HEADER HYDROLASE/HYDROLASE INHIBITOR 21-JAN-14 4OK3
TITLE CRYSTAL STRUCTURE OF HEPATITIS C VIRUS NS3 HELICASE INHIBITOR CO-
TITLE 2 COMPLEX WITH COMPOUND 7 [[1-(3-CHLOROBENZYL)-1H-INDOL-3-YL]ACETIC
TITLE 3 ACID]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE NS3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1206-1656;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_TAXID: 11103;
SOURCE 4 GENE: NS3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HEPATITIS, ATPASE, NTPASE, NS3 HELICASE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.PADYANA
REVDAT 3 28-FEB-24 4OK3 1 REMARK SEQADV LINK
REVDAT 2 02-APR-14 4OK3 1 JRNL
REVDAT 1 05-MAR-14 4OK3 0
JRNL AUTH S.R.LAPLANTE,A.K.PADYANA,A.ABEYWARDANE,P.BONNEAU,M.CARTIER,
JRNL AUTH 2 R.COULOMBE,A.JAKALIAN,J.WILDESON-JONES,X.LI,S.LIANG,
JRNL AUTH 3 G.MCKERCHER,P.WHITE,Q.ZHANG,S.J.TAYLOR
JRNL TITL INTEGRATED STRATEGIES FOR IDENTIFYING LEADS THAT TARGET THE
JRNL TITL 2 NS3 HELICASE OF THE HEPATITIS C VIRUS.
JRNL REF J.MED.CHEM. V. 57 2074 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 24467709
JRNL DOI 10.1021/JM401432C
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 45249
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2281
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 47.6805 - 5.7925 0.99 2860 146 0.1826 0.2384
REMARK 3 2 5.7925 - 4.5989 1.00 2726 168 0.1858 0.2698
REMARK 3 3 4.5989 - 4.0179 1.00 2705 145 0.1850 0.2235
REMARK 3 4 4.0179 - 3.6507 1.00 2720 148 0.2188 0.2511
REMARK 3 5 3.6507 - 3.3891 1.00 2701 118 0.2450 0.3200
REMARK 3 6 3.3891 - 3.1893 1.00 2679 146 0.2591 0.3436
REMARK 3 7 3.1893 - 3.0296 1.00 2679 138 0.2805 0.3689
REMARK 3 8 3.0296 - 2.8978 1.00 2656 154 0.2931 0.3230
REMARK 3 9 2.8978 - 2.7862 1.00 2673 149 0.2839 0.3791
REMARK 3 10 2.7862 - 2.6901 1.00 2645 131 0.3150 0.3543
REMARK 3 11 2.6901 - 2.6060 1.00 2632 149 0.3061 0.3538
REMARK 3 12 2.6060 - 2.5315 1.00 2683 131 0.3185 0.4077
REMARK 3 13 2.5315 - 2.4649 1.00 2658 118 0.3062 0.3689
REMARK 3 14 2.4649 - 2.4047 1.00 2637 160 0.3086 0.3838
REMARK 3 15 2.4047 - 2.3501 1.00 2651 136 0.3085 0.3487
REMARK 3 16 2.3501 - 2.3000 1.00 2663 144 0.3298 0.4088
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.21
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 : 0.010 6544
REMARK 3 ANGLE : 1.397 8936
REMARK 3 CHIRALITY : 0.052 1037
REMARK 3 PLANARITY : 0.007 1149
REMARK 3 DIHEDRAL : 15.149 2327
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4OK3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084592.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : D*TREK 9.9.2L
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.9.2L
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45339
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.290
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
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 : 6.52
REMARK 200 R MERGE FOR SHELL (I) : 0.78700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 40.69700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.97700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.11600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.97700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.69700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.11600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 167
REMARK 465 GLY A 168
REMARK 465 SER A 169
REMARK 465 SER A 170
REMARK 465 HIS A 171
REMARK 465 HIS A 172
REMARK 465 HIS A 173
REMARK 465 HIS A 174
REMARK 465 HIS A 175
REMARK 465 HIS A 176
REMARK 465 SER A 177
REMARK 465 SER A 178
REMARK 465 GLY A 179
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 465 ASP A 186
REMARK 465 VAL A 382
REMARK 465 ALA A 383
REMARK 465 LEU A 384
REMARK 465 GLY A 385
REMARK 465 ILE A 386
REMARK 465 TYR A 391
REMARK 465 TYR A 392
REMARK 465 ARG A 393
REMARK 465 GLY A 394
REMARK 465 LEU A 395
REMARK 465 ASP A 396
REMARK 465 VAL A 397
REMARK 465 THR A 402
REMARK 465 ASN A 403
REMARK 465 GLY A 404
REMARK 465 PHE A 418
REMARK 465 THR A 419
REMARK 465 VAL A 630
REMARK 465 MET B 167
REMARK 465 GLY B 168
REMARK 465 SER B 169
REMARK 465 SER B 170
REMARK 465 HIS B 171
REMARK 465 HIS B 172
REMARK 465 HIS B 173
REMARK 465 HIS B 174
REMARK 465 HIS B 175
REMARK 465 HIS B 176
REMARK 465 SER B 177
REMARK 465 SER B 178
REMARK 465 GLY B 179
REMARK 465 ARG B 180
REMARK 465 SER B 181
REMARK 465 PRO B 182
REMARK 465 VAL B 183
REMARK 465 PHE B 184
REMARK 465 THR B 185
REMARK 465 ASP B 186
REMARK 465 HIS B 246
REMARK 465 GLY B 247
REMARK 465 VAL B 248
REMARK 465 ASP B 249
REMARK 465 PRO B 250
REMARK 465 ASN B 251
REMARK 465 ILE B 252
REMARK 465 ARG B 253
REMARK 465 THR B 254
REMARK 465 GLY B 255
REMARK 465 VAL B 256
REMARK 465 ARG B 257
REMARK 465 THR B 258
REMARK 465 ILE B 259
REMARK 465 THR B 260
REMARK 465 THR B 261
REMARK 465 GLY B 262
REMARK 465 MET B 415
REMARK 465 THR B 416
REMARK 465 GLY B 417
REMARK 465 PHE B 418
REMARK 465 THR B 419
REMARK 465 VAL B 629
REMARK 465 VAL B 630
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 OG SER B 553 OE1 GLU B 555 2.19
REMARK 500 O PRO A 574 OG1 THR A 596 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 375 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LEU B 588 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
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 -65.23 -125.03
REMARK 500 LYS A 372 -73.37 -53.13
REMARK 500 ASP A 375 55.79 -152.05
REMARK 500 ALA A 378 -170.28 125.09
REMARK 500 ALA A 379 26.58 -74.49
REMARK 500 LYS A 380 -57.35 -29.83
REMARK 500 ILE A 400 122.96 -177.68
REMARK 500 THR A 443 -86.15 -130.29
REMARK 500 MET A 581 -35.34 -34.69
REMARK 500 LEU A 585 50.07 -100.96
REMARK 500 ARG A 587 52.91 -154.68
REMARK 500 LEU A 592 0.33 -59.55
REMARK 500 GLU A 628 -165.45 -75.91
REMARK 500 SER B 211 102.72 -49.75
REMARK 500 LYS B 352 -164.78 -118.89
REMARK 500 TYR B 392 -178.76 -172.24
REMARK 500 ASP B 396 -95.53 -121.96
REMARK 500 VAL B 397 44.51 -143.32
REMARK 500 ASN B 403 35.32 -150.71
REMARK 500 ASP B 405 131.98 -33.81
REMARK 500 ASP B 441 53.82 -140.65
REMARK 500 THR B 443 -94.60 -124.12
REMARK 500 GLN B 572 85.42 31.49
REMARK 500 TRP B 578 14.33 -140.97
REMARK 500 CYS B 584 -17.26 -46.10
REMARK 500 ILE B 586 49.73 -87.52
REMARK 500 ARG B 587 44.07 -95.97
REMARK 500 HIS B 593 67.34 -49.19
REMARK 500 PRO B 597 91.41 -69.22
REMARK 500 LEU B 611 34.43 -89.02
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 ASP A 375 GLU A 376 141.62
REMARK 500 GLU A 376 LEU A 377 146.55
REMARK 500 LEU A 377 ALA A 378 123.29
REMARK 500 PRO B 401 THR B 402 144.97
REMARK 500 THR B 402 ASN B 403 -149.04
REMARK 500 ASP B 579 GLN B 580 -147.81
REMARK 500 LYS B 589 PRO B 590 142.24
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 A 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 437 OD2
REMARK 620 2 ASP A 437 OD1 52.9
REMARK 620 3 HOH A 839 O 53.5 106.3
REMARK 620 4 ASP B 437 OD2 98.2 133.6 56.6
REMARK 620 5 HOH B 704 O 103.7 65.1 132.9 94.4
REMARK 620 6 HOH B 737 O 83.2 121.7 49.9 82.3 172.7
REMARK 620 7 HOH B 750 O 163.8 118.9 131.1 78.0 61.2 111.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 703 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 437 OD2
REMARK 620 2 GLU A 447 OE2 91.5
REMARK 620 3 HOH A 839 O 49.8 121.1
REMARK 620 4 ASP B 437 OD1 108.3 149.0 89.8
REMARK 620 5 ASP B 437 OD2 67.6 158.1 50.1 44.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2SY A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OJQ RELATED DB: PDB
REMARK 900 RELATED ID: 4OK5 RELATED DB: PDB
REMARK 900 RELATED ID: 4OK6 RELATED DB: PDB
REMARK 900 RELATED ID: 4OKS RELATED DB: PDB
DBREF 4OK3 A 180 630 UNP K4KA16 K4KA16_9HEPC 1206 1656
DBREF 4OK3 B 180 630 UNP K4KA16 K4KA16_9HEPC 1206 1656
SEQADV 4OK3 MET A 167 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 GLY A 168 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER A 169 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER A 170 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS A 171 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS A 172 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS A 173 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS A 174 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS A 175 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS A 176 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER A 177 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER A 178 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 GLY A 179 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 ASN A 403 UNP K4KA16 SER 1429 CONFLICT
SEQADV 4OK3 MET A 505 UNP K4KA16 THR 1531 CONFLICT
SEQADV 4OK3 MET B 167 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 GLY B 168 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER B 169 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER B 170 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS B 171 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS B 172 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS B 173 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS B 174 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS B 175 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 HIS B 176 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER B 177 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 SER B 178 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 GLY B 179 UNP K4KA16 EXPRESSION TAG
SEQADV 4OK3 ASN B 403 UNP K4KA16 SER 1429 CONFLICT
SEQADV 4OK3 MET B 505 UNP K4KA16 THR 1531 CONFLICT
SEQRES 1 A 464 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 464 ARG SER PRO VAL PHE THR ASP ASN SER SER PRO PRO ALA
SEQRES 3 A 464 VAL PRO GLN SER PHE GLN VAL ALA HIS LEU HIS ALA PRO
SEQRES 4 A 464 THR GLY SER GLY LYS SER THR LYS VAL PRO ALA ALA TYR
SEQRES 5 A 464 ALA ALA GLN GLY TYR LYS VAL LEU VAL LEU ASN PRO SER
SEQRES 6 A 464 VAL ALA ALA THR LEU GLY PHE GLY ALA TYR MET SER LYS
SEQRES 7 A 464 ALA HIS GLY VAL ASP PRO ASN ILE ARG THR GLY VAL ARG
SEQRES 8 A 464 THR ILE THR THR GLY SER PRO ILE THR TYR SER THR TYR
SEQRES 9 A 464 GLY LYS PHE LEU ALA ASP GLY GLY CYS SER GLY GLY ALA
SEQRES 10 A 464 TYR ASP ILE ILE ILE CYS ASP GLU CYS HIS SER THR ASP
SEQRES 11 A 464 ALA THR SER ILE LEU GLY ILE GLY THR VAL LEU ASP GLN
SEQRES 12 A 464 ALA GLU THR ALA GLY ALA ARG LEU VAL VAL LEU ALA THR
SEQRES 13 A 464 ALA THR PRO PRO GLY SER VAL THR VAL SER HIS PRO ASN
SEQRES 14 A 464 ILE GLU GLU VAL ALA LEU SER THR THR GLY GLU ILE PRO
SEQRES 15 A 464 PHE TYR GLY LYS ALA ILE PRO LEU GLU VAL ILE LYS GLY
SEQRES 16 A 464 GLY ARG HIS LEU ILE PHE CYS HIS SER LYS LYS LYS CYS
SEQRES 17 A 464 ASP GLU LEU ALA ALA LYS LEU VAL ALA LEU GLY ILE ASN
SEQRES 18 A 464 ALA VAL ALA TYR TYR ARG GLY LEU ASP VAL SER VAL ILE
SEQRES 19 A 464 PRO THR ASN GLY ASP VAL VAL VAL VAL SER THR ASP ALA
SEQRES 20 A 464 LEU MET THR GLY PHE THR GLY ASP PHE ASP SER VAL ILE
SEQRES 21 A 464 ASP CYS ASN THR CYS VAL THR GLN THR VAL ASP PHE SER
SEQRES 22 A 464 LEU ASP PRO THR PHE THR ILE GLU THR THR THR LEU PRO
SEQRES 23 A 464 GLN ASP ALA VAL SER ARG THR GLN ARG ARG GLY ARG THR
SEQRES 24 A 464 GLY ARG GLY LYS PRO GLY ILE TYR ARG PHE VAL ALA PRO
SEQRES 25 A 464 GLY GLU ARG PRO SER GLY MET PHE ASP SER SER VAL LEU
SEQRES 26 A 464 CYS GLU CYS TYR ASP ALA GLY CYS ALA TRP TYR GLU LEU
SEQRES 27 A 464 MET PRO ALA GLU THR THR VAL ARG LEU ARG ALA TYR MET
SEQRES 28 A 464 ASN THR PRO GLY LEU PRO VAL CYS GLN ASP HIS LEU GLU
SEQRES 29 A 464 PHE TRP GLU GLY VAL PHE THR GLY LEU THR HIS ILE ASP
SEQRES 30 A 464 ALA HIS PHE LEU SER GLN THR LYS GLN SER GLY GLU ASN
SEQRES 31 A 464 PHE PRO TYR LEU VAL ALA TYR GLN ALA THR VAL CYS ALA
SEQRES 32 A 464 ARG ALA GLN ALA PRO PRO PRO SER TRP ASP GLN MET TRP
SEQRES 33 A 464 LYS CYS LEU ILE ARG LEU LYS PRO THR LEU HIS GLY PRO
SEQRES 34 A 464 THR PRO LEU LEU TYR ARG LEU GLY ALA VAL GLN ASN GLU
SEQRES 35 A 464 VAL THR LEU THR HIS PRO ILE THR LYS TYR ILE MET THR
SEQRES 36 A 464 CYS MET SER ALA ASP LEU GLU VAL VAL
SEQRES 1 B 464 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 464 ARG SER PRO VAL PHE THR ASP ASN SER SER PRO PRO ALA
SEQRES 3 B 464 VAL PRO GLN SER PHE GLN VAL ALA HIS LEU HIS ALA PRO
SEQRES 4 B 464 THR GLY SER GLY LYS SER THR LYS VAL PRO ALA ALA TYR
SEQRES 5 B 464 ALA ALA GLN GLY TYR LYS VAL LEU VAL LEU ASN PRO SER
SEQRES 6 B 464 VAL ALA ALA THR LEU GLY PHE GLY ALA TYR MET SER LYS
SEQRES 7 B 464 ALA HIS GLY VAL ASP PRO ASN ILE ARG THR GLY VAL ARG
SEQRES 8 B 464 THR ILE THR THR GLY SER PRO ILE THR TYR SER THR TYR
SEQRES 9 B 464 GLY LYS PHE LEU ALA ASP GLY GLY CYS SER GLY GLY ALA
SEQRES 10 B 464 TYR ASP ILE ILE ILE CYS ASP GLU CYS HIS SER THR ASP
SEQRES 11 B 464 ALA THR SER ILE LEU GLY ILE GLY THR VAL LEU ASP GLN
SEQRES 12 B 464 ALA GLU THR ALA GLY ALA ARG LEU VAL VAL LEU ALA THR
SEQRES 13 B 464 ALA THR PRO PRO GLY SER VAL THR VAL SER HIS PRO ASN
SEQRES 14 B 464 ILE GLU GLU VAL ALA LEU SER THR THR GLY GLU ILE PRO
SEQRES 15 B 464 PHE TYR GLY LYS ALA ILE PRO LEU GLU VAL ILE LYS GLY
SEQRES 16 B 464 GLY ARG HIS LEU ILE PHE CYS HIS SER LYS LYS LYS CYS
SEQRES 17 B 464 ASP GLU LEU ALA ALA LYS LEU VAL ALA LEU GLY ILE ASN
SEQRES 18 B 464 ALA VAL ALA TYR TYR ARG GLY LEU ASP VAL SER VAL ILE
SEQRES 19 B 464 PRO THR ASN GLY ASP VAL VAL VAL VAL SER THR ASP ALA
SEQRES 20 B 464 LEU MET THR GLY PHE THR GLY ASP PHE ASP SER VAL ILE
SEQRES 21 B 464 ASP CYS ASN THR CYS VAL THR GLN THR VAL ASP PHE SER
SEQRES 22 B 464 LEU ASP PRO THR PHE THR ILE GLU THR THR THR LEU PRO
SEQRES 23 B 464 GLN ASP ALA VAL SER ARG THR GLN ARG ARG GLY ARG THR
SEQRES 24 B 464 GLY ARG GLY LYS PRO GLY ILE TYR ARG PHE VAL ALA PRO
SEQRES 25 B 464 GLY GLU ARG PRO SER GLY MET PHE ASP SER SER VAL LEU
SEQRES 26 B 464 CYS GLU CYS TYR ASP ALA GLY CYS ALA TRP TYR GLU LEU
SEQRES 27 B 464 MET PRO ALA GLU THR THR VAL ARG LEU ARG ALA TYR MET
SEQRES 28 B 464 ASN THR PRO GLY LEU PRO VAL CYS GLN ASP HIS LEU GLU
SEQRES 29 B 464 PHE TRP GLU GLY VAL PHE THR GLY LEU THR HIS ILE ASP
SEQRES 30 B 464 ALA HIS PHE LEU SER GLN THR LYS GLN SER GLY GLU ASN
SEQRES 31 B 464 PHE PRO TYR LEU VAL ALA TYR GLN ALA THR VAL CYS ALA
SEQRES 32 B 464 ARG ALA GLN ALA PRO PRO PRO SER TRP ASP GLN MET TRP
SEQRES 33 B 464 LYS CYS LEU ILE ARG LEU LYS PRO THR LEU HIS GLY PRO
SEQRES 34 B 464 THR PRO LEU LEU TYR ARG LEU GLY ALA VAL GLN ASN GLU
SEQRES 35 B 464 VAL THR LEU THR HIS PRO ILE THR LYS TYR ILE MET THR
SEQRES 36 B 464 CYS MET SER ALA ASP LEU GLU VAL VAL
HET 2SY A 701 21
HET CA A 702 1
HET CA A 703 1
HETNAM 2SY [1-(3-CHLOROBENZYL)-1H-INDOL-3-YL]ACETIC ACID
HETNAM CA CALCIUM ION
FORMUL 3 2SY C17 H14 CL N O2
FORMUL 4 CA 2(CA 2+)
FORMUL 6 HOH *104(H2 O)
HELIX 1 1 PRO A 205 GLY A 209 5 5
HELIX 2 2 THR A 212 GLN A 221 1 10
HELIX 3 3 SER A 231 GLY A 247 1 17
HELIX 4 4 TYR A 270 ASP A 276 1 7
HELIX 5 5 ASP A 296 GLY A 314 1 19
HELIX 6 6 PRO A 355 ILE A 359 5 5
HELIX 7 7 SER A 370 ASP A 375 1 6
HELIX 8 8 ASP A 454 GLY A 463 1 10
HELIX 9 9 ASP A 487 TRP A 501 1 15
HELIX 10 10 MET A 505 THR A 519 1 15
HELIX 11 11 HIS A 528 GLY A 538 1 11
HELIX 12 12 ASP A 543 GLY A 554 1 12
HELIX 13 13 PHE A 557 ALA A 571 1 15
HELIX 14 14 ASP A 579 ILE A 586 5 8
HELIX 15 15 ARG A 587 LEU A 592 1 6
HELIX 16 16 HIS A 613 LEU A 627 1 15
HELIX 17 17 THR B 212 GLN B 221 1 10
HELIX 18 18 TYR B 270 ASP B 276 1 7
HELIX 19 19 ASP B 296 ALA B 310 1 15
HELIX 20 20 PRO B 355 ILE B 359 5 5
HELIX 21 21 SER B 370 ALA B 383 1 14
HELIX 22 22 ASP B 454 ARG B 464 1 11
HELIX 23 23 ASP B 487 TRP B 501 1 15
HELIX 24 24 MET B 505 ASN B 518 1 14
HELIX 25 25 HIS B 528 LEU B 539 1 12
HELIX 26 26 ASP B 543 SER B 553 1 11
HELIX 27 27 PHE B 557 GLN B 572 1 16
HELIX 28 28 ASP B 579 ILE B 586 5 8
HELIX 29 29 HIS B 613 LEU B 627 1 15
SHEET 1 A 7 GLN A 198 HIS A 203 0
SHEET 2 A 7 LEU A 317 THR A 322 1 O VAL A 318 N ALA A 200
SHEET 3 A 7 ILE A 286 CYS A 289 1 N CYS A 289 O VAL A 319
SHEET 4 A 7 VAL A 225 ASN A 229 1 N LEU A 226 O ILE A 288
SHEET 5 A 7 ILE A 265 THR A 269 1 O THR A 266 N VAL A 227
SHEET 6 A 7 ASN A 251 ARG A 253 1 N ASN A 251 O TYR A 267
SHEET 7 A 7 THR A 258 ILE A 259 -1 O ILE A 259 N ILE A 252
SHEET 1 B 6 ILE A 336 ALA A 340 0
SHEET 2 B 6 GLY A 471 PHE A 475 1 O TYR A 473 N VAL A 339
SHEET 3 B 6 SER A 424 ASP A 427 1 N VAL A 425 O ARG A 474
SHEET 4 B 6 ARG A 363 PHE A 367 1 N LEU A 365 O ILE A 426
SHEET 5 B 6 VAL A 406 SER A 410 1 O VAL A 408 N HIS A 364
SHEET 6 B 6 ALA A 388 VAL A 389 1 N VAL A 389 O VAL A 409
SHEET 1 C 2 THR A 430 ASP A 437 0
SHEET 2 C 2 THR A 445 PRO A 452 -1 O THR A 445 N ASP A 437
SHEET 1 D 2 THR A 596 PRO A 597 0
SHEET 2 D 2 VAL A 609 THR A 610 1 O THR A 610 N THR A 596
SHEET 1 E 5 GLN B 198 HIS B 203 0
SHEET 2 E 5 LEU B 317 THR B 322 1 O VAL B 318 N ALA B 200
SHEET 3 E 5 ILE B 286 CYS B 289 1 N CYS B 289 O VAL B 319
SHEET 4 E 5 VAL B 225 ASN B 229 1 N LEU B 226 O ILE B 288
SHEET 5 E 5 ILE B 265 THR B 269 1 O THR B 266 N VAL B 227
SHEET 1 F 6 ILE B 336 ALA B 340 0
SHEET 2 F 6 GLY B 471 PHE B 475 1 O TYR B 473 N GLU B 337
SHEET 3 F 6 SER B 424 ASP B 427 1 N VAL B 425 O ARG B 474
SHEET 4 F 6 ARG B 363 PHE B 367 1 N PHE B 367 O ILE B 426
SHEET 5 F 6 VAL B 406 SER B 410 1 O VAL B 408 N ILE B 366
SHEET 6 F 6 ALA B 388 TYR B 391 1 N VAL B 389 O VAL B 409
SHEET 1 G 2 ILE B 347 PHE B 349 0
SHEET 2 G 2 LYS B 352 ILE B 354 -1 O LYS B 352 N PHE B 349
SHEET 1 H 2 THR B 430 ASP B 437 0
SHEET 2 H 2 THR B 445 PRO B 452 -1 O GLU B 447 N THR B 435
SHEET 1 I 2 THR B 596 PRO B 597 0
SHEET 2 I 2 VAL B 609 THR B 610 1 O THR B 610 N THR B 596
LINK OD2 ASP A 437 CA CA A 702 1555 1555 2.23
LINK OD1 ASP A 437 CA CA A 702 1555 1555 2.63
LINK OD2 ASP A 437 CA CA A 703 1555 1555 2.96
LINK OE2 GLU A 447 CA CA A 703 1555 1555 2.32
LINK CA CA A 702 O HOH A 839 1555 1555 2.82
LINK CA CA A 702 OD2 ASP B 437 1555 1555 2.26
LINK CA CA A 702 O HOH B 704 1555 1555 2.69
LINK CA CA A 702 O HOH B 737 1555 1555 2.91
LINK CA CA A 702 O HOH B 750 1555 1555 2.34
LINK CA CA A 703 O HOH A 839 1555 1555 2.51
LINK CA CA A 703 OD1 ASP B 437 1555 1555 2.43
LINK CA CA A 703 OD2 ASP B 437 1555 1555 3.14
CISPEP 1 LYS A 360 GLY A 361 0 -3.06
CISPEP 2 SER A 398 VAL A 399 0 -1.40
CISPEP 3 ASP A 441 PRO A 442 0 11.19
CISPEP 4 ASP B 441 PRO B 442 0 5.87
SITE 1 AC1 10 VAL A 232 THR A 254 GLY A 255 THR A 269
SITE 2 AC1 10 GLY A 271 LYS A 272 ALA A 275 THR A 298
SITE 3 AC1 10 ALA A 497 TYR A 502
SITE 1 AC2 6 ASP A 437 HOH A 839 ASP B 437 HOH B 704
SITE 2 AC2 6 HOH B 737 HOH B 750
SITE 1 AC3 4 ASP A 437 GLU A 447 HOH A 839 ASP B 437
CRYST1 81.394 104.232 117.954 90.00 90.00 90.00 P 21 21 21 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 0.012286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008478 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
