HEADER HYDROLASE/DNA 17-DEC-97 1A1V
TITLE HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE
TITLE 2 STRANDED SDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (NS3 PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HELICASE DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*UP*UP*UP*UP*UP*UP*UP*U)-3');
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: SINGLE STRANDED DNA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS (ISOLATE H);
SOURCE 3 ORGANISM_TAXID: 11108;
SOURCE 4 STRAIN: H;
SOURCE 5 GENE: NS3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-BS(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHETIC DEOXYOLIGONUCLEOTIDE
KEYWDS HEPATITIS C VIRUS, RNA HELICASE, NONSTRUCTURAL PROTEINS,
KEYWDS 2 SINGLE-STRANDED DNA, HYDROLASE/DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.KIM,K.A.MORGENSTERN,J.P.GRIFFITH,M.D.DWYER,J.A.THOMSON,
AUTHOR 2 M.A.MURCKO,C.LIN,P.R.CARON
REVDAT 2 24-FEB-09 1A1V 1 VERSN
REVDAT 1 13-JAN-99 1A1V 0
JRNL AUTH J.L.KIM,K.A.MORGENSTERN,J.P.GRIFFITH,M.D.DWYER,
JRNL AUTH 2 J.A.THOMSON,M.A.MURCKO,C.LIN,P.R.CARON
JRNL TITL HEPATITIS C VIRUS NS3 RNA HELICASE DOMAIN WITH A
JRNL TITL 2 BOUND OLIGONUCLEOTIDE: THE CRYSTAL STRUCTURE
JRNL TITL 3 PROVIDES INSIGHTS INTO THE MODE OF UNWINDING.
JRNL REF STRUCTURE V. 6 89 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9493270
JRNL DOI 10.1016/S0969-2126(98)00010-0
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 25780
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 SET) : 0.228
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2323
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.27
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1748
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 227
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3220
REMARK 3 NUCLEIC ACID ATOMS : 107
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.10
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.41
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.33
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.100 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.850 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.710 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A1V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31255
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.35500
REMARK 200 R SYM FOR SHELL (I) : 0.13800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 36.55000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.75000
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 APPLY THE FOLLOWING TO CHAINS: B, 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 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 DU B 9
REMARK 465 MET A 166
REMARK 465 VAL A 167
REMARK 465 ASP A 168
REMARK 465 PHE A 169
REMARK 465 ILE A 170
REMARK 465 PRO A 171
REMARK 465 VAL A 172
REMARK 465 GLU A 173
REMARK 465 ASN A 174
REMARK 465 LEU A 175
REMARK 465 GLU A 176
REMARK 465 THR A 177
REMARK 465 THR A 178
REMARK 465 MET 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 ASN A 187
REMARK 465 SER A 188
REMARK 465 SER A 189
REMARK 465 MET A 415
REMARK 465 THR A 416
REMARK 465 GLY A 417
REMARK 465 ALA A 625
REMARK 465 ASP A 626
REMARK 465 LEU A 627
REMARK 465 GLU A 628
REMARK 465 VAL A 629
REMARK 465 VAL A 630
REMARK 465 THR A 631
REMARK 465 GLY A 632
REMARK 465 SER A 633
REMARK 465 GLY A 634
REMARK 465 SER A 635
REMARK 465 HIS A 636
REMARK 465 HIS A 637
REMARK 465 HIS A 638
REMARK 465 HIS A 639
REMARK 465 HIS A 640
REMARK 465 HIS A 641
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 DU B 2 O5' C5' C4' O4' C3' C2' C1'
REMARK 470 DU B 2 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DU B 2 C6
REMARK 470 DU B 3 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DU B 3 C6
REMARK 470 GLN A 195 CG CD OE1 NE2
REMARK 470 LYS A 244 CG CD CE NZ
REMARK 470 GLU A 357 CG CD OE1 OE2
REMARK 470 LYS A 360 CG CD CE NZ
REMARK 470 LYS A 372 CE NZ
REMARK 470 GLU A 530 CG CD OE1 OE2
REMARK 470 HIS A 541 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 580 CG CD OE1 NE2
REMARK 470 LYS A 583 CG CD CE NZ
REMARK 470 ARG A 587 CG CD NE CZ NH1 NH2
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 -60.76 -142.05
REMARK 500 CYS A 292 2.48 -62.68
REMARK 500 THR A 322 145.64 -171.56
REMARK 500 SER A 342 -165.74 -117.94
REMARK 500 LYS A 352 -158.92 -105.53
REMARK 500 VAL A 406 147.90 -172.62
REMARK 500 THR A 443 -87.41 -124.78
REMARK 500 GLU A 447 -151.76 -134.47
REMARK 500 ASP A 527 85.39 -68.68
REMARK 500 LYS A 589 -51.38 -26.74
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 B 106 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A1138 DISTANCE = 6.61 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
DBREF 1A1V A 167 631 UNP P27958 POLG_HCVH 1193 1657
DBREF 1A1V B 2 9 PDB 1A1V 1A1V 2 9
SEQADV 1A1V ALA A 192 UNP P27958 VAL 1218 CONFLICT
SEQADV 1A1V VAL A 248 UNP P27958 ILE 1274 CONFLICT
SEQADV 1A1V CME A 279 UNP P27958 CYS 1305 MODIFIED RESIDUE
SEQADV 1A1V PHE A 418 UNP P27958 TYR 1444 CONFLICT
SEQADV 1A1V CME A 431 UNP P27958 CYS 1457 MODIFIED RESIDUE
SEQADV 1A1V THR A 449 UNP P27958 ILE 1475 CONFLICT
SEQADV 1A1V CME A 499 UNP P27958 CYS 1525 MODIFIED RESIDUE
SEQADV 1A1V PHE A 557 UNP P27958 LEU 1583 CONFLICT
SEQADV 1A1V VAL A 609 UNP P27958 ILE 1635 CONFLICT
SEQADV 1A1V ILE A 615 UNP P27958 VAL 1641 CONFLICT
SEQRES 1 A 476 MET VAL ASP PHE ILE PRO VAL GLU ASN LEU GLU THR THR
SEQRES 2 A 476 MET ARG SER PRO VAL PHE THR ASP ASN SER SER PRO PRO
SEQRES 3 A 476 ALA VAL PRO GLN SER PHE GLN VAL ALA HIS LEU HIS ALA
SEQRES 4 A 476 PRO THR GLY SER GLY LYS SER THR LYS VAL PRO ALA ALA
SEQRES 5 A 476 TYR ALA ALA GLN GLY TYR LYS VAL LEU VAL LEU ASN PRO
SEQRES 6 A 476 SER VAL ALA ALA THR LEU GLY PHE GLY ALA TYR MET SER
SEQRES 7 A 476 LYS ALA HIS GLY VAL ASP PRO ASN ILE ARG THR GLY VAL
SEQRES 8 A 476 ARG THR ILE THR THR GLY SER PRO ILE THR TYR SER THR
SEQRES 9 A 476 TYR GLY LYS PHE LEU ALA ASP GLY GLY CME SER GLY GLY
SEQRES 10 A 476 ALA TYR ASP ILE ILE ILE CYS ASP GLU CYS HIS SER THR
SEQRES 11 A 476 ASP ALA THR SER ILE LEU GLY ILE GLY THR VAL LEU ASP
SEQRES 12 A 476 GLN ALA GLU THR ALA GLY ALA ARG LEU VAL VAL LEU ALA
SEQRES 13 A 476 THR ALA THR PRO PRO GLY SER VAL THR VAL PRO HIS PRO
SEQRES 14 A 476 ASN ILE GLU GLU VAL ALA LEU SER THR THR GLY GLU ILE
SEQRES 15 A 476 PRO PHE TYR GLY LYS ALA ILE PRO LEU GLU VAL ILE LYS
SEQRES 16 A 476 GLY GLY ARG HIS LEU ILE PHE CYS HIS SER LYS LYS LYS
SEQRES 17 A 476 CYS ASP GLU LEU ALA ALA LYS LEU VAL ALA LEU GLY ILE
SEQRES 18 A 476 ASN ALA VAL ALA TYR TYR ARG GLY LEU ASP VAL SER VAL
SEQRES 19 A 476 ILE PRO THR SER GLY ASP VAL VAL VAL VAL ALA THR ASP
SEQRES 20 A 476 ALA LEU MET THR GLY PHE THR GLY ASP PHE ASP SER VAL
SEQRES 21 A 476 ILE ASP CYS ASN THR CME VAL THR GLN THR VAL ASP PHE
SEQRES 22 A 476 SER LEU ASP PRO THR PHE THR ILE GLU THR THR THR LEU
SEQRES 23 A 476 PRO GLN ASP ALA VAL SER ARG THR GLN ARG ARG GLY ARG
SEQRES 24 A 476 THR GLY ARG GLY LYS PRO GLY ILE TYR ARG PHE VAL ALA
SEQRES 25 A 476 PRO GLY GLU ARG PRO SER GLY MET PHE ASP SER SER VAL
SEQRES 26 A 476 LEU CYS GLU CYS TYR ASP ALA GLY CME ALA TRP TYR GLU
SEQRES 27 A 476 LEU THR PRO ALA GLU THR THR VAL ARG LEU ARG ALA TYR
SEQRES 28 A 476 MET ASN THR PRO GLY LEU PRO VAL CYS GLN ASP HIS LEU
SEQRES 29 A 476 GLU PHE TRP GLU GLY VAL PHE THR GLY LEU THR HIS ILE
SEQRES 30 A 476 ASP ALA HIS PHE LEU SER GLN THR LYS GLN SER GLY GLU
SEQRES 31 A 476 ASN PHE PRO TYR LEU VAL ALA TYR GLN ALA THR VAL CYS
SEQRES 32 A 476 ALA ARG ALA GLN ALA PRO PRO PRO SER TRP ASP GLN MET
SEQRES 33 A 476 TRP LYS CYS LEU ILE ARG LEU LYS PRO THR LEU HIS GLY
SEQRES 34 A 476 PRO THR PRO LEU LEU TYR ARG LEU GLY ALA VAL GLN ASN
SEQRES 35 A 476 GLU VAL THR LEU THR HIS PRO ILE THR LYS TYR ILE MET
SEQRES 36 A 476 THR CYS MET SER ALA ASP LEU GLU VAL VAL THR GLY SER
SEQRES 37 A 476 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 8 DU DU DU DU DU DU DU DU
MODRES 1A1V CME A 279 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1A1V CME A 431 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1A1V CME A 499 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 279 12
HET CME A 431 12
HET CME A 499 12
HET SO4 A1001 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
FORMUL 2 CME 3(C5 H11 N O3 S2)
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *159(H2 O)
HELIX 1 1 LYS A 213 GLN A 221 1 9
HELIX 2 2 VAL A 232 HIS A 246 1 15
HELIX 3 3 TYR A 270 ALA A 275 1 6
HELIX 4 4 ALA A 297 GLN A 309 1 13
HELIX 5 5 LEU A 356 LYS A 360 5 5
HELIX 6 6 LYS A 371 ALA A 383 1 13
HELIX 7 7 VAL A 397 VAL A 399 5 3
HELIX 8 8 ALA A 455 ARG A 464 1 10
HELIX 9 9 SER A 488 ALA A 500 1 13
HELIX 10 10 PRO A 506 ASN A 518 1 13
HELIX 11 11 LEU A 529 GLY A 538 1 10
HELIX 12 12 ALA A 544 GLN A 552 1 9
HELIX 13 13 PRO A 558 ALA A 571 1 14
HELIX 14 14 GLN A 580 LEU A 585 5 6
HELIX 15 15 LYS A 589 THR A 591 5 3
HELIX 16 16 PRO A 614 CYS A 622 1 9
SHEET 1 A 6 GLN A 198 HIS A 203 0
SHEET 2 A 6 LEU A 317 THR A 322 1 N VAL A 318 O GLN A 198
SHEET 3 A 6 ILE A 286 ASP A 290 1 N ILE A 287 O LEU A 317
SHEET 4 A 6 VAL A 225 ASN A 229 1 N LEU A 226 O ILE A 286
SHEET 5 A 6 ILE A 265 THR A 269 1 N THR A 266 O VAL A 225
SHEET 6 A 6 ASN A 251 ARG A 253 1 N ASN A 251 O TYR A 267
SHEET 1 B 2 ILE A 347 PHE A 349 0
SHEET 2 B 2 LYS A 352 ILE A 354 -1 N ILE A 354 O ILE A 347
SHEET 1 C 3 ARG A 363 PHE A 367 0
SHEET 2 C 3 VAL A 406 ALA A 410 1 N VAL A 406 O HIS A 364
SHEET 3 C 3 ALA A 388 TYR A 391 1 N VAL A 389 O VAL A 407
SHEET 1 D 2 SER A 424 ASP A 427 0
SHEET 2 D 2 ILE A 472 PHE A 475 1 N ILE A 472 O VAL A 425
SHEET 1 E 2 THR A 433 ASP A 437 0
SHEET 2 E 2 THR A 445 THR A 449 -1 N THR A 449 O THR A 433
LINK N CME A 279 C GLY A 278 1555 1555 1.32
LINK C CME A 279 N SER A 280 1555 1555 1.33
LINK N CME A 431 C THR A 430 1555 1555 1.33
LINK C CME A 431 N VAL A 432 1555 1555 1.32
LINK N CME A 499 C GLY A 498 1555 1555 1.33
LINK C CME A 499 N ALA A 500 1555 1555 1.33
CISPEP 1 ASP A 441 PRO A 442 0 0.45
SITE 1 AC1 9 PRO A 205 THR A 206 GLY A 207 SER A 208
SITE 2 AC1 9 GLY A 209 LYS A 210 SER A 211 HOH A1062
SITE 3 AC1 9 HOH A1070
CRYST1 73.100 117.500 63.400 90.00 90.00 90.00 P 21 21 2 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 0.013680 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015773 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
