HEADER SYNTHASE 14-MAY-97 1AJ0
TITLE CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI DIHYDROPTEROATE
TITLE 2 SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROPTEROATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DHPS;
COMPND 5 EC: 2.5.1.15
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS ANTIBIOTIC, RESISTANCE, TRANSFERASE, FOLATE, BIOSYNTHESIS, SYNTHASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ACHARI,D.O.SOMERS,J.N.CHAMPNESS,P.K.BRYANT,J.ROSEMOND,D.K.STAMMERS
REVDAT 4 07-FEB-24 1AJ0 1 REMARK
REVDAT 3 13-JUL-11 1AJ0 1 VERSN
REVDAT 2 24-FEB-09 1AJ0 1 VERSN
REVDAT 1 20-MAY-98 1AJ0 0
JRNL AUTH A.ACHARI,D.O.SOMERS,J.N.CHAMPNESS,P.K.BRYANT,J.ROSEMOND,
JRNL AUTH 2 D.K.STAMMERS
JRNL TITL CRYSTAL STRUCTURE OF THE ANTI-BACTERIAL SULFONAMIDE DRUG
JRNL TITL 2 TARGET DIHYDROPTEROATE SYNTHASE.
JRNL REF NAT.STRUCT.BIOL. V. 4 490 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9187658
JRNL DOI 10.1038/NSB0697-490
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.0
REMARK 3 NUMBER OF REFLECTIONS : 18585
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 23206
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2147
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 105
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.010 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.032 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.038 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.101 ; 0.120
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.179 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.223 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : 0.230 ; 0.500
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 1.800 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 17.900; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 24.300; 20.000
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-93
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : 8.4
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : XENGEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23202
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PROFFT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 42%
REMARK 280 AMMONIUM SULFATE, 50MM TRIS-HCL, PH 8.4.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y,-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 30.33500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.45500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.33500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.45500
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
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: 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 448 O HOH A 448 4555 1.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG A 163 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 VAL A 216 N - CA - CB ANGL. DEV. = -15.6 DEGREES
REMARK 500 ARG A 235 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
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 PHE A 28 48.43 -92.51
REMARK 500 SER A 29 -169.82 -46.83
REMARK 500 ASP A 30 10.69 59.80
REMARK 500 THR A 33 98.67 52.40
REMARK 500 HIS A 34 -148.20 -91.12
REMARK 500 ASP A 156 111.05 -161.11
REMARK 500 ARG A 220 18.60 54.73
REMARK 500 ARG A 280 145.94 174.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 163 0.11 SIDE CHAIN
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 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PH2 A 559
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAN A 561
DBREF 1AJ0 A 1 282 UNP P0AC13 DHPS_ECOLI 1 282
SEQRES 1 A 282 MET LYS LEU PHE ALA GLN GLY THR SER LEU ASP LEU SER
SEQRES 2 A 282 HIS PRO HIS VAL MET GLY ILE LEU ASN VAL THR PRO ASP
SEQRES 3 A 282 SER PHE SER ASP GLY GLY THR HIS ASN SER LEU ILE ASP
SEQRES 4 A 282 ALA VAL LYS HIS ALA ASN LEU MET ILE ASN ALA GLY ALA
SEQRES 5 A 282 THR ILE ILE ASP VAL GLY GLY GLU SER THR ARG PRO GLY
SEQRES 6 A 282 ALA ALA GLU VAL SER VAL GLU GLU GLU LEU GLN ARG VAL
SEQRES 7 A 282 ILE PRO VAL VAL GLU ALA ILE ALA GLN ARG PHE GLU VAL
SEQRES 8 A 282 TRP ILE SER VAL ASP THR SER LYS PRO GLU VAL ILE ARG
SEQRES 9 A 282 GLU SER ALA LYS VAL GLY ALA HIS ILE ILE ASN ASP ILE
SEQRES 10 A 282 ARG SER LEU SER GLU PRO GLY ALA LEU GLU ALA ALA ALA
SEQRES 11 A 282 GLU THR GLY LEU PRO VAL CYS LEU MET HIS MET GLN GLY
SEQRES 12 A 282 ASN PRO LYS THR MET GLN GLU ALA PRO LYS TYR ASP ASP
SEQRES 13 A 282 VAL PHE ALA GLU VAL ASN ARG TYR PHE ILE GLU GLN ILE
SEQRES 14 A 282 ALA ARG CYS GLU GLN ALA GLY ILE ALA LYS GLU LYS LEU
SEQRES 15 A 282 LEU LEU ASP PRO GLY PHE GLY PHE GLY LYS ASN LEU SER
SEQRES 16 A 282 HIS ASN TYR SER LEU LEU ALA ARG LEU ALA GLU PHE HIS
SEQRES 17 A 282 HIS PHE ASN LEU PRO LEU LEU VAL GLY MET SER ARG LYS
SEQRES 18 A 282 SER MET ILE GLY GLN LEU LEU ASN VAL GLY PRO SER GLU
SEQRES 19 A 282 ARG LEU SER GLY SER LEU ALA CYS ALA VAL ILE ALA ALA
SEQRES 20 A 282 MET GLN GLY ALA HIS ILE ILE ARG VAL HIS ASP VAL LYS
SEQRES 21 A 282 GLU THR VAL GLU ALA MET ARG VAL VAL GLU ALA THR LEU
SEQRES 22 A 282 SER ALA LYS GLU ASN LYS ARG TYR GLU
HET SO4 A 284 5
HET PH2 A 559 14
HET SAN A 561 11
HETNAM SO4 SULFATE ION
HETNAM PH2 2-AMINO-6-HYDROXYMETHYL-7,8-DIHYDRO-3H-PTERIDIN-4-ONE
HETNAM SAN SULFANILAMIDE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 PH2 C7 H9 N5 O2
FORMUL 4 SAN C6 H8 N2 O2 S
FORMUL 5 HOH *105(H2 O)
HELIX 1 1 ASN A 35 ALA A 50 5 16
HELIX 2 2 VAL A 71 ARG A 88 1 18
HELIX 3 3 PRO A 100 LYS A 108 1 9
HELIX 4 4 ALA A 125 THR A 132 1 8
HELIX 5 5 VAL A 157 GLN A 174 1 18
HELIX 6 6 LYS A 179 LYS A 181 5 3
HELIX 7 7 LEU A 194 ALA A 202 1 9
HELIX 8 8 LEU A 204 PHE A 210 5 7
HELIX 9 9 SER A 222 LEU A 228 1 7
HELIX 10 10 PRO A 232 GLU A 234 5 3
HELIX 11 11 LEU A 236 GLN A 249 1 14
HELIX 12 12 VAL A 259 ALA A 275 1 17
SHEET 1 A 2 LYS A 2 ALA A 5 0
SHEET 2 A 2 THR A 8 ASP A 11 -1 N LEU A 10 O LEU A 3
SHEET 1 B 7 ILE A 253 VAL A 256 0
SHEET 2 B 7 HIS A 16 ASN A 22 1 N HIS A 16 O ILE A 254
SHEET 3 B 7 ILE A 54 GLY A 58 1 N ILE A 54 O GLY A 19
SHEET 4 B 7 TRP A 92 ASP A 96 1 N TRP A 92 O ILE A 55
SHEET 5 B 7 ILE A 113 ASP A 116 1 N ILE A 113 O VAL A 95
SHEET 6 B 7 PRO A 135 MET A 139 1 N PRO A 135 O ILE A 114
SHEET 7 B 7 LEU A 182 ASP A 185 1 N LEU A 183 O VAL A 136
SITE 1 AC1 7 ASN A 22 ARG A 63 ARG A 255 HIS A 257
SITE 2 AC1 7 HOH A 312 PH2 A 559 SAN A 561
SITE 1 AC2 13 THR A 62 ASP A 96 ASN A 115 ILE A 117
SITE 2 AC2 13 ASP A 185 PHE A 190 LEU A 215 GLY A 217
SITE 3 AC2 13 LYS A 221 ARG A 255 SO4 A 284 HOH A 419
SITE 4 AC2 13 SAN A 561
SITE 1 AC3 8 THR A 62 ARG A 63 SER A 219 ARG A 220
SITE 2 AC3 8 LYS A 221 HIS A 257 SO4 A 284 PH2 A 559
CRYST1 92.910 60.670 59.820 90.00 114.67 90.00 C 1 21 1 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 0.010763 0.000000 0.004944 0.00000
SCALE2 0.000000 0.016483 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018396 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
