLY ILE TYR ARG PHE VAL THR PRO
SEQRES 24 A 451 GLY GLU ARG PRO SER GLY MET PHE ASP SER SER VAL LEU
SEQRES 25 A 451 CYS GLU CYS TYR ASP ALA GLY CYS ALA TRP TYR GLU LEU
SEQRES 26 A 451 THR PRO ALA GLU THR SER VAL ARG LEU ARG ALA TYR LEU
SEQRES 27 A 451 ASN THR PRO GLY LEU PRO VAL CYS GLN ASP HIS LEU GLU
SEQRES 28 A 451 PHE TRP GLU SER VAL PHE THR GLY LEU THR HIS ILE ASP
SEQRES 29 A 451 ALA HIS PHE LEU SER GLN THR LYS GLN ALA GLY ASP ASN
SEQRES 30 A 451 PHE PRO TYR LEU VAL ALA TYR GLN ALA THR VAL CYS ALA
SEQRES 31 A 451 ARG ALA GLN ALA PRO PRO PRO SER TRP ASP GLN MET TRP
SEQRES 32 A 451 LYS SER LEU THR ARG LEU LYS PRO THR LEU LEU GLY PRO
SEQRES 33 A 451 THR PRO LEU LEU TYR ARG LEU GLY ALA LEU GLN ASN GLU
SEQRES 34 A 451 VAL THR LEU THR HIS PRO ILE THR LYS TYR ILE MET ALA
SEQRES 35 A 451 CYS MET SER ALA ASP LEU GLU VAL VAL
HET NA A 701 1
HET CL A 702 1
HET 3VY A 703 14
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM 3VY (1-METHYL-1H-INDOL-3-YL)ACETIC ACID
FORMUL 2 NA NA 1+
FORMUL 3 CL CL 1-
FORMUL 4 3VY C11 H11 N O2
FORMUL 5 HOH *117(H2 O)
HELIX 1 AA1 THR A 212 GLN A 221 1 10
HELIX 2 AA2 SER A 231 GLY A 247 1 17
HELIX 3 AA3 TYR A 270 ASP A 276 1 7
HELIX 4 AA4 ASP A 296 ALA A 310 1 15
HELIX 5 AA5 PRO A 355 ILE A 359 5 5
HELIX 6 AA6 SER A 370 LEU A 384 1 15
HELIX 7 AA7 ASP A 396 ILE A 400 5 5
HELIX 8 AA8 ASP A 412 THR A 416 5 5
HELIX 9 AA9 ASP A 454 GLY A 463 1 10
HELIX 10 AB1 ASP A 487 TRP A 501 1 15
HELIX 11 AB2 THR A 505 THR A 519 1 15
HELIX 12 AB3 HIS A 528 GLY A 538 1 11
HELIX 13 AB4 ASP A 543 GLY A 554 1 12
HELIX 14 AB5 PHE A 557 ALA A 571 1 15
HELIX 15 AB6 ASP A 579 THR A 586 5 8
HELIX 16 AB7 LEU A 588 LEU A 592 5 5
HELIX 17 AB8 HIS A 613 ALA A 625 1 13
SHEET 1 AA1 7 GLN A 198 HIS A 203 0
SHEET 2 AA1 7 LEU A 317 THR A 322 1 O LEU A 320 N ALA A 200
SHEET 3 AA1 7 ILE A 286 CYS A 289 1 N CYS A 289 O VAL A 319
SHEET 4 AA1 7 VAL A 225 ASN A 229 1 N LEU A 226 O ILE A 288
SHEET 5 AA1 7 ILE A 265 THR A 269 1 O THR A 266 N VAL A 227
SHEET 6 AA1 7 ASN A 251 ARG A 253 1 N ASN A 251 O TYR A 267
SHEET 7 AA1 7 ALA A 258 ILE A 259 -1 O ILE A 259 N ILE A 252
SHEET 1 AA2 6 ILE A 336 ALA A 340 0
SHEET 2 AA2 6 GLY A 471 PHE A 475 1 O GLY A 471 N GLU A 337
SHEET 3 AA2 6 SER A 424 ASP A 427 1 N ASP A 427 O ARG A 474
SHEET 4 AA2 6 ARG A 363 PHE A 367 1 N PHE A 367 O ILE A 426
SHEET 5 AA2 6 VAL A 406 ALA A 410 1 O VAL A 408 N ILE A 366
SHEET 6 AA2 6 ALA A 388 TYR A 391 1 N VAL A 389 O VAL A 409
SHEET 1 AA3 2 ILE A 347 PHE A 349 0
SHEET 2 AA3 2 LYS A 352 ILE A 354 -1 O LYS A 352 N PHE A 349
SHEET 1 AA4 2 THR A 430 ASP A 437 0
SHEET 2 AA4 2 THR A 445 PRO A 452 -1 O THR A 449 N THR A 433
SHEET 1 AA5 2 THR A 596 PRO A 597 0
SHEET 2 AA5 2 VAL A 609 THR A 610 1 O THR A 610 N THR A 596
LINK OD1 ASN A 387 NA NA A 701 1555 1555 3.15
LINK OD1 ASN A 387 NA NA A 701 1555 4555 2.25
LINK NA NA A 701 O HOH A 802 1555 1555 2.78
CISPEP 1 GLY A 281 GLY A 282 0 5.01
CISPEP 2 THR A 416 GLY A 417 0 3.40
CISPEP 3 ASP A 441 PRO A 442 0 6.19
CISPEP 4 GLY A 479 GLU A 480 0 -6.38
SITE 1 AC1 2 ASN A 387 HOH A 802
SITE 1 AC2 4 GLY A 209 SER A 211 THR A 212 HOH A 815
SITE 1 AC3 9 VAL A 232 THR A 254 GLY A 255 THR A 269
SITE 2 AC3 9 GLY A 271 LYS A 272 ALA A 275 TYR A 502
SITE 3 AC3 9 HOH A 900
CRYST1 92.444 92.444 104.133 90.00 90.00 120.00 P 31 2 1 6
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 0.010817 0.006245 0.000000 0.00000
SCALE2 0.000000 0.012491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009603 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
