HEADER VIRAL PROTEIN, HYDROLASE 14-NOV-13 4NLV
TITLE POLIOVIRUS POLYMERASE - G289A/C290F LOOP MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-DIRECTED RNA POLYMERASE 3D-POL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P3D-POL, GENOME POLYPROTEIN;
COMPND 5 EC: 2.7.7.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN POLIOVIRUS 1;
SOURCE 3 ORGANISM_TAXID: 12081;
SOURCE 4 STRAIN: MAHONEY;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKK
KEYWDS POLYMERASE, RNA DEPENDENT RNA POLYMERASE, RDRP, VIRUS, VIRAL PROTEIN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.SHOLDERS,O.B.PEERSEN
REVDAT 2 26-MAR-14 4NLV 1 JRNL
REVDAT 1 22-JAN-14 4NLV 0
JRNL AUTH A.J.SHOLDERS,O.B.PEERSEN
JRNL TITL DISTINCT CONFORMATIONS OF A PUTATIVE TRANSLOCATION ELEMENT
JRNL TITL 2 IN POLIOVIRUS POLYMERASE.
JRNL REF J.MOL.BIOL. V. 426 1407 2014
JRNL REFN ISSN 0022-2836
JRNL PMID 24424421
JRNL DOI 10.1016/J.JMB.2013.12.031
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 41635
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.400
REMARK 3 FREE R VALUE TEST SET COUNT : 4463
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1555
REMARK 3 BIN R VALUE (WORKING SET) : 0.3108
REMARK 3 BIN FREE R VALUE : 0.3246
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 122
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3710
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.35700
REMARK 3 B22 (A**2) : -5.35700
REMARK 3 B33 (A**2) : 10.71400
REMARK 3 B12 (A**2) : -6.78800
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : NULL
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.985 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.236 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.339 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 31.97
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 : PROTEIN_REP3.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : AJS2.PARAM
REMARK 3 PARAMETER FILE 5 : NTPS.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NLV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB083365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE FLAT SI CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.570
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
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 : 6.44
REMARK 200 R MERGE FOR SHELL (I) : 0.35800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: GROWN IN SODIUM ACETATE, CACODYLATE,
REMARK 280 DTT. TRANSFERRED TO 250 MM SODIUM ACETATE, 30% (W/V) PEG-400, 0.1
REMARK 280 M CACODYLIC ACID, 2 MM DTT, PH 7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 74.41533
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 37.20767
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.81150
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 18.60383
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 93.01917
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 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 GLU A 226 -154.54 -83.91
REMARK 500 LYS A 276 -114.61 62.85
REMARK 500 ASP A 406 113.40 -173.16
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 911 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 285 O
REMARK 620 2 LEU A 268 O 85.4
REMARK 620 3 GLY A 284 O 74.9 133.8
REMARK 620 4 SER A 271 OG 140.2 86.3 134.2
REMARK 620 5 HOH A1104 O 76.2 119.1 96.4 74.2
REMARK 620 6 ASN A 269 O 116.7 77.3 75.2 99.2 161.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 911
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NLO RELATED DB: PDB
REMARK 900 RELATED ID: 4NLP RELATED DB: PDB
REMARK 900 RELATED ID: 4NLQ RELATED DB: PDB
REMARK 900 RELATED ID: 4NLR RELATED DB: PDB
REMARK 900 RELATED ID: 4NLS RELATED DB: PDB
REMARK 900 RELATED ID: 4NLT RELATED DB: PDB
REMARK 900 RELATED ID: 4NLU RELATED DB: PDB
REMARK 900 RELATED ID: 4NLW RELATED DB: PDB
REMARK 900 RELATED ID: 4NLX RELATED DB: PDB
REMARK 900 RELATED ID: 4NLY RELATED DB: PDB
DBREF 4NLV A 1 461 UNP P03300 POLG_POL1M 1749 2209
SEQADV 4NLV ALA A 289 UNP P03300 GLY 2037 ENGINEERED MUTATION
SEQADV 4NLV PHE A 290 UNP P03300 CYS 2038 ENGINEERED MUTATION
SEQADV 4NLV ASP A 446 UNP P03300 LEU 2194 ENGINEERED MUTATION
SEQADV 4NLV ASP A 455 UNP P03300 ARG 2203 ENGINEERED MUTATION
SEQRES 1 A 461 GLY GLU ILE GLN TRP MET ARG PRO SER LYS GLU VAL GLY
SEQRES 2 A 461 TYR PRO ILE ILE ASN ALA PRO SER LYS THR LYS LEU GLU
SEQRES 3 A 461 PRO SER ALA PHE HIS TYR VAL PHE GLU GLY VAL LYS GLU
SEQRES 4 A 461 PRO ALA VAL LEU THR LYS ASN ASP PRO ARG LEU LYS THR
SEQRES 5 A 461 ASP PHE GLU GLU ALA ILE PHE SER LYS TYR VAL GLY ASN
SEQRES 6 A 461 LYS ILE THR GLU VAL ASP GLU TYR MET LYS GLU ALA VAL
SEQRES 7 A 461 ASP HIS TYR ALA GLY GLN LEU MET SER LEU ASP ILE ASN
SEQRES 8 A 461 THR GLU GLN MET CAS LEU GLU ASP ALA MET TYR GLY THR
SEQRES 9 A 461 ASP GLY LEU GLU ALA LEU ASP LEU SER THR SER ALA GLY
SEQRES 10 A 461 TYR PRO TYR VAL ALA MET GLY LYS LYS LYS ARG ASP ILE
SEQRES 11 A 461 LEU ASN LYS GLN THR ARG ASP THR LYS GLU MET GLN LYS
SEQRES 12 A 461 LEU LEU ASP THR TYR GLY ILE ASN LEU PRO LEU VAL THR
SEQRES 13 A 461 TYR VAL LYS ASP GLU LEU ARG SER LYS THR LYS VAL GLU
SEQRES 14 A 461 GLN GLY LYS SER ARG LEU ILE GLU ALA SER SER LEU ASN
SEQRES 15 A 461 ASP SER VAL ALA MET ARG MET ALA PHE GLY ASN LEU TYR
SEQRES 16 A 461 ALA ALA PHE HIS LYS ASN PRO GLY VAL ILE THR GLY SER
SEQRES 17 A 461 ALA VAL GLY CAS ASP PRO ASP LEU PHE TRP SER LYS ILE
SEQRES 18 A 461 PRO VAL LEU MET GLU GLU LYS LEU PHE ALA PHE ASP TYR
SEQRES 19 A 461 THR GLY TYR ASP ALA SER LEU SER PRO ALA TRP PHE GLU
SEQRES 20 A 461 ALA LEU LYS MET VAL LEU GLU LYS ILE GLY PHE GLY ASP
SEQRES 21 A 461 ARG VAL ASP TYR ILE ASP TYR LEU ASN HIS SER HIS HIS
SEQRES 22 A 461 LEU TYR LYS ASN LYS THR TYR CAS VAL LYS GLY GLY MET
SEQRES 23 A 461 PRO SER ALA PHE SER GLY THR SER ILE PHE ASN SER MET
SEQRES 24 A 461 ILE ASN ASN LEU ILE ILE ARG THR LEU LEU LEU LYS THR
SEQRES 25 A 461 TYR LYS GLY ILE ASP LEU ASP HIS LEU LYS MET ILE ALA
SEQRES 26 A 461 TYR GLY ASP ASP VAL ILE ALA SER TYR PRO HIS GLU VAL
SEQRES 27 A 461 ASP ALA SER LEU LEU ALA GLN SER GLY LYS ASP TYR GLY
SEQRES 28 A 461 LEU THR MET THR PRO ALA ASP LYS SER ALA THR PHE GLU
SEQRES 29 A 461 THR VAL THR TRP GLU ASN VAL THR PHE LEU LYS ARG PHE
SEQRES 30 A 461 PHE ARG ALA ASP GLU LYS TYR PRO PHE LEU ILE HIS PRO
SEQRES 31 A 461 VAL MET PRO MET LYS GLU ILE HIS GLU SER ILE ARG TRP
SEQRES 32 A 461 THR LYS ASP PRO ARG ASN THR GLN ASP HIS VAL ARG SER
SEQRES 33 A 461 LEU CYS LEU LEU ALA TRP HIS ASN GLY GLU GLU GLU TYR
SEQRES 34 A 461 ASN LYS PHE LEU ALA LYS ILE ARG SER VAL PRO ILE GLY
SEQRES 35 A 461 ARG ALA LEU ASP LEU PRO GLU TYR SER THR LEU TYR ASP
SEQRES 36 A 461 ARG TRP LEU ASP SER PHE
MODRES 4NLV CAS A 96 CYS S-(DIMETHYLARSENIC)CYSTEINE
MODRES 4NLV CAS A 212 CYS S-(DIMETHYLARSENIC)CYSTEINE
MODRES 4NLV CAS A 281 CYS S-(DIMETHYLARSENIC)CYSTEINE
HET CAS A 96 9
HET CAS A 212 9
HET CAS A 281 9
HET ACY A 901 4
HET ACY A 902 4
HET ACY A 903 4
HET ACY A 904 4
HET ACY A 905 4
HET ACY A 906 4
HET ACY A 907 4
HET ACY A 908 4
HET 1PE A 909 16
HET 1PE A 910 16
HET NA A 911 1
HETNAM CAS S-(DIMETHYLARSENIC)CYSTEINE
HETNAM ACY ACETIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM NA SODIUM ION
HETSYN 1PE PEG400
FORMUL 1 CAS 3(C5 H12 AS N O2 S)
FORMUL 2 ACY 8(C2 H4 O2)
FORMUL 10 1PE 2(C10 H22 O6)
FORMUL 12 NA NA 1+
FORMUL 13 HOH *214(H2 O)
HELIX 1 1 LYS A 10 GLY A 13 5 4
HELIX 2 2 ASP A 53 SER A 60 1 8
HELIX 3 3 ASP A 71 SER A 87 1 17
HELIX 4 4 CAS A 96 GLY A 103 1 8
HELIX 5 5 PRO A 119 MET A 123 5 5
HELIX 6 6 LYS A 126 ILE A 130 5 5
HELIX 7 7 THR A 138 GLY A 149 1 12
HELIX 8 8 SER A 164 GLN A 170 1 7
HELIX 9 9 SER A 180 ASN A 201 1 22
HELIX 10 10 ASP A 213 TRP A 218 1 6
HELIX 11 11 LYS A 220 MET A 225 1 6
HELIX 12 12 GLY A 236 LEU A 241 1 6
HELIX 13 13 SER A 242 ILE A 256 1 15
HELIX 14 14 PHE A 258 ARG A 261 5 4
HELIX 15 15 VAL A 262 ASN A 269 1 8
HELIX 16 16 GLY A 292 TYR A 313 1 22
HELIX 17 17 ASP A 317 LEU A 321 5 5
HELIX 18 18 ASP A 339 ASP A 349 1 11
HELIX 19 19 ASP A 358 SER A 360 5 3
HELIX 20 20 PRO A 393 ARG A 402 1 10
HELIX 21 21 ASP A 406 ARG A 408 5 3
HELIX 22 22 ASN A 409 TRP A 422 1 14
HELIX 23 23 GLY A 425 ARG A 437 1 13
HELIX 24 24 VAL A 439 ALA A 444 1 6
HELIX 25 25 GLU A 449 ASP A 459 1 11
SHEET 1 A 5 GLU A 2 PRO A 8 0
SHEET 2 A 5 LYS A 278 LYS A 283 -1 O CAS A 281 N GLN A 4
SHEET 3 A 5 HIS A 270 TYR A 275 -1 N TYR A 275 O LYS A 278
SHEET 4 A 5 LEU A 154 VAL A 158 1 N THR A 156 O LEU A 274
SHEET 5 A 5 LEU A 175 ALA A 178 -1 O ILE A 176 N TYR A 157
SHEET 1 B 2 GLU A 26 PRO A 27 0
SHEET 2 B 2 TRP A 403 THR A 404 -1 O THR A 404 N GLU A 26
SHEET 1 C 2 GLU A 39 PRO A 40 0
SHEET 2 C 2 LEU A 162 ARG A 163 -1 O ARG A 163 N GLU A 39
SHEET 1 D 3 LYS A 228 PHE A 230 0
SHEET 2 D 3 ASP A 329 TYR A 334 -1 O TYR A 334 N LYS A 228
SHEET 3 D 3 LYS A 322 TYR A 326 -1 N TYR A 326 O ASP A 329
SHEET 1 E 2 PHE A 232 TYR A 234 0
SHEET 2 E 2 MET A 354 PRO A 356 -1 O THR A 355 N ASP A 233
SHEET 1 F 3 THR A 372 PHE A 373 0
SHEET 2 F 3 ARG A 376 ALA A 380 -1 O ARG A 376 N PHE A 373
SHEET 3 F 3 ILE A 388 VAL A 391 -1 O HIS A 389 N ARG A 379
LINK C MET A 95 N CAS A 96 1555 1555 1.33
LINK C CAS A 96 N LEU A 97 1555 1555 1.33
LINK C GLY A 211 N CAS A 212 1555 1555 1.32
LINK C CAS A 212 N ASP A 213 1555 1555 1.33
LINK C TYR A 280 N CAS A 281 1555 1555 1.32
LINK C CAS A 281 N VAL A 282 1555 1555 1.33
LINK O GLY A 285 NA NA A 911 1555 1555 2.49
LINK O LEU A 268 NA NA A 911 1555 1555 2.53
LINK O GLY A 284 NA NA A 911 1555 1555 2.54
LINK OG SER A 271 NA NA A 911 1555 1555 2.66
LINK NA NA A 911 O HOH A1104 1555 1555 2.69
LINK O ASN A 269 NA NA A 911 1555 1555 2.91
CISPEP 1 TYR A 118 PRO A 119 0 0.10
SITE 1 AC1 5 ILE A 401 TRP A 403 THR A 404 THR A 410
SITE 2 AC1 5 HIS A 413
SITE 1 AC2 1 MET A 189
SITE 1 AC3 4 MET A 392 GLU A 396 SER A 400 HOH A1130
SITE 1 AC4 5 TYR A 334 HIS A 336 PRO A 440 ARG A 443
SITE 2 AC4 5 HOH A1088
SITE 1 AC5 1 ARG A 379
SITE 1 AC6 3 SER A 219 PHE A 461 HOH A1108
SITE 1 AC7 1 PHE A 378
SITE 1 AC8 6 LEU A 268 ASN A 269 SER A 271 GLY A 284
SITE 2 AC8 6 GLY A 285 HOH A1104
CRYST1 128.530 128.530 111.623 90.00 90.00 120.00 P 65 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 0.007780 0.004492 0.000000 0.00000
SCALE2 0.000000 0.008984 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008959 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
