HEADER TRANSFERASE 19-FEB-97 1AD1
TITLE DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROPTEROATE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DHPS;
COMPND 5 EC: 2.5.1.15;
COMPND 6 OTHER_DETAILS: APO FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280
KEYWDS SYNTHETASE, TRANSFERASE, DIHYDROPTEROATE SYNTHETASE, DHPS, APO FORM,
KEYWDS 2 COMPLEX WITH OH-CH2-PTERIN-PYROPHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KOSTREWA,C.OEFNER,A.D'ARCY
REVDAT 4 07-FEB-24 1AD1 1 REMARK LINK
REVDAT 3 24-FEB-09 1AD1 1 VERSN
REVDAT 2 01-APR-03 1AD1 1 JRNL
REVDAT 1 29-APR-98 1AD1 0
JRNL AUTH I.C.HAMPELE,A.D'ARCY,G.E.DALE,D.KOSTREWA,J.NIELSEN,C.OEFNER,
JRNL AUTH 2 M.G.PAGE,H.J.SCHONFELD,D.STUBER,R.L.THEN
JRNL TITL STRUCTURE AND FUNCTION OF THE DIHYDROPTEROATE SYNTHASE FROM
JRNL TITL 2 STAPHYLOCOCCUS AUREUS.
JRNL REF J.MOL.BIOL. V. 268 21 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9149138
JRNL DOI 10.1006/JMBI.1997.0944
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.50
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 23608
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 SET) : 0.159
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3984
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 401
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) : 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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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:
REMARK 3 CONVENTIONAL RESTRAINED POSITIONAL AND TEMPERATURE FACTOR
REMARK 3 REFINEMENT WITH STEREOCHEMICAL PARAMETERS FROM ENGH & HUBER.
REMARK 3
REMARK 3 THE ELECTRON DENSITY OF THE TRIS MOLECULE IS ONLY POORLY
REMARK 3 DEFINED.
REMARK 4
REMARK 4 1AD1 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_1000170667.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-96
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 21.09500
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 300 REMARK: THE ASYMMETRIC UNIT OF THE CRYSTAL CONTAINS ONE DIMER.
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: 3490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 266
REMARK 465 SER A 267
REMARK 465 ASP B 15
REMARK 465 SER B 16
REMARK 465 PHE B 17
REMARK 465 SER B 18
REMARK 465 ASP B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 LYS B 22
REMARK 465 PHE B 23
REMARK 465 ASN B 24
REMARK 465 ARG B 52
REMARK 465 PRO B 53
REMARK 465 GLY B 54
REMARK 465 HIS B 55
REMARK 465 GLU B 56
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 SER A 18 -71.81 -56.75
REMARK 500 SER A 201 112.30 -35.90
REMARK 500 ASN B 134 35.97 -94.82
REMARK 500 ALA B 173 37.27 38.99
REMARK 500 SER B 201 109.85 -27.02
REMARK 500 ARG B 202 11.12 59.21
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 K A 268 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 75 O
REMARK 620 2 PHE A 77 O 88.4
REMARK 620 3 VAL A 79 O 136.4 78.5
REMARK 620 4 HOH A 517 O 80.9 164.0 101.2
REMARK 620 5 HOH A 589 O 147.5 88.8 74.3 106.7
REMARK 620 6 HOH A 594 O 63.2 91.8 156.7 94.0 84.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 1 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 75 O
REMARK 620 2 PHE B 77 O 88.9
REMARK 620 3 VAL B 79 O 135.4 80.8
REMARK 620 4 HOH B 291 O 82.4 168.8 100.6
REMARK 620 5 HOH B 424 O 134.5 122.1 85.6 69.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 500
DBREF 1AD1 A 2 267 UNP O05701 DHPS_STAAU 2 267
DBREF 1AD1 B 2 267 UNP O05701 DHPS_STAAU 2 267
SEQRES 1 A 266 THR LYS THR LYS ILE MET GLY ILE LEU ASN VAL THR PRO
SEQRES 2 A 266 ASP SER PHE SER ASP GLY GLY LYS PHE ASN ASN VAL GLU
SEQRES 3 A 266 SER ALA VAL THR ARG VAL LYS ALA MET MET ASP GLU GLY
SEQRES 4 A 266 ALA ASP ILE ILE ASP VAL GLY GLY VAL SER THR ARG PRO
SEQRES 5 A 266 GLY HIS GLU MET ILE THR VAL GLU GLU GLU LEU ASN ARG
SEQRES 6 A 266 VAL LEU PRO VAL VAL GLU ALA ILE VAL GLY PHE ASP VAL
SEQRES 7 A 266 LYS ILE SER VAL ASP THR PHE ARG SER GLU VAL ALA GLU
SEQRES 8 A 266 ALA CYS LEU LYS LEU GLY VAL ASP ILE ILE ASN ASP GLN
SEQRES 9 A 266 TRP ALA GLY LEU TYR ASP HIS ARG MET PHE GLN VAL VAL
SEQRES 10 A 266 ALA LYS TYR ASP ALA GLU ILE VAL LEU MET HIS ASN GLY
SEQRES 11 A 266 ASN GLY ASN ARG ASP GLU PRO VAL VAL GLU GLU MET LEU
SEQRES 12 A 266 THR SER LEU LEU ALA GLN ALA HIS GLN ALA LYS ILE ALA
SEQRES 13 A 266 GLY ILE PRO SER ASN LYS ILE TRP LEU ASP PRO GLY ILE
SEQRES 14 A 266 GLY PHE ALA LYS THR ARG ASN GLU GLU ALA GLU VAL MET
SEQRES 15 A 266 ALA ARG LEU ASP GLU LEU VAL ALA THR GLU TYR PRO VAL
SEQRES 16 A 266 LEU LEU ALA THR SER ARG LYS ARG PHE THR LYS GLU MET
SEQRES 17 A 266 MET GLY TYR ASP THR THR PRO VAL GLU ARG ASP GLU VAL
SEQRES 18 A 266 THR ALA ALA THR THR ALA TYR GLY ILE MET LYS GLY VAL
SEQRES 19 A 266 ARG ALA VAL ARG VAL HIS ASN VAL GLU LEU ASN ALA LYS
SEQRES 20 A 266 LEU ALA LYS GLY ILE ASP PHE LEU LYS GLU ASN GLU ASN
SEQRES 21 A 266 ALA ARG HIS ASN PHE SER
SEQRES 1 B 266 THR LYS THR LYS ILE MET GLY ILE LEU ASN VAL THR PRO
SEQRES 2 B 266 ASP SER PHE SER ASP GLY GLY LYS PHE ASN ASN VAL GLU
SEQRES 3 B 266 SER ALA VAL THR ARG VAL LYS ALA MET MET ASP GLU GLY
SEQRES 4 B 266 ALA ASP ILE ILE ASP VAL GLY GLY VAL SER THR ARG PRO
SEQRES 5 B 266 GLY HIS GLU MET ILE THR VAL GLU GLU GLU LEU ASN ARG
SEQRES 6 B 266 VAL LEU PRO VAL VAL GLU ALA ILE VAL GLY PHE ASP VAL
SEQRES 7 B 266 LYS ILE SER VAL ASP THR PHE ARG SER GLU VAL ALA GLU
SEQRES 8 B 266 ALA CYS LEU LYS LEU GLY VAL ASP ILE ILE ASN ASP GLN
SEQRES 9 B 266 TRP ALA GLY LEU TYR ASP HIS ARG MET PHE GLN VAL VAL
SEQRES 10 B 266 ALA LYS TYR ASP ALA GLU ILE VAL LEU MET HIS ASN GLY
SEQRES 11 B 266 ASN GLY ASN ARG ASP GLU PRO VAL VAL GLU GLU MET LEU
SEQRES 12 B 266 THR SER LEU LEU ALA GLN ALA HIS GLN ALA LYS ILE ALA
SEQRES 13 B 266 GLY ILE PRO SER ASN LYS ILE TRP LEU ASP PRO GLY ILE
SEQRES 14 B 266 GLY PHE ALA LYS THR ARG ASN GLU GLU ALA GLU VAL MET
SEQRES 15 B 266 ALA ARG LEU ASP GLU LEU VAL ALA THR GLU TYR PRO VAL
SEQRES 16 B 266 LEU LEU ALA THR SER ARG LYS ARG PHE THR LYS GLU MET
SEQRES 17 B 266 MET GLY TYR ASP THR THR PRO VAL GLU ARG ASP GLU VAL
SEQRES 18 B 266 THR ALA ALA THR THR ALA TYR GLY ILE MET LYS GLY VAL
SEQRES 19 B 266 ARG ALA VAL ARG VAL HIS ASN VAL GLU LEU ASN ALA LYS
SEQRES 20 B 266 LEU ALA LYS GLY ILE ASP PHE LEU LYS GLU ASN GLU ASN
SEQRES 21 B 266 ALA ARG HIS ASN PHE SER
HET K A 268 1
HET TRS A 500 8
HET K B 1 1
HETNAM K POTASSIUM ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 K 2(K 1+)
FORMUL 4 TRS C4 H12 N O3 1+
FORMUL 6 HOH *401(H2 O)
HELIX 1 1 PRO A 14 SER A 16 5 3
HELIX 2 2 VAL A 26 ASP A 38 1 13
HELIX 3 3 VAL A 60 ILE A 74 1 15
HELIX 4 4 SER A 88 LYS A 96 1 9
HELIX 5 5 HIS A 112 LYS A 120 5 9
HELIX 6 6 VAL A 139 ILE A 156 1 18
HELIX 7 7 SER A 161 LYS A 163 5 3
HELIX 8 8 ARG A 176 ALA A 184 1 9
HELIX 9 9 LEU A 186 THR A 192 1 7
HELIX 10 10 ARG A 204 MET A 209 1 6
HELIX 11 11 PRO A 216 LYS A 233 5 18
HELIX 12 12 VAL A 243 HIS A 264 1 22
HELIX 13 13 VAL B 26 ASP B 38 1 13
HELIX 14 14 VAL B 60 ILE B 74 1 15
HELIX 15 15 SER B 88 LEU B 97 1 10
HELIX 16 16 HIS B 112 TYR B 121 5 10
HELIX 17 17 VAL B 139 ALA B 157 1 19
HELIX 18 18 SER B 161 LYS B 163 5 3
HELIX 19 19 ARG B 176 MET B 183 1 8
HELIX 20 20 LEU B 186 THR B 192 1 7
HELIX 21 21 ARG B 204 MET B 210 1 7
HELIX 22 22 PRO B 216 MET B 232 5 17
HELIX 23 23 VAL B 243 HIS B 264 1 22
SHEET 1 A 7 ALA A 237 VAL A 240 0
SHEET 2 A 7 LYS A 5 ASN A 11 1 N LYS A 5 O VAL A 238
SHEET 3 A 7 ILE A 43 GLY A 47 1 N ILE A 43 O GLY A 8
SHEET 4 A 7 LYS A 80 ASP A 84 1 N LYS A 80 O ILE A 44
SHEET 5 A 7 ILE A 101 ASP A 104 1 N ILE A 101 O VAL A 83
SHEET 6 A 7 GLU A 124 MET A 128 1 N GLU A 124 O ILE A 102
SHEET 7 A 7 ILE A 164 ASP A 167 1 N TRP A 165 O ILE A 125
SHEET 1 B 7 ALA B 237 VAL B 240 0
SHEET 2 B 7 LYS B 5 ASN B 11 1 N LYS B 5 O VAL B 238
SHEET 3 B 7 ILE B 43 GLY B 47 1 N ILE B 43 O GLY B 8
SHEET 4 B 7 LYS B 80 ASP B 84 1 N LYS B 80 O ILE B 44
SHEET 5 B 7 ILE B 101 ASP B 104 1 N ILE B 101 O VAL B 83
SHEET 6 B 7 GLU B 124 MET B 128 1 N GLU B 124 O ILE B 102
SHEET 7 B 7 ILE B 164 ASP B 167 1 N TRP B 165 O ILE B 125
LINK O VAL A 75 K K A 268 1555 1555 2.83
LINK O PHE A 77 K K A 268 1555 1555 2.71
LINK O VAL A 79 K K A 268 1555 1555 2.68
LINK K K A 268 O HOH A 517 1555 1555 2.89
LINK K K A 268 O HOH A 589 1555 1555 3.07
LINK K K A 268 O HOH A 594 1555 1555 3.18
LINK K K B 1 O VAL B 75 1555 1555 2.81
LINK K K B 1 O PHE B 77 1555 1555 2.71
LINK K K B 1 O VAL B 79 1555 1555 2.58
LINK K K B 1 O HOH B 291 1555 1555 2.73
LINK K K B 1 O HOH B 424 1555 1555 3.44
SITE 1 AC1 4 VAL B 75 PHE B 77 VAL B 79 HOH B 291
SITE 1 AC2 5 VAL A 75 PHE A 77 VAL A 79 HOH A 517
SITE 2 AC2 5 HOH A 589
SITE 1 AC3 1 LYS A 96
CRYST1 64.470 42.190 101.320 90.00 106.33 90.00 P 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 0.015511 0.000000 0.004545 0.00000
SCALE2 0.000000 0.023702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010285 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
