HEADER OXIDOREDUCTASE 05-JUL-10 3NTO
TITLE CRYSTAL STRUCTURE OF K97V MUTANT MYO-INOSITOL DEHYDROGENASE FROM
TITLE 2 BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INOSITOL 2-DEHYDROGENASE/D-CHIRO-INOSITOL 3-DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MYO-INOSITOL 2-DEHYDROGENASE/D-CHIRO-INOSITOL 3-
COMPND 5 DEHYDROGENASE, MI 2-DEHYDROGENASE/DCI 3-DEHYDROGENASE;
COMPND 6 EC: 1.1.1.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: BSU39700, E83G, IDH, IOLG, NP_391849.2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHISTEV
KEYWDS K97V MUTANT, BSIDH, OXIDOREDUCTASE, N-TERMINAL ROSSMANN FOLD DOMAIN,
KEYWDS 2 GLYCERALDEHYDE-3-PHOSPHATE LIKE C-TERMINAL DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.VAN STRAATEN,D.R.J.PALMER,D.A.R.SANDERS
REVDAT 4 27-DEC-23 3NTO 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3NTO 1 REMARK
REVDAT 2 01-DEC-10 3NTO 1 JRNL
REVDAT 1 15-SEP-10 3NTO 0
JRNL AUTH K.E.VAN STRAATEN,H.ZHENG,D.R.PALMER,D.A.SANDERS
JRNL TITL STRUCTURAL INVESTIGATION OF MYO-INOSITOL DEHYDROGENASE FROM
JRNL TITL 2 BACILLUS SUBTILIS: IMPLICATIONS FOR CATALYTIC MECHANISM AND
JRNL TITL 3 INOSITOL DEHYDROGENASE SUBFAMILY CLASSIFICATION.
JRNL REF BIOCHEM.J. V. 432 237 2010
JRNL REFN ISSN 0264-6021
JRNL PMID 20809899
JRNL DOI 10.1042/BJ20101079
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 31217
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1561
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 19.6715 - 4.1089 0.99 3124 164 0.1583 0.2002
REMARK 3 2 4.1089 - 3.2662 1.00 3016 159 0.1517 0.1810
REMARK 3 3 3.2662 - 2.8548 1.00 3022 159 0.1745 0.2183
REMARK 3 4 2.8548 - 2.5944 1.00 2999 158 0.1704 0.2039
REMARK 3 5 2.5944 - 2.4088 1.00 2964 156 0.1692 0.2000
REMARK 3 6 2.4088 - 2.2670 1.00 2984 157 0.1734 0.2243
REMARK 3 7 2.2670 - 2.1536 1.00 2981 157 0.1681 0.2465
REMARK 3 8 2.1536 - 2.0600 1.00 2956 155 0.1708 0.1937
REMARK 3 9 2.0600 - 1.9807 1.00 2964 156 0.1742 0.2303
REMARK 3 10 1.9807 - 1.9124 0.90 2646 140 0.1931 0.2264
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 : 0.38
REMARK 3 B_SOL : 41.72
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.20930
REMARK 3 B22 (A**2) : -4.50270
REMARK 3 B33 (A**2) : -8.70660
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 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 : 0.007 2736
REMARK 3 ANGLE : 1.023 3716
REMARK 3 CHIRALITY : 0.073 422
REMARK 3 PLANARITY : 0.004 481
REMARK 3 DIHEDRAL : 13.610 1025
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3NTO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-08
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 : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31224
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.4100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.13700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.000
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: APO-IDH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CACL2, 0.1M HEPES PH 7.5, 14% PEG
REMARK 280 400, MICROBATCH, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 26.13500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.75000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 64.35000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.13500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.75000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.35000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.13500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.75000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.35000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.13500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.75000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 64.35000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 -52.27000
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 BIOMT1 3 -1.000000 0.000000 0.000000 -52.27000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 HOH A 601 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 604 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 618 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 679 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 686 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 PHE A 339
REMARK 465 THR A 340
REMARK 465 THR A 341
REMARK 465 VAL A 342
REMARK 465 GLN A 343
REMARK 465 ASN A 344
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 LYS A 24 -35.95 -130.24
REMARK 500 THR A 173 -64.35 -101.90
REMARK 500 LYS A 232 -40.77 69.42
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 EPE A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MZ0 RELATED DB: PDB
REMARK 900 APO-IDH
REMARK 900 RELATED ID: 3NT2 RELATED DB: PDB
REMARK 900 IDH WITH BOUND COFACTOR
REMARK 900 RELATED ID: 3NT4 RELATED DB: PDB
REMARK 900 IDH WITH BOUND COFACTOR AND INOSITOL
REMARK 900 RELATED ID: 3NT5 RELATED DB: PDB
REMARK 900 IDH WITH BOUND COFACTOR AND INOSOSE
REMARK 900 RELATED ID: 3NTQ RELATED DB: PDB
REMARK 900 K97V MUTANT IDH WITH BOUND COFACTOR
REMARK 900 RELATED ID: 3NTR RELATED DB: PDB
REMARK 900 K97V MUTANT IDH WITH BOUND COFACTOR AND INOSITOL
DBREF 3NTO A 1 344 UNP P26935 IOLG_BACSU 1 344
SEQADV 3NTO VAL A 97 UNP P26935 LYS 97 ENGINEERED MUTATION
SEQRES 1 A 344 MET SER LEU ARG ILE GLY VAL ILE GLY THR GLY ALA ILE
SEQRES 2 A 344 GLY LYS GLU HIS ILE ASN ARG ILE THR ASN LYS LEU SER
SEQRES 3 A 344 GLY ALA GLU ILE VAL ALA VAL THR ASP VAL ASN GLN GLU
SEQRES 4 A 344 ALA ALA GLN LYS VAL VAL GLU GLN TYR GLN LEU ASN ALA
SEQRES 5 A 344 THR VAL TYR PRO ASN ASP ASP SER LEU LEU ALA ASP GLU
SEQRES 6 A 344 ASN VAL ASP ALA VAL LEU VAL THR SER TRP GLY PRO ALA
SEQRES 7 A 344 HIS GLU SER SER VAL LEU LYS ALA ILE LYS ALA GLN LYS
SEQRES 8 A 344 TYR VAL PHE CYS GLU VAL PRO LEU ALA THR THR ALA GLU
SEQRES 9 A 344 GLY CYS MET ARG ILE VAL GLU GLU GLU ILE LYS VAL GLY
SEQRES 10 A 344 LYS ARG LEU VAL GLN VAL GLY PHE MET ARG ARG TYR ASP
SEQRES 11 A 344 SER GLY TYR VAL GLN LEU LYS GLU ALA LEU ASP ASN HIS
SEQRES 12 A 344 VAL ILE GLY GLU PRO LEU MET ILE HIS CYS ALA HIS ARG
SEQRES 13 A 344 ASN PRO THR VAL GLY ASP ASN TYR THR THR ASP MET ALA
SEQRES 14 A 344 VAL VAL ASP THR LEU VAL HIS GLU ILE ASP VAL LEU HIS
SEQRES 15 A 344 TRP LEU VAL ASN ASP ASP TYR GLU SER VAL GLN VAL ILE
SEQRES 16 A 344 TYR PRO LYS LYS SER LYS ASN ALA LEU PRO HIS LEU LYS
SEQRES 17 A 344 ASP PRO GLN ILE VAL VAL ILE GLU THR LYS GLY GLY ILE
SEQRES 18 A 344 VAL ILE ASN ALA GLU ILE TYR VAL ASN CYS LYS TYR GLY
SEQRES 19 A 344 TYR ASP ILE GLN CYS GLU ILE VAL GLY GLU ASP GLY ILE
SEQRES 20 A 344 ILE LYS LEU PRO GLU PRO SER SER ILE SER LEU ARG LYS
SEQRES 21 A 344 GLU GLY ARG PHE SER THR ASP ILE LEU MET ASP TRP GLN
SEQRES 22 A 344 ARG ARG PHE VAL ALA ALA TYR ASP VAL GLU ILE GLN ASP
SEQRES 23 A 344 PHE ILE ASP SER ILE GLN LYS LYS GLY GLU VAL SER GLY
SEQRES 24 A 344 PRO THR ALA TRP ASP GLY TYR ILE ALA ALA VAL THR THR
SEQRES 25 A 344 ASP ALA CYS VAL LYS ALA GLN GLU SER GLY GLN LYS GLU
SEQRES 26 A 344 LYS VAL GLU LEU LYS GLU LYS PRO GLU PHE TYR GLN SER
SEQRES 27 A 344 PHE THR THR VAL GLN ASN
HET EPE A 401 15
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 2 EPE C8 H18 N2 O4 S
FORMUL 3 HOH *352(H2 O)
HELIX 1 1 GLY A 11 LYS A 24 1 14
HELIX 2 2 ASN A 37 TYR A 48 1 12
HELIX 3 3 ASN A 57 ALA A 63 1 7
HELIX 4 4 TRP A 75 PRO A 77 5 3
HELIX 5 5 ALA A 78 ALA A 89 1 12
HELIX 6 6 THR A 102 GLY A 117 1 16
HELIX 7 7 PHE A 125 TYR A 129 5 5
HELIX 8 8 ASP A 130 ASN A 142 1 13
HELIX 9 9 ASP A 167 ASP A 172 1 6
HELIX 10 10 LEU A 174 ASN A 186 1 13
HELIX 11 11 ASP A 271 ARG A 275 5 5
HELIX 12 12 PHE A 276 GLY A 295 1 20
HELIX 13 13 THR A 301 GLY A 322 1 22
HELIX 14 14 PRO A 333 GLN A 337 5 5
SHEET 1 A 6 THR A 53 VAL A 54 0
SHEET 2 A 6 ALA A 28 THR A 34 1 N VAL A 33 O THR A 53
SHEET 3 A 6 LEU A 3 ILE A 8 1 N ILE A 5 O GLU A 29
SHEET 4 A 6 ALA A 69 VAL A 72 1 O LEU A 71 N ILE A 8
SHEET 5 A 6 TYR A 92 CYS A 95 1 O PHE A 94 N VAL A 72
SHEET 6 A 6 VAL A 121 VAL A 123 1 O GLN A 122 N CYS A 95
SHEET 1 B 7 ILE A 247 LYS A 249 0
SHEET 2 B 7 ASP A 236 GLY A 243 -1 N ILE A 241 O ILE A 248
SHEET 3 B 7 PRO A 148 ARG A 156 -1 N LEU A 149 O VAL A 242
SHEET 4 B 7 VAL A 222 TYR A 228 1 O GLU A 226 N CYS A 153
SHEET 5 B 7 GLN A 211 THR A 217 -1 N ILE A 215 O ILE A 223
SHEET 6 B 7 TYR A 189 ILE A 195 -1 N GLU A 190 O GLU A 216
SHEET 7 B 7 GLU A 325 LYS A 326 -1 O GLU A 325 N VAL A 192
SHEET 1 C 2 SER A 257 LYS A 260 0
SHEET 2 C 2 ARG A 263 THR A 266 -1 O SER A 265 N LEU A 258
CISPEP 1 VAL A 97 PRO A 98 0 0.28
CISPEP 2 ASP A 209 PRO A 210 0 5.56
SITE 1 AC1 8 VAL A 160 GLY A 161 TYR A 164 ASP A 172
SITE 2 AC1 8 THR A 173 TYR A 235 TRP A 272 HOH A 683
CRYST1 52.270 119.500 128.700 90.00 90.00 90.00 I 2 2 2 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 0.019131 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007770 0.00000
(ATOM LINES ARE NOT SHOWN.)
END