HEADER LIGAND BINDING PROTEIN 10-APR-07 2PH1
TITLE CRYSTAL STRUCTURE OF NUCLEOTIDE-BINDING PROTEIN AF2382 FROM
TITLE 2 ARCHAEOGLOBUS FULGIDUS, NORTHEAST STRUCTURAL GENOMICS TARGET GR165
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEOTIDE-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS DSM 4304;
SOURCE 3 ORGANISM_TAXID: 224325;
SOURCE 4 STRAIN: DSM 4304, VC-16, JCM 9628, NBRC 100126;
SOURCE 5 ATCC: 49558;
SOURCE 6 GENE: AF_2382;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: BL21;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, LIGAND
KEYWDS 3 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,M.ABASHIDZE,J.SEETHARAMAN,H.JANJUA,Y.FANG,R.XIAO,J.LIU,
AUTHOR 2 M.C.BARAN,T.B.ACTON,G.T.MONTELIONE,J.F.HUNT,L.TONG,NORTHEAST
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 18-OCT-17 2PH1 1 REMARK
REVDAT 3 13-JUL-11 2PH1 1 VERSN
REVDAT 2 24-FEB-09 2PH1 1 VERSN
REVDAT 1 24-APR-07 2PH1 0
JRNL AUTH F.FOROUHAR,M.ABASHIDZE,J.SEETHARAMAN,H.JANJUA,Y.FANG,R.XIAO,
JRNL AUTH 2 J.LIU,M.C.BARAN,T.B.ACTON,G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF NUCLEOTIDE-BINDING PROTEIN AF2382 FROM
JRNL TITL 2 ARCHAEOGLOBUS FULGIDUS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 112851.270
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 12442
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) : 0.217
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1211
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.80
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 948
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 104
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.035
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -15.84000
REMARK 3 B22 (A**2) : 14.77000
REMARK 3 B33 (A**2) : 1.07000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.46
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 24.76
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: XTALVIEW HAS ALSO BEEN USED IN THE
REMARK 3 REFINEMENT. THE FRIEDEL PAIRS WERE USED FOR PHASING
REMARK 4
REMARK 4 2PH1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13903
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 49.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.41300
REMARK 200 R SYM FOR SHELL (I) : 0.34400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.080
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 20 MM TRIS-HCL PH
REMARK 280 7.5, 100 MM SODIUM CHLORIDE, 5 MM DTT. PRECIPITANT SOLUTION: 100
REMARK 280 MM HEPES PH 7.5, 55% MPD, MICROBATCH UNDER OIL, TEMPERATURE 293K
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 33.46850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.09300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.46850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.09300
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 66.93700
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 ZN ZN A 301 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 MSE A 1
REMARK 465 GLN A 2
REMARK 465 LYS A 3
REMARK 465 SER A 251
REMARK 465 ALA A 252
REMARK 465 PRO A 253
REMARK 465 PHE A 254
REMARK 465 LEU A 255
REMARK 465 GLU A 256
REMARK 465 HIS A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
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 ARG A 109 -155.04 -64.62
REMARK 500 LEU A 112 23.28 -77.69
REMARK 500 GLU A 128 35.92 -93.06
REMARK 500 GLU A 164 41.57 -99.24
REMARK 500 THR A 180 21.94 -150.10
REMARK 500 ASN A 219 65.69 35.27
REMARK 500 GLU A 245 42.45 -83.30
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 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 199 SG
REMARK 620 2 CYS A 196 SG 113.3
REMARK 620 3 CYS A 199 SG 98.3 119.3
REMARK 620 4 CYS A 196 SG 115.4 100.0 111.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GR165 RELATED DB: TARGETDB
DBREF 2PH1 A 1 254 UNP O30288 O30288_ARCFU 1 254
SEQADV 2PH1 MSE A 1 UNP O30288 MET 1 MODIFIED RESIDUE
SEQADV 2PH1 MSE A 24 UNP O30288 MET 24 MODIFIED RESIDUE
SEQADV 2PH1 MSE A 93 UNP O30288 MET 93 MODIFIED RESIDUE
SEQADV 2PH1 MSE A 95 UNP O30288 MET 95 MODIFIED RESIDUE
SEQADV 2PH1 MSE A 116 UNP O30288 MET 116 MODIFIED RESIDUE
SEQADV 2PH1 MSE A 148 UNP O30288 MET 148 MODIFIED RESIDUE
SEQADV 2PH1 MSE A 176 UNP O30288 MET 176 MODIFIED RESIDUE
SEQADV 2PH1 MSE A 191 UNP O30288 MET 191 MODIFIED RESIDUE
SEQADV 2PH1 LEU A 255 UNP O30288 CLONING ARTIFACT
SEQADV 2PH1 GLU A 256 UNP O30288 CLONING ARTIFACT
SEQADV 2PH1 HIS A 257 UNP O30288 CLONING ARTIFACT
SEQADV 2PH1 HIS A 258 UNP O30288 CLONING ARTIFACT
SEQADV 2PH1 HIS A 259 UNP O30288 CLONING ARTIFACT
SEQADV 2PH1 HIS A 260 UNP O30288 CLONING ARTIFACT
SEQADV 2PH1 HIS A 261 UNP O30288 CLONING ARTIFACT
SEQADV 2PH1 HIS A 262 UNP O30288 CLONING ARTIFACT
SEQRES 1 A 262 MSE GLN LYS ARG VAL THR ASP GLU GLU ILE LYS GLU ARG
SEQRES 2 A 262 LEU GLY LYS ILE LYS SER ARG ILE ALA VAL MSE SER GLY
SEQRES 3 A 262 LYS GLY GLY VAL GLY LYS SER THR VAL THR ALA LEU LEU
SEQRES 4 A 262 ALA VAL HIS TYR ALA ARG GLN GLY LYS LYS VAL GLY ILE
SEQRES 5 A 262 LEU ASP ALA ASP PHE LEU GLY PRO SER ILE PRO ILE LEU
SEQRES 6 A 262 PHE GLY LEU ARG ASN ALA ARG ILE ALA VAL SER ALA GLU
SEQRES 7 A 262 GLY LEU GLU PRO VAL LEU THR GLN LYS TYR GLY ILE LYS
SEQRES 8 A 262 VAL MSE SER MSE GLN PHE LEU LEU PRO LYS GLU ASN THR
SEQRES 9 A 262 PRO VAL ILE TRP ARG GLY PRO LEU ILE ALA GLY MSE ILE
SEQRES 10 A 262 ARG GLU PHE LEU GLY ARG VAL ALA TRP GLY GLU LEU ASP
SEQRES 11 A 262 HIS LEU LEU ILE ASP LEU PRO PRO GLY THR GLY ASP ALA
SEQRES 12 A 262 PRO LEU THR VAL MSE GLN ASP ALA LYS PRO THR GLY VAL
SEQRES 13 A 262 VAL VAL VAL SER THR PRO GLN GLU LEU THR ALA VAL ILE
SEQRES 14 A 262 VAL GLU LYS ALA ILE ASN MSE ALA GLU GLU THR ASN THR
SEQRES 15 A 262 SER VAL LEU GLY LEU VAL GLU ASN MSE SER TYR PHE VAL
SEQRES 16 A 262 CYS PRO ASN CYS GLY HIS LYS SER TYR ILE PHE GLY GLU
SEQRES 17 A 262 GLY LYS GLY GLU SER LEU ALA LYS LYS TYR ASN ILE GLY
SEQRES 18 A 262 PHE PHE THR SER ILE PRO ILE GLU GLU GLU LEU ILE LYS
SEQRES 19 A 262 LEU ALA ASP SER GLY ARG ILE GLU GLU TYR GLU LYS ASP
SEQRES 20 A 262 TRP PHE GLU SER ALA PRO PHE LEU GLU HIS HIS HIS HIS
SEQRES 21 A 262 HIS HIS
MODRES 2PH1 MSE A 24 MET SELENOMETHIONINE
MODRES 2PH1 MSE A 93 MET SELENOMETHIONINE
MODRES 2PH1 MSE A 95 MET SELENOMETHIONINE
MODRES 2PH1 MSE A 116 MET SELENOMETHIONINE
MODRES 2PH1 MSE A 148 MET SELENOMETHIONINE
MODRES 2PH1 MSE A 176 MET SELENOMETHIONINE
MODRES 2PH1 MSE A 191 MET SELENOMETHIONINE
HET MSE A 24 8
HET MSE A 93 8
HET MSE A 95 8
HET MSE A 116 8
HET MSE A 148 8
HET MSE A 176 8
HET MSE A 191 8
HET ZN A 301 1
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 ZN ZN 2+
FORMUL 3 HOH *37(H2 O)
HELIX 1 1 THR A 6 GLY A 15 1 10
HELIX 2 2 GLY A 31 GLN A 46 1 16
HELIX 3 3 PRO A 60 PHE A 66 1 7
HELIX 4 4 SER A 94 LEU A 99 5 6
HELIX 5 5 GLY A 110 ARG A 123 1 14
HELIX 6 6 ASP A 142 LYS A 152 1 11
HELIX 7 7 THR A 166 GLU A 179 1 14
HELIX 8 8 LYS A 210 TYR A 218 1 9
HELIX 9 9 GLU A 229 SER A 238 1 10
HELIX 10 10 ARG A 240 TYR A 244 5 5
SHEET 1 A 8 VAL A 83 LEU A 84 0
SHEET 2 A 8 LYS A 91 MSE A 93 -1 O VAL A 92 N VAL A 83
SHEET 3 A 8 VAL A 50 ASP A 54 1 N ASP A 54 O MSE A 93
SHEET 4 A 8 HIS A 131 ASP A 135 1 O LEU A 133 N GLY A 51
SHEET 5 A 8 ARG A 20 MSE A 24 1 N VAL A 23 O ILE A 134
SHEET 6 A 8 GLY A 155 SER A 160 1 O VAL A 157 N ALA A 22
SHEET 7 A 8 VAL A 184 GLU A 189 1 O LEU A 185 N VAL A 156
SHEET 8 A 8 PHE A 222 SER A 225 1 O THR A 224 N GLU A 189
SHEET 1 B 2 ALA A 74 SER A 76 0
SHEET 2 B 2 GLY A 79 GLU A 81 -1 O GLU A 81 N ALA A 74
SHEET 1 C 2 PHE A 194 VAL A 195 0
SHEET 2 C 2 LYS A 202 SER A 203 -1 O SER A 203 N PHE A 194
LINK C VAL A 23 N MSE A 24 1555 1555 1.33
LINK C MSE A 24 N SER A 25 1555 1555 1.33
LINK C VAL A 92 N MSE A 93 1555 1555 1.32
LINK C MSE A 93 N SER A 94 1555 1555 1.33
LINK C SER A 94 N MSE A 95 1555 1555 1.33
LINK C MSE A 95 N GLN A 96 1555 1555 1.33
LINK C GLY A 115 N MSE A 116 1555 1555 1.33
LINK C MSE A 116 N ILE A 117 1555 1555 1.32
LINK C VAL A 147 N MSE A 148 1555 1555 1.32
LINK C MSE A 148 N GLN A 149 1555 1555 1.33
LINK C ASN A 175 N MSE A 176 1555 1555 1.33
LINK C MSE A 176 N ALA A 177 1555 1555 1.33
LINK C ASN A 190 N MSE A 191 1555 1555 1.33
LINK C MSE A 191 N SER A 192 1555 1555 1.32
LINK ZN ZN A 301 SG CYS A 199 1555 1555 2.55
LINK ZN ZN A 301 SG CYS A 196 1555 1555 2.54
LINK ZN ZN A 301 SG CYS A 199 1555 2655 2.53
LINK ZN ZN A 301 SG CYS A 196 1555 2655 2.62
SITE 1 AC1 2 CYS A 196 CYS A 199
CRYST1 66.937 78.186 49.597 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 0.014939 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012790 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
