HEADER OXIDOREDUCTASE 17-NOV-99 1DF7
TITLE DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH
TITLE 2 NADPH AND METHOTREXATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DHFR;
COMPND 5 EC: 1.5.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773
KEYWDS DIHYDROFOLATE REDUCTASE, STRUCTURE-BASED INHIBITOR DESIGN,
KEYWDS 2 FOLATEANALOGS, ROSSMANN FOLD, NICOTINAMIDE ADENINE DINUCLEOTIDE,
KEYWDS 3 METHOTREXATE, TUBERCULOSIS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.LI,R.SIRAWARAPORN,P.CHITNUMSUB,W.SIRAWARAPORN,J.WOODEN,
AUTHOR 2 F.ATHAPPILLY,S.TURLEY,W.G.HOL
REVDAT 5 07-FEB-24 1DF7 1 REMARK
REVDAT 4 13-JUL-11 1DF7 1 VERSN
REVDAT 3 24-FEB-09 1DF7 1 VERSN
REVDAT 2 28-JUN-00 1DF7 1 SOURCE HETATM DBREF
REVDAT 1 09-MAR-00 1DF7 0
JRNL AUTH R.LI,R.SIRAWARAPORN,P.CHITNUMSUB,W.SIRAWARAPORN,J.WOODEN,
JRNL AUTH 2 F.ATHAPPILLY,S.TURLEY,W.G.HOL
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF M. TUBERCULOSIS DIHYDROFOLATE
JRNL TITL 2 REDUCTASE REVEALS OPPORTUNITIES FOR THE DESIGN OF NOVEL
JRNL TITL 3 TUBERCULOSIS DRUGS.
JRNL REF J.MOL.BIOL. V. 295 307 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10623528
JRNL DOI 10.1006/JMBI.1999.3328
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,A.ROSOWSKY,R.L.BLAKLEY
REMARK 1 TITL COMPARISON OF TWO INDEPENDENT CRYSTAL STRUCTURES OF HUMAN
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE TERNARY COMPLEXES REDUCED WITH
REMARK 1 TITL 3 NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE AND THE VERY
REMARK 1 TITL 4 TIGHT-BINDING INHIBITOR PT523
REMARK 1 REF BIOCHEMISTRY V. 36 13897 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI971711L
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 23394
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2311
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 : 1244
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 195
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) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 1.690
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: NULL
REMARK 4
REMARK 4 1DF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000010034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0188
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109952
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.26300
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: NULL
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM ACETATE,
REMARK 280 GLYCEROL, NADPH, METHOTREXATE, POTASSIUM PHOSPHATE, DTT,
REMARK 280 POTASSIUM CHLORIDE, PH 4.5, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 29.41500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 14.70750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.12250
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 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: 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 GLY A 95 N GLY A 95 CA -0.130
REMARK 500 GLY A 95 CA GLY A 95 C 0.109
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 21 39.90 -73.31
REMARK 500 LEU A 24 79.97 -153.64
REMARK 500 ALA A 69 -76.11 -34.37
REMARK 500 ASP A 70 66.69 -116.78
REMARK 500 LEU A 86 31.96 -90.99
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 TYR A 154 0.07 SIDE CHAIN
REMARK 500 TYR A 156 0.09 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 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DG5 RELATED DB: PDB
REMARK 900 RELATED ID: 1DG7 RELATED DB: PDB
REMARK 900 RELATED ID: 1DG8 RELATED DB: PDB
DBREF 1DF7 A 1 159 UNP P0A546 DYR_MYCTU 1 159
SEQRES 1 A 159 MET VAL GLY LEU ILE TRP ALA GLN ALA THR SER GLY VAL
SEQRES 2 A 159 ILE GLY ARG GLY GLY ASP ILE PRO TRP ARG LEU PRO GLU
SEQRES 3 A 159 ASP GLN ALA HIS PHE ARG GLU ILE THR MET GLY HIS THR
SEQRES 4 A 159 ILE VAL MET GLY ARG ARG THR TRP ASP SER LEU PRO ALA
SEQRES 5 A 159 LYS VAL ARG PRO LEU PRO GLY ARG ARG ASN VAL VAL LEU
SEQRES 6 A 159 SER ARG GLN ALA ASP PHE MET ALA SER GLY ALA GLU VAL
SEQRES 7 A 159 VAL GLY SER LEU GLU GLU ALA LEU THR SER PRO GLU THR
SEQRES 8 A 159 TRP VAL ILE GLY GLY GLY GLN VAL TYR ALA LEU ALA LEU
SEQRES 9 A 159 PRO TYR ALA THR ARG CYS GLU VAL THR GLU VAL ASP ILE
SEQRES 10 A 159 GLY LEU PRO ARG GLU ALA GLY ASP ALA LEU ALA PRO VAL
SEQRES 11 A 159 LEU ASP GLU THR TRP ARG GLY GLU THR GLY GLU TRP ARG
SEQRES 12 A 159 PHE SER ARG SER GLY LEU ARG TYR ARG LEU TYR SER TYR
SEQRES 13 A 159 HIS ARG SER
HET SO4 A 506 5
HET NDP A 500 48
HET MTX A 501 33
HET GOL A 502 6
HET GOL A 503 6
HET GOL A 504 6
HET GOL A 505 6
HETNAM SO4 SULFATE ION
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM MTX METHOTREXATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 O4 S 2-
FORMUL 3 NDP C21 H30 N7 O17 P3
FORMUL 4 MTX C20 H22 N8 O5
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *195(H2 O)
HELIX 1 1 LEU A 24 MET A 36 1 13
HELIX 2 2 ARG A 44 LEU A 50 1 7
HELIX 3 3 PRO A 51 ARG A 55 5 5
HELIX 4 4 SER A 81 LEU A 86 1 6
HELIX 5 5 GLY A 96 LEU A 104 1 9
HELIX 6 6 PRO A 105 ALA A 107 5 3
SHEET 1 A 8 GLU A 77 VAL A 79 0
SHEET 2 A 8 ARG A 61 LEU A 65 1 O ASN A 62 N GLU A 77
SHEET 3 A 8 THR A 39 GLY A 43 1 N ILE A 40 O ARG A 61
SHEET 4 A 8 THR A 91 VAL A 93 1 O TRP A 92 N VAL A 41
SHEET 5 A 8 VAL A 2 ALA A 9 1 N GLY A 3 O THR A 91
SHEET 6 A 8 ARG A 109 VAL A 115 1 O ARG A 109 N LEU A 4
SHEET 7 A 8 ARG A 150 HIS A 157 -1 O ARG A 152 N GLU A 114
SHEET 8 A 8 ARG A 136 THR A 139 -1 N ARG A 136 O HIS A 157
SHEET 1 A1 8 GLU A 77 VAL A 79 0
SHEET 2 A1 8 ARG A 61 LEU A 65 1 O ASN A 62 N GLU A 77
SHEET 3 A1 8 THR A 39 GLY A 43 1 N ILE A 40 O ARG A 61
SHEET 4 A1 8 THR A 91 VAL A 93 1 O TRP A 92 N VAL A 41
SHEET 5 A1 8 VAL A 2 ALA A 9 1 N GLY A 3 O THR A 91
SHEET 6 A1 8 ARG A 109 VAL A 115 1 O ARG A 109 N LEU A 4
SHEET 7 A1 8 ARG A 150 HIS A 157 -1 O ARG A 152 N GLU A 114
SHEET 8 A1 8 ARG A 143 PHE A 144 -1 N ARG A 143 O TYR A 151
SHEET 1 B 2 VAL A 13 GLY A 15 0
SHEET 2 B 2 ALA A 126 LEU A 127 -1 O ALA A 126 N ILE A 14
CISPEP 1 ARG A 55 PRO A 56 0 0.13
CISPEP 2 GLY A 95 GLY A 96 0 -6.88
SITE 1 AC1 2 ARG A 44 ARG A 45
SITE 1 AC2 34 TRP A 6 ALA A 7 ILE A 14 GLY A 15
SITE 2 AC2 34 GLY A 18 ASP A 19 ILE A 20 GLY A 43
SITE 3 AC2 34 ARG A 44 ARG A 45 THR A 46 LEU A 65
SITE 4 AC2 34 SER A 66 ARG A 67 GLN A 68 GLY A 80
SITE 5 AC2 34 ILE A 94 GLY A 96 GLY A 97 GLN A 98
SITE 6 AC2 34 VAL A 99 TYR A 100 LEU A 102 ALA A 126
SITE 7 AC2 34 MTX A 501 GOL A 503 HOH A 514 HOH A 519
SITE 8 AC2 34 HOH A 543 HOH A 556 HOH A 571 HOH A 577
SITE 9 AC2 34 HOH A 629 HOH A 648
SITE 1 AC3 19 ILE A 5 TRP A 6 ILE A 20 PRO A 25
SITE 2 AC3 19 ASP A 27 GLN A 28 ALA A 29 PHE A 31
SITE 3 AC3 19 ARG A 32 PRO A 51 ARG A 60 ILE A 94
SITE 4 AC3 19 TYR A 100 NDP A 500 GOL A 502 HOH A 508
SITE 5 AC3 19 HOH A 542 HOH A 559 HOH A 682
SITE 1 AC4 6 TRP A 22 LEU A 24 ASP A 27 GLN A 28
SITE 2 AC4 6 MTX A 501 HOH A 609
SITE 1 AC5 10 ARG A 45 GLN A 98 GLY A 124 GLY A 148
SITE 2 AC5 10 LEU A 149 NDP A 500 HOH A 509 HOH A 517
SITE 3 AC5 10 HOH A 574 HOH A 628
SITE 1 AC6 7 HIS A 30 GLU A 33 ALA A 52 ARG A 143
SITE 2 AC6 7 LEU A 153 HOH A 552 HOH A 677
SITE 1 AC7 5 GLN A 8 THR A 10 GLU A 114 TYR A 154
SITE 2 AC7 5 TYR A 156
CRYST1 60.510 60.510 58.830 90.00 90.00 90.00 P 41 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 0.016526 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016526 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016998 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
