HEADER HYDROLASE 09-MAR-07 2P3N
TITLE THERMOTOGA MARITIMA IMPASE TM1415
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INOSITOL-1-MONOPHOSPHATASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: IMPASE, INOSITOL-1-PHOSPHATASE, I-1-PASE;
COMPND 5 EC: 3.1.3.25;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 STRAIN: MSB8;
SOURCE 5 GENE: SUHB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23A(+)
KEYWDS TETRAMER, INOSITOL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.STIEGLITZ,M.F.ROBERTS,W.LI,B.STEC
REVDAT 6 03-APR-24 2P3N 1 REMARK
REVDAT 5 21-FEB-24 2P3N 1 REMARK LINK
REVDAT 4 13-JUL-11 2P3N 1 VERSN
REVDAT 3 24-FEB-09 2P3N 1 VERSN
REVDAT 2 15-MAY-07 2P3N 1 JRNL
REVDAT 1 24-APR-07 2P3N 0
JRNL AUTH K.A.STIEGLITZ,M.F.ROBERTS,W.LI,B.STEC
JRNL TITL CRYSTAL STRUCTURE OF THE TETRAMERIC INOSITOL 1-PHOSPHATE
JRNL TITL 2 PHOSPHATASE (TM1415) FROM THE HYPERTHERMOPHILE, THERMOTOGA
JRNL TITL 3 MARITIMA.
JRNL REF FEBS J. V. 274 2461 2007
JRNL REFN ISSN 1742-464X
JRNL PMID 17419729
JRNL DOI 10.1111/J.0014-2956.2007.05779.X
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.00
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) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 46203
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) : 0.207
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1815
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 241
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 : 8084
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 302
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.53300
REMARK 3 B22 (A**2) : 9.61600
REMARK 3 B33 (A**2) : -7.08300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.99300
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.367
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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: NULL
REMARK 4
REMARK 4 2P3N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041924.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 110
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46203
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 42.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: HOMOLOGY BUILT MODEL FROM HUMAN, AF AND MJ IMPASES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 400, 0.2M MAGNESIUM SULFATE,
REMARK 280 50MM AMMONIUM SULFATE, 50MM CACODYLATE, PH 8.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 51.93650
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 THR A 32 24.18 -141.78
REMARK 500 PRO A 58 -63.55 -26.87
REMARK 500 ASP A 59 53.60 -105.58
REMARK 500 ASN A 140 129.16 -39.61
REMARK 500 VAL A 154 -104.60 -40.02
REMARK 500 THR A 157 -77.69 -44.25
REMARK 500 GLU A 223 121.47 -30.08
REMARK 500 ASP B 502 -73.25 -127.64
REMARK 500 TRP B 522 123.33 -38.81
REMARK 500 ASP B 526 42.67 -92.56
REMARK 500 THR B 532 18.03 -168.11
REMARK 500 ASP B 536 105.21 -163.26
REMARK 500 ASP B 559 25.57 -73.25
REMARK 500 GLU B 570 -164.84 -58.61
REMARK 500 VAL B 654 -79.58 -19.08
REMARK 500 THR B 657 -78.20 -67.74
REMARK 500 ARG B 696 75.78 61.86
REMARK 500 ASP B 718 -157.90 -81.01
REMARK 500 ILE B 738 19.63 -142.30
REMARK 500 VAL C1154 -78.00 -45.46
REMARK 500 PHE C1156 -71.54 -35.29
REMARK 500 MET C1164 -39.51 -135.68
REMARK 500 ARG C1167 14.50 -140.57
REMARK 500 ARG C1196 68.39 37.88
REMARK 500 THR D1532 43.61 -143.68
REMARK 500 PHE D1557 54.20 -142.86
REMARK 500 ASP D1655 -39.08 -138.63
REMARK 500 THR D1657 -73.74 -37.32
REMARK 500 ARG D1696 109.19 69.84
REMARK 500 GLU D1723 162.67 -43.06
REMARK 500 LYS D1744 -72.73 -58.88
REMARK 500 ILE D1753 -83.23 -120.66
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 MG A1758 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 65 OE1
REMARK 620 2 ASP A 79 OD2 83.8
REMARK 620 3 ILE A 81 O 167.6 97.6
REMARK 620 4 HOH A2128 O 88.5 99.6 103.4
REMARK 620 5 HOH A2189 O 83.8 93.4 83.8 164.1
REMARK 620 6 HOH A2191 O 90.8 174.4 88.1 78.6 87.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1759 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 565 OE1
REMARK 620 2 ASP B 579 OD1 120.4
REMARK 620 3 ILE B 581 O 153.1 84.6
REMARK 620 4 HOH B2120 O 77.1 155.2 82.8
REMARK 620 5 HOH B2176 O 101.5 87.1 88.6 71.2
REMARK 620 6 HOH B2188 O 78.6 102.0 86.9 98.7 169.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1761 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C1065 OE1
REMARK 620 2 ASP C1079 OD2 75.4
REMARK 620 3 ILE C1081 O 160.0 89.1
REMARK 620 4 HOH C2105 O 79.9 89.8 87.6
REMARK 620 5 HOH C2107 O 88.5 85.3 103.0 168.2
REMARK 620 6 HOH C2193 O 109.6 163.7 88.8 106.2 79.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1763 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D1565 OE1
REMARK 620 2 ASP D1579 OD2 79.7
REMARK 620 3 ILE D1581 O 149.0 90.6
REMARK 620 4 HOH D2133 O 110.1 99.8 100.5
REMARK 620 5 HOH D2194 O 68.9 94.9 82.9 164.9
REMARK 620 6 HOH D2195 O 102.5 175.2 89.5 75.5 89.8
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 MG A 1758
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1759
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1763
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P3V RELATED DB: PDB
DBREF 2P3N A 1 256 UNP O33832 SUHB_THEMA 1 256
DBREF 2P3N B 501 756 UNP O33832 SUHB_THEMA 1 256
DBREF 2P3N C 1001 1256 UNP O33832 SUHB_THEMA 1 256
DBREF 2P3N D 1501 1756 UNP O33832 SUHB_THEMA 1 256
SEQRES 1 A 256 MET ASP ARG LEU ASP PHE SER ILE LYS LEU LEU ARG LYS
SEQRES 2 A 256 VAL GLY HIS LEU LEU MET ILE HIS TRP GLY ARG VAL ASP
SEQRES 3 A 256 ASN VAL GLU LYS LYS THR GLY PHE LYS ASP ILE VAL THR
SEQRES 4 A 256 GLU ILE ASP ARG GLU ALA GLN ARG MET ILE VAL ASP GLU
SEQRES 5 A 256 ILE ARG LYS PHE PHE PRO ASP GLU ASN ILE MET ALA GLU
SEQRES 6 A 256 GLU GLY ILE PHE GLU LYS GLY ASP ARG LEU TRP ILE ILE
SEQRES 7 A 256 ASP PRO ILE ASP GLY THR ILE ASN PHE VAL HIS GLY LEU
SEQRES 8 A 256 PRO ASN PHE SER ILE SER LEU ALA TYR VAL GLU ASN GLY
SEQRES 9 A 256 GLU VAL LYS LEU GLY VAL VAL HIS ALA PRO ALA LEU ASN
SEQRES 10 A 256 GLU THR LEU TYR ALA GLU GLU GLY SER GLY ALA PHE PHE
SEQRES 11 A 256 ASN GLY GLU ARG ILE ARG VAL SER GLU ASN ALA SER LEU
SEQRES 12 A 256 GLU GLU CYS VAL GLY SER THR GLY SER TYR VAL ASP PHE
SEQRES 13 A 256 THR GLY LYS PHE ILE GLU ARG MET GLU LYS ARG THR ARG
SEQRES 14 A 256 ARG ILE ARG ILE LEU GLY SER ALA ALA LEU ASN ALA ALA
SEQRES 15 A 256 TYR VAL GLY ALA GLY ARG VAL ASP PHE PHE VAL THR TRP
SEQRES 16 A 256 ARG ILE ASN PRO TRP ASP ILE ALA ALA GLY LEU ILE ILE
SEQRES 17 A 256 VAL LYS GLU ALA GLY GLY MET VAL THR ASP PHE SER GLY
SEQRES 18 A 256 LYS GLU ALA ASN ALA PHE SER LYS ASN PHE ILE PHE SER
SEQRES 19 A 256 ASN GLY LEU ILE HIS ASP GLU VAL VAL LYS VAL VAL ASN
SEQRES 20 A 256 GLU VAL VAL GLU GLU ILE GLY GLY LYS
SEQRES 1 B 256 MET ASP ARG LEU ASP PHE SER ILE LYS LEU LEU ARG LYS
SEQRES 2 B 256 VAL GLY HIS LEU LEU MET ILE HIS TRP GLY ARG VAL ASP
SEQRES 3 B 256 ASN VAL GLU LYS LYS THR GLY PHE LYS ASP ILE VAL THR
SEQRES 4 B 256 GLU ILE ASP ARG GLU ALA GLN ARG MET ILE VAL ASP GLU
SEQRES 5 B 256 ILE ARG LYS PHE PHE PRO ASP GLU ASN ILE MET ALA GLU
SEQRES 6 B 256 GLU GLY ILE PHE GLU LYS GLY ASP ARG LEU TRP ILE ILE
SEQRES 7 B 256 ASP PRO ILE ASP GLY THR ILE ASN PHE VAL HIS GLY LEU
SEQRES 8 B 256 PRO ASN PHE SER ILE SER LEU ALA TYR VAL GLU ASN GLY
SEQRES 9 B 256 GLU VAL LYS LEU GLY VAL VAL HIS ALA PRO ALA LEU ASN
SEQRES 10 B 256 GLU THR LEU TYR ALA GLU GLU GLY SER GLY ALA PHE PHE
SEQRES 11 B 256 ASN GLY GLU ARG ILE ARG VAL SER GLU ASN ALA SER LEU
SEQRES 12 B 256 GLU GLU CYS VAL GLY SER THR GLY SER TYR VAL ASP PHE
SEQRES 13 B 256 THR GLY LYS PHE ILE GLU ARG MET GLU LYS ARG THR ARG
SEQRES 14 B 256 ARG ILE ARG ILE LEU GLY SER ALA ALA LEU ASN ALA ALA
SEQRES 15 B 256 TYR VAL GLY ALA GLY ARG VAL ASP PHE PHE VAL THR TRP
SEQRES 16 B 256 ARG ILE ASN PRO TRP ASP ILE ALA ALA GLY LEU ILE ILE
SEQRES 17 B 256 VAL LYS GLU ALA GLY GLY MET VAL THR ASP PHE SER GLY
SEQRES 18 B 256 LYS GLU ALA ASN ALA PHE SER LYS ASN PHE ILE PHE SER
SEQRES 19 B 256 ASN GLY LEU ILE HIS ASP GLU VAL VAL LYS VAL VAL ASN
SEQRES 20 B 256 GLU VAL VAL GLU GLU ILE GLY GLY LYS
SEQRES 1 C 256 MET ASP ARG LEU ASP PHE SER ILE LYS LEU LEU ARG LYS
SEQRES 2 C 256 VAL GLY HIS LEU LEU MET ILE HIS TRP GLY ARG VAL ASP
SEQRES 3 C 256 ASN VAL GLU LYS LYS THR GLY PHE LYS ASP ILE VAL THR
SEQRES 4 C 256 GLU ILE ASP ARG GLU ALA GLN ARG MET ILE VAL ASP GLU
SEQRES 5 C 256 ILE ARG LYS PHE PHE PRO ASP GLU ASN ILE MET ALA GLU
SEQRES 6 C 256 GLU GLY ILE PHE GLU LYS GLY ASP ARG LEU TRP ILE ILE
SEQRES 7 C 256 ASP PRO ILE ASP GLY THR ILE ASN PHE VAL HIS GLY LEU
SEQRES 8 C 256 PRO ASN PHE SER ILE SER LEU ALA TYR VAL GLU ASN GLY
SEQRES 9 C 256 GLU VAL LYS LEU GLY VAL VAL HIS ALA PRO ALA LEU ASN
SEQRES 10 C 256 GLU THR LEU TYR ALA GLU GLU GLY SER GLY ALA PHE PHE
SEQRES 11 C 256 ASN GLY GLU ARG ILE ARG VAL SER GLU ASN ALA SER LEU
SEQRES 12 C 256 GLU GLU CYS VAL GLY SER THR GLY SER TYR VAL ASP PHE
SEQRES 13 C 256 THR GLY LYS PHE ILE GLU ARG MET GLU LYS ARG THR ARG
SEQRES 14 C 256 ARG ILE ARG ILE LEU GLY SER ALA ALA LEU ASN ALA ALA
SEQRES 15 C 256 TYR VAL GLY ALA GLY ARG VAL ASP PHE PHE VAL THR TRP
SEQRES 16 C 256 ARG ILE ASN PRO TRP ASP ILE ALA ALA GLY LEU ILE ILE
SEQRES 17 C 256 VAL LYS GLU ALA GLY GLY MET VAL THR ASP PHE SER GLY
SEQRES 18 C 256 LYS GLU ALA ASN ALA PHE SER LYS ASN PHE ILE PHE SER
SEQRES 19 C 256 ASN GLY LEU ILE HIS ASP GLU VAL VAL LYS VAL VAL ASN
SEQRES 20 C 256 GLU VAL VAL GLU GLU ILE GLY GLY LYS
SEQRES 1 D 256 MET ASP ARG LEU ASP PHE SER ILE LYS LEU LEU ARG LYS
SEQRES 2 D 256 VAL GLY HIS LEU LEU MET ILE HIS TRP GLY ARG VAL ASP
SEQRES 3 D 256 ASN VAL GLU LYS LYS THR GLY PHE LYS ASP ILE VAL THR
SEQRES 4 D 256 GLU ILE ASP ARG GLU ALA GLN ARG MET ILE VAL ASP GLU
SEQRES 5 D 256 ILE ARG LYS PHE PHE PRO ASP GLU ASN ILE MET ALA GLU
SEQRES 6 D 256 GLU GLY ILE PHE GLU LYS GLY ASP ARG LEU TRP ILE ILE
SEQRES 7 D 256 ASP PRO ILE ASP GLY THR ILE ASN PHE VAL HIS GLY LEU
SEQRES 8 D 256 PRO ASN PHE SER ILE SER LEU ALA TYR VAL GLU ASN GLY
SEQRES 9 D 256 GLU VAL LYS LEU GLY VAL VAL HIS ALA PRO ALA LEU ASN
SEQRES 10 D 256 GLU THR LEU TYR ALA GLU GLU GLY SER GLY ALA PHE PHE
SEQRES 11 D 256 ASN GLY GLU ARG ILE ARG VAL SER GLU ASN ALA SER LEU
SEQRES 12 D 256 GLU GLU CYS VAL GLY SER THR GLY SER TYR VAL ASP PHE
SEQRES 13 D 256 THR GLY LYS PHE ILE GLU ARG MET GLU LYS ARG THR ARG
SEQRES 14 D 256 ARG ILE ARG ILE LEU GLY SER ALA ALA LEU ASN ALA ALA
SEQRES 15 D 256 TYR VAL GLY ALA GLY ARG VAL ASP PHE PHE VAL THR TRP
SEQRES 16 D 256 ARG ILE ASN PRO TRP ASP ILE ALA ALA GLY LEU ILE ILE
SEQRES 17 D 256 VAL LYS GLU ALA GLY GLY MET VAL THR ASP PHE SER GLY
SEQRES 18 D 256 LYS GLU ALA ASN ALA PHE SER LYS ASN PHE ILE PHE SER
SEQRES 19 D 256 ASN GLY LEU ILE HIS ASP GLU VAL VAL LYS VAL VAL ASN
SEQRES 20 D 256 GLU VAL VAL GLU GLU ILE GLY GLY LYS
HET MG A1758 1
HET MG B1759 1
HET MG C1761 1
HET MG D1763 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG 4(MG 2+)
FORMUL 9 HOH *302(H2 O)
HELIX 1 1 MET A 1 TRP A 22 1 22
HELIX 2 2 THR A 39 PHE A 57 1 19
HELIX 3 3 GLY A 83 GLY A 90 1 8
HELIX 4 4 SER A 142 GLU A 145 5 4
HELIX 5 5 ASP A 155 GLU A 165 1 11
HELIX 6 6 SER A 176 ALA A 186 1 11
HELIX 7 7 ASN A 198 ALA A 212 1 15
HELIX 8 8 ILE A 238 GLY A 254 1 17
HELIX 9 9 ASP B 502 TRP B 522 1 21
HELIX 10 10 THR B 539 PHE B 557 1 19
HELIX 11 11 GLY B 583 GLY B 590 1 8
HELIX 12 12 SER B 642 GLU B 645 5 4
HELIX 13 13 THR B 657 ARG B 663 1 7
HELIX 14 14 SER B 676 ALA B 686 1 11
HELIX 15 15 ASN B 698 ASP B 701 5 4
HELIX 16 16 ILE B 702 ALA B 712 1 11
HELIX 17 17 ILE B 738 GLU B 748 1 11
HELIX 18 18 MET C 1001 TRP C 1022 1 22
HELIX 19 19 THR C 1039 PHE C 1057 1 19
HELIX 20 20 GLY C 1083 GLY C 1090 1 8
HELIX 21 21 SER C 1142 GLU C 1145 5 4
HELIX 22 22 ASP C 1155 LYS C 1166 1 12
HELIX 23 23 SER C 1176 ALA C 1186 1 11
HELIX 24 24 ASN C 1198 ALA C 1212 1 15
HELIX 25 25 ILE C 1238 GLY C 1254 1 17
HELIX 26 26 ASP D 1502 TRP D 1522 1 21
HELIX 27 27 GLU D 1540 PHE D 1557 1 18
HELIX 28 28 GLY D 1583 GLY D 1590 1 8
HELIX 29 29 SER D 1642 GLU D 1645 5 4
HELIX 30 30 ASP D 1655 LYS D 1666 1 12
HELIX 31 31 SER D 1676 ALA D 1686 1 11
HELIX 32 32 ASN D 1698 ALA D 1712 1 15
HELIX 33 33 ILE D 1738 GLU D 1752 1 15
SHEET 1 A 2 GLU A 29 LYS A 30 0
SHEET 2 A 2 ILE A 37 VAL A 38 -1 O VAL A 38 N GLU A 29
SHEET 1 B 7 ASN A 61 ALA A 64 0
SHEET 2 B 7 ARG A 74 ASP A 82 1 O TRP A 76 N MET A 63
SHEET 3 B 7 SER A 95 GLU A 102 -1 O SER A 95 N ASP A 82
SHEET 4 B 7 GLU A 105 ALA A 113 -1 O GLU A 105 N GLU A 102
SHEET 5 B 7 GLU A 118 GLU A 123 -1 O LEU A 120 N VAL A 111
SHEET 6 B 7 GLY A 127 PHE A 130 -1 O PHE A 129 N TYR A 121
SHEET 7 B 7 GLU A 133 ARG A 134 -1 O GLU A 133 N PHE A 130
SHEET 1 C 5 ARG A 170 ARG A 172 0
SHEET 2 C 5 VAL A 147 THR A 150 1 N GLY A 148 O ARG A 172
SHEET 3 C 5 PHE A 191 TRP A 195 1 O PHE A 191 N SER A 149
SHEET 4 C 5 ASN A 230 SER A 234 -1 O PHE A 233 N PHE A 192
SHEET 5 C 5 MET A 215 THR A 217 -1 N MET A 215 O SER A 234
SHEET 1 D 2 GLU B 529 LYS B 530 0
SHEET 2 D 2 ILE B 537 VAL B 538 -1 O VAL B 538 N GLU B 529
SHEET 1 E 7 MET B 563 ALA B 564 0
SHEET 2 E 7 ARG B 574 ASP B 582 1 O TRP B 576 N MET B 563
SHEET 3 E 7 SER B 595 GLU B 602 -1 O ALA B 599 N ILE B 577
SHEET 4 E 7 GLU B 605 ALA B 613 -1 O GLU B 605 N GLU B 602
SHEET 5 E 7 GLU B 618 GLU B 623 -1 O LEU B 620 N VAL B 611
SHEET 6 E 7 GLY B 627 PHE B 630 -1 O PHE B 629 N TYR B 621
SHEET 7 E 7 GLU B 633 ARG B 634 -1 O GLU B 633 N PHE B 630
SHEET 1 F 5 ARG B 670 ARG B 672 0
SHEET 2 F 5 VAL B 647 THR B 650 1 N GLY B 648 O ARG B 672
SHEET 3 F 5 PHE B 691 THR B 694 1 O VAL B 693 N SER B 649
SHEET 4 F 5 PHE B 731 SER B 734 -1 O PHE B 733 N PHE B 692
SHEET 5 F 5 MET B 715 THR B 717 -1 N MET B 715 O SER B 734
SHEET 1 G 2 GLU C1029 LYS C1030 0
SHEET 2 G 2 ILE C1037 VAL C1038 -1 O VAL C1038 N GLU C1029
SHEET 1 H 7 ASN C1061 ALA C1064 0
SHEET 2 H 7 ARG C1074 ASP C1082 1 O ILE C1078 N MET C1063
SHEET 3 H 7 SER C1095 GLU C1102 -1 O SER C1095 N ASP C1082
SHEET 4 H 7 GLU C1105 ALA C1113 -1 O LYS C1107 N TYR C1100
SHEET 5 H 7 GLU C1118 GLU C1123 -1 O LEU C1120 N VAL C1111
SHEET 6 H 7 ALA C1128 PHE C1130 -1 O PHE C1129 N TYR C1121
SHEET 7 H 7 GLU C1133 ILE C1135 -1 O ILE C1135 N ALA C1128
SHEET 1 I 5 ARG C1170 ARG C1172 0
SHEET 2 I 5 VAL C1147 THR C1150 1 N GLY C1148 O ARG C1172
SHEET 3 I 5 PHE C1191 THR C1194 1 O VAL C1193 N SER C1149
SHEET 4 I 5 PHE C1231 SER C1234 -1 O PHE C1233 N PHE C1192
SHEET 5 I 5 MET C1215 THR C1217 -1 N MET C1215 O SER C1234
SHEET 1 J 2 VAL D1528 LYS D1530 0
SHEET 2 J 2 ILE D1537 THR D1539 -1 O VAL D1538 N GLU D1529
SHEET 1 K 8 ILE D1568 PHE D1569 0
SHEET 2 K 8 ASN D1561 ALA D1564 -1 N ALA D1564 O ILE D1568
SHEET 3 K 8 ARG D1574 ASP D1582 1 O ILE D1578 N MET D1563
SHEET 4 K 8 SER D1595 GLU D1602 -1 O SER D1595 N ASP D1582
SHEET 5 K 8 GLU D1605 ALA D1613 -1 O HIS D1612 N ILE D1596
SHEET 6 K 8 GLU D1618 GLU D1623 -1 O LEU D1620 N VAL D1611
SHEET 7 K 8 GLY D1627 PHE D1630 -1 O PHE D1629 N TYR D1621
SHEET 8 K 8 GLU D1633 ILE D1635 -1 O GLU D1633 N PHE D1630
SHEET 1 L 2 VAL D1647 SER D1649 0
SHEET 2 L 2 ARG D1670 ARG D1672 1 O ARG D1672 N GLY D1648
SHEET 1 M 3 PHE D1691 TRP D1695 0
SHEET 2 M 3 ASN D1730 SER D1734 -1 O PHE D1733 N PHE D1692
SHEET 3 M 3 MET D1715 THR D1717 -1 N THR D1717 O ILE D1732
LINK OE1 GLU A 65 MG MG A1758 1555 1555 2.10
LINK OD2 ASP A 79 MG MG A1758 1555 1555 2.17
LINK O ILE A 81 MG MG A1758 1555 1555 2.06
LINK MG MG A1758 O HOH A2128 1555 1555 2.11
LINK MG MG A1758 O HOH A2189 1555 1555 2.26
LINK MG MG A1758 O HOH A2191 1555 1555 1.94
LINK OE1 GLU B 565 MG MG B1759 1555 1555 2.19
LINK OD1 ASP B 579 MG MG B1759 1555 1555 2.15
LINK O ILE B 581 MG MG B1759 1555 1555 2.05
LINK MG MG B1759 O HOH B2120 1555 1555 2.14
LINK MG MG B1759 O HOH B2176 1555 1555 2.36
LINK MG MG B1759 O HOH B2188 1555 1555 2.19
LINK OE1 GLU C1065 MG MG C1761 1555 1555 2.10
LINK OD2 ASP C1079 MG MG C1761 1555 1555 2.10
LINK O ILE C1081 MG MG C1761 1555 1555 2.17
LINK MG MG C1761 O HOH C2105 1555 1555 2.01
LINK MG MG C1761 O HOH C2107 1555 1555 2.20
LINK MG MG C1761 O HOH C2193 1555 1555 1.93
LINK OE1 GLU D1565 MG MG D1763 1555 1555 2.14
LINK OD2 ASP D1579 MG MG D1763 1555 1555 2.12
LINK O ILE D1581 MG MG D1763 1555 1555 2.11
LINK MG MG D1763 O HOH D2133 1555 1555 2.19
LINK MG MG D1763 O HOH D2194 1555 1555 2.24
LINK MG MG D1763 O HOH D2195 1555 1555 2.07
SITE 1 AC1 7 GLU A 65 ASP A 79 ILE A 81 ASP A 82
SITE 2 AC1 7 HOH A2128 HOH A2189 HOH A2191
SITE 1 AC2 6 GLU B 565 ASP B 579 ILE B 581 HOH B2120
SITE 2 AC2 6 HOH B2176 HOH B2188
SITE 1 AC3 6 GLU C1065 ASP C1079 ILE C1081 HOH C2105
SITE 2 AC3 6 HOH C2107 HOH C2193
SITE 1 AC4 6 GLU D1565 ASP D1579 ILE D1581 HOH D2133
SITE 2 AC4 6 HOH D2194 HOH D2195
CRYST1 62.024 103.873 80.512 90.00 101.93 90.00 P 1 21 1 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 0.016123 0.000000 0.003406 0.00000
SCALE2 0.000000 0.009627 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012695 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
