HEADER HYDROLASE 16-OCT-13 4N81
TITLE ANOTHER FLEXIBLE REGION AT THE ACTIVE SITE OF AN INOSITOL
TITLE 2 MONOPHOSPHATASE FROM ZYMOMONAS MOBILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INOSITOL MONOPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IMPASE/FBPASE;
COMPND 5 EC: 3.1.3.25;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZYMOMONAS MOBILIS;
SOURCE 3 ORGANISM_TAXID: 264203;
SOURCE 4 STRAIN: ZM4;
SOURCE 5 GENE: ZMO1518;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.HWANG,S.Y.PARK,J.S.KIM
REVDAT 2 20-MAR-24 4N81 1 REMARK
REVDAT 1 01-OCT-14 4N81 0
JRNL AUTH H.J.HWANG,S.Y.PARK,J.S.KIM
JRNL TITL CRYSTAL STRUCTURE OF CBBF FROM ZYMOMONAS MOBILIS AND ITS
JRNL TITL 2 FUNCTIONAL IMPLICATION
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 445 78 2014
JRNL REFN ISSN 0006-291X
JRNL PMID 24491569
JRNL DOI 10.1016/J.BBRC.2014.01.152
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 28577
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2832
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 39.3030 - 5.1561 1.00 1372 159 0.1734 0.1826
REMARK 3 2 5.1561 - 4.0939 1.00 1338 137 0.1310 0.1556
REMARK 3 3 4.0939 - 3.5768 1.00 1317 121 0.1326 0.1691
REMARK 3 4 3.5768 - 3.2500 1.00 1313 137 0.1438 0.1747
REMARK 3 5 3.2500 - 3.0171 1.00 1288 139 0.1544 0.1719
REMARK 3 6 3.0171 - 2.8393 1.00 1282 154 0.1508 0.1933
REMARK 3 7 2.8393 - 2.6971 1.00 1263 164 0.1526 0.1725
REMARK 3 8 2.6971 - 2.5797 1.00 1263 159 0.1468 0.1721
REMARK 3 9 2.5797 - 2.4804 1.00 1303 136 0.1469 0.1748
REMARK 3 10 2.4804 - 2.3949 1.00 1252 147 0.1368 0.1939
REMARK 3 11 2.3949 - 2.3200 1.00 1291 134 0.1467 0.1979
REMARK 3 12 2.3200 - 2.2537 1.00 1257 157 0.1429 0.1901
REMARK 3 13 2.2537 - 2.1944 1.00 1269 150 0.1387 0.1745
REMARK 3 14 2.1944 - 2.1408 1.00 1257 129 0.1325 0.1587
REMARK 3 15 2.1408 - 2.0922 1.00 1299 128 0.1421 0.1768
REMARK 3 16 2.0922 - 2.0476 1.00 1273 130 0.1380 0.2028
REMARK 3 17 2.0476 - 2.0067 1.00 1288 133 0.1467 0.1905
REMARK 3 18 2.0067 - 1.9688 1.00 1269 133 0.1534 0.1920
REMARK 3 19 1.9688 - 1.9337 1.00 1269 130 0.1550 0.2173
REMARK 3 20 1.9337 - 1.9009 1.00 1282 155 0.1642 0.2279
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.45
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 : 0.019 2032
REMARK 3 ANGLE : 1.721 2757
REMARK 3 CHIRALITY : 0.150 302
REMARK 3 PLANARITY : 0.011 365
REMARK 3 DIHEDRAL : 13.866 751
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4740 39.9509 27.5964
REMARK 3 T TENSOR
REMARK 3 T11: 0.1095 T22: 0.1557
REMARK 3 T33: 0.1016 T12: 0.0004
REMARK 3 T13: -0.0240 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.3151 L22: 1.6580
REMARK 3 L33: 0.7318 L12: -0.6558
REMARK 3 L13: -0.3685 L23: 0.0822
REMARK 3 S TENSOR
REMARK 3 S11: 0.0743 S12: 0.2606 S13: -0.0522
REMARK 3 S21: -0.2046 S22: -0.0643 S23: 0.1116
REMARK 3 S31: -0.0012 S32: -0.0962 S33: -0.0237
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 4N81 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082868.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28603
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 60.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11%(W/V) POLYETHYLENE GLYCOL 4000,
REMARK 280 0.2M LITHIUM SULFATE, 0.1M TRIS-HCL, PH 8.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 50.18267
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 25.09133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.09133
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 50.18267
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: 3530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 75.27400
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 HOH A 622 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 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 71
REMARK 465 MET A 72
REMARK 465 GLY A 73
REMARK 465 VAL A 74
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 SER A 75 OG
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 O HOH A 553 O HOH A 661 2.03
REMARK 500 O HOH A 485 O HOH A 606 2.07
REMARK 500 O HOH A 525 O HOH A 612 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 605 O HOH A 605 4556 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 198 CB CYS A 198 SG -0.114
REMARK 500 GLU A 219 CD GLU A 219 OE2 0.099
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 PRO A 77 -159.05 -134.99
REMARK 500 ASP A 78 -18.10 70.23
REMARK 500 ALA A 99 39.68 -94.93
REMARK 500 ASP A 186 -127.29 53.12
REMARK 500
REMARK 500 REMARK: NULL
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 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N89 RELATED DB: PDB
DBREF 4N81 A 1 259 UNP Q5NMB8 Q5NMB8_ZYMMO 1 259
SEQRES 1 A 259 MET SER ARG SER ALA TYR GLU ASP ASP ILE ARG LEU ALA
SEQRES 2 A 259 HIS ARG LEU ALA ASP VAL ALA ALA ASP ILE ILE ARG PRO
SEQRES 3 A 259 PHE PHE ARG ALA PRO LEU THR ILE ASP LEU LYS ALA ASP
SEQRES 4 A 259 HIS SER PRO VAL THR LYS ALA ASP ARG GLY ALA GLU GLN
SEQRES 5 A 259 ALA MET ARG ALA ILE LEU GLU GLN GLU ARG PRO GLU ASP
SEQRES 6 A 259 GLY ILE PHE GLY GLU GLU MET GLY VAL SER ARG PRO ASP
SEQRES 7 A 259 ALA ARG ARG LEU TRP VAL LEU ASP PRO ILE ASP GLY THR
SEQRES 8 A 259 ARG ALA PHE ILE GLY GLY ARG ALA SER PHE GLY THR LEU
SEQRES 9 A 259 ILE ALA LEU VAL GLU ASP GLY ARG PRO VAL LEU GLY ILE
SEQRES 10 A 259 ILE ASN GLN PRO ILE HIS GLN GLU ARG TRP VAL GLY VAL
SEQRES 11 A 259 LYS ASP LEU PRO THR SER PHE ASN GLY GLU VAL ILE HIS
SEQRES 12 A 259 THR ARG SER CYS PRO ALA LEU ASP HIS ALA LEU LEU ALA
SEQRES 13 A 259 THR THR SER PRO TRP LEU PHE GLU LYS GLU GLY GLU VAL
SEQRES 14 A 259 HIS PHE ASP LYS ILE ARG LEU LYS CYS ARG ASP THR LEU
SEQRES 15 A 259 LEU GLY GLY ASP CYS TYR ASN TYR GLY LEU LEU SER LEU
SEQRES 16 A 259 GLY HIS CYS ASP LEU VAL VAL GLU GLN GLY LEU LYS PHE
SEQRES 17 A 259 TYR ASP PHE ALA ALA LEU VAL PRO ILE VAL GLU GLY ALA
SEQRES 18 A 259 GLY GLY ILE MET ARG ASP TRP GLN ASN ARG PRO LEU ASN
SEQRES 19 A 259 LYS ASN SER VAL GLY GLU VAL ILE ALA ALA GLY ASP HIS
SEQRES 20 A 259 HIS LEU ILE GLU PRO ALA LEU SER ALA MET GLU LEU
HET SO4 A 301 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *292(H2 O)
HELIX 1 1 TYR A 6 ARG A 25 1 20
HELIX 2 2 PRO A 26 PHE A 28 5 3
HELIX 3 3 SER A 41 ARG A 62 1 22
HELIX 4 4 GLY A 90 GLY A 96 1 7
HELIX 5 5 ALA A 149 HIS A 152 5 4
HELIX 6 6 SER A 159 PHE A 163 5 5
HELIX 7 7 GLU A 164 LEU A 176 1 13
HELIX 8 8 ASP A 186 LEU A 195 1 10
HELIX 9 9 LYS A 207 ALA A 212 1 6
HELIX 10 10 ALA A 213 ALA A 221 1 9
HELIX 11 11 ASP A 246 HIS A 248 5 3
HELIX 12 12 LEU A 249 GLU A 258 1 10
SHEET 1 A 7 GLY A 66 ILE A 67 0
SHEET 2 A 7 ARG A 81 ASP A 89 1 O ARG A 81 N GLY A 66
SHEET 3 A 7 GLY A 102 GLU A 109 -1 O GLY A 102 N ASP A 89
SHEET 4 A 7 ARG A 112 GLN A 120 -1 O VAL A 114 N LEU A 107
SHEET 5 A 7 GLU A 125 VAL A 130 -1 O GLU A 125 N GLN A 120
SHEET 6 A 7 LEU A 133 PHE A 137 -1 O SER A 136 N VAL A 128
SHEET 7 A 7 GLU A 140 VAL A 141 -1 O GLU A 140 N PHE A 137
SHEET 1 B 5 ASP A 180 LEU A 183 0
SHEET 2 B 5 LEU A 154 THR A 157 1 N LEU A 155 O ASP A 180
SHEET 3 B 5 LEU A 200 GLU A 203 1 N LEU A 200 O LEU A 154
SHEET 4 B 5 VAL A 241 ALA A 244 -1 O VAL A 241 N GLU A 203
SHEET 5 B 5 ILE A 224 ARG A 226 -1 N ARG A 226 O ILE A 242
SITE 1 AC1 9 ASP A 86 ILE A 88 ASP A 89 GLY A 90
SITE 2 AC1 9 THR A 91 ASP A 210 HOH A 423 HOH A 476
SITE 3 AC1 9 HOH A 483
CRYST1 90.747 90.747 75.274 90.00 90.00 120.00 P 32 2 1 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 0.011020 0.006362 0.000000 0.00000
SCALE2 0.000000 0.012724 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013285 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
