HEADER OXIDOREDUCTASE 16-APR-03 1P33
TITLE PTERIDINE REDUCTASE FROM LEISHMANIA TARENTOLAE COMPLEX WITH NADPH AND
TITLE 2 MTX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTERIDINE REDUCTASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: PTERIDINE REDUCTASE;
COMPND 5 SYNONYM: H REGION METHOTREXATE RESISTANCE PROTEIN;
COMPND 6 EC: 1.1.1.253;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA TARENTOLAE;
SOURCE 3 ORGANISM_TAXID: 5689;
SOURCE 4 GENE: PTR1 OR LTDH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET16B;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMALC-2
KEYWDS PTERIDINE REDUCTASE, COMPLEX, NADPH, MTX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHAO,T.BRAY,M.OUELLETTE,M.ZHAO,R.A.FERRE,D.MATTHEWS,J.M.WHITELEY,
AUTHOR 2 K.I.VARUGHESE
REVDAT 3 16-AUG-23 1P33 1 REMARK
REVDAT 2 24-FEB-09 1P33 1 VERSN
REVDAT 1 02-SEP-03 1P33 0
JRNL AUTH H.ZHAO,T.BRAY,M.OUELLETTE,M.ZHAO,R.A.FERRE,D.MATTHEWS,
JRNL AUTH 2 J.M.WHITELEY,K.I.VARUGHESE
JRNL TITL STRUCTURE OF PTERIDINE REDUCTASE (PTR1) FROM LEISHMANIA
JRNL TITL 2 TARENTOLAE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 59 1539 2003
JRNL REFN ISSN 0907-4449
JRNL PMID 12925782
JRNL DOI 10.1107/S0907444903013131
REMARK 2
REMARK 2 RESOLUTION. 2.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 40720
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4096
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 567
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8067
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 324
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 23.97400
REMARK 3 B22 (A**2) : -9.60600
REMARK 3 B33 (A**2) : -14.36800
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 2.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.630
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1P33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018949.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 211913
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.860
REMARK 200 RESOLUTION RANGE LOW (A) : 300.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.39400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1E7W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% 1,4-BUTANDIOL, 12.5MM CTMC, 100MM
REMARK 280 HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 45.65050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.77250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.05150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.77250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.65050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.05150
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 MET A 0
REMARK 465 THR A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 PRO A 4
REMARK 465 PHE A 74
REMARK 465 SER A 75
REMARK 465 GLU A 76
REMARK 465 THR A 77
REMARK 465 ASP A 78
REMARK 465 GLY A 79
REMARK 465 LYS A 121
REMARK 465 ASP A 122
REMARK 465 ALA A 123
REMARK 465 GLY A 124
REMARK 465 GLU A 125
REMARK 465 GLY A 126
REMARK 465 GLY A 127
REMARK 465 SER A 128
REMARK 465 SER A 129
REMARK 465 VAL A 130
REMARK 465 GLY A 131
REMARK 465 MET B 0
REMARK 465 THR B 1
REMARK 465 THR B 2
REMARK 465 PHE B 74
REMARK 465 SER B 75
REMARK 465 GLU B 76
REMARK 465 THR B 77
REMARK 465 ASP B 78
REMARK 465 GLY B 79
REMARK 465 ASP B 122
REMARK 465 ALA B 123
REMARK 465 GLY B 124
REMARK 465 GLU B 125
REMARK 465 GLY B 126
REMARK 465 GLY B 127
REMARK 465 SER B 128
REMARK 465 SER B 129
REMARK 465 VAL B 130
REMARK 465 GLY B 131
REMARK 465 ASP B 132
REMARK 465 MET C 0
REMARK 465 THR C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 PHE C 74
REMARK 465 SER C 75
REMARK 465 GLU C 76
REMARK 465 THR C 77
REMARK 465 ASP C 78
REMARK 465 GLY C 79
REMARK 465 ASP C 122
REMARK 465 ALA C 123
REMARK 465 GLY C 124
REMARK 465 GLU C 125
REMARK 465 GLY C 126
REMARK 465 GLY C 127
REMARK 465 SER C 128
REMARK 465 SER C 129
REMARK 465 VAL C 130
REMARK 465 GLY C 131
REMARK 465 ASP C 132
REMARK 465 MET D 0
REMARK 465 THR D 1
REMARK 465 THR D 2
REMARK 465 SER D 3
REMARK 465 PRO D 4
REMARK 465 PHE D 74
REMARK 465 SER D 75
REMARK 465 GLU D 76
REMARK 465 THR D 77
REMARK 465 ASP D 78
REMARK 465 GLY D 79
REMARK 465 ASP D 122
REMARK 465 ALA D 123
REMARK 465 GLY D 124
REMARK 465 GLU D 125
REMARK 465 GLY D 126
REMARK 465 GLY D 127
REMARK 465 SER D 128
REMARK 465 SER D 129
REMARK 465 VAL D 130
REMARK 465 GLY D 131
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 ALA B 72 C SER B 73 N -0.195
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 ALA A 72 N - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 GLU A 134 N - CA - C ANGL. DEV. = -23.9 DEGREES
REMARK 500 ALA B 72 O - C - N ANGL. DEV. = -22.1 DEGREES
REMARK 500 THR C 5 N - CA - C ANGL. DEV. = 16.6 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 ARG A 17 -101.55 45.89
REMARK 500 SER A 40 60.65 -64.58
REMARK 500 ASN A 68 68.63 -69.69
REMARK 500 ALA A 72 -85.90 -34.60
REMARK 500 ARG A 102 144.60 -172.11
REMARK 500 PRO A 115 155.20 -47.55
REMARK 500 THR A 116 68.26 -163.10
REMARK 500 GLU A 134 -49.54 174.15
REMARK 500 ALA A 148 -60.96 -133.91
REMARK 500 ALA A 167 -53.58 -25.43
REMARK 500 SER A 173 60.53 -150.52
REMARK 500 VAL A 180 -141.96 -120.04
REMARK 500 GLN A 186 77.06 -115.63
REMARK 500 VAL A 228 74.40 16.52
REMARK 500 LEU A 229 158.43 -41.28
REMARK 500 PRO A 230 -97.19 -22.89
REMARK 500 ASP A 231 -29.55 173.07
REMARK 500 ASP A 232 53.78 -109.63
REMARK 500 TYR A 248 -2.65 74.76
REMARK 500 THR B 5 142.37 61.74
REMARK 500 ARG B 17 -129.59 44.81
REMARK 500 SER B 40 48.02 -82.58
REMARK 500 ALA B 64 121.47 -173.35
REMARK 500 CYS B 103 105.89 -165.98
REMARK 500 THR B 116 61.31 -156.06
REMARK 500 PRO B 117 153.10 -40.08
REMARK 500 ARG B 120 -151.52 -85.48
REMARK 500 GLU B 134 -42.94 -136.04
REMARK 500 ALA B 148 -64.24 -142.33
REMARK 500 SER B 173 58.10 -147.16
REMARK 500 VAL B 180 -155.35 -123.12
REMARK 500 GLN B 186 72.32 -106.69
REMARK 500 PRO B 187 118.44 -37.67
REMARK 500 TYR B 191 52.32 -99.63
REMARK 500 SER B 227 -146.06 -105.35
REMARK 500 TYR B 248 -1.17 73.15
REMARK 500 ARG C 17 -135.02 45.16
REMARK 500 ASN C 57 57.34 37.86
REMARK 500 MET C 98 14.15 -68.16
REMARK 500 HIS C 99 -30.62 -141.53
REMARK 500 ARG C 120 -68.64 -4.33
REMARK 500 GLU C 134 -15.74 -46.25
REMARK 500 ALA C 148 -52.71 -139.53
REMARK 500 ASP C 164 34.52 -86.99
REMARK 500 ALA C 167 -35.88 -29.33
REMARK 500 SER C 173 71.15 -178.59
REMARK 500 VAL C 180 -141.39 -104.18
REMARK 500 TYR C 191 53.85 -105.88
REMARK 500 VAL C 228 91.18 -15.70
REMARK 500 ASP C 231 -168.68 -58.69
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA B 72 -23.13
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 NDP A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX B 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX C 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX D 354
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E7W RELATED DB: PDB
REMARK 900 PTR1 FROM LEISHMANIA MAJOR COMPLEX WITH MTX
REMARK 900 RELATED ID: 1E92 RELATED DB: PDB
REMARK 900 PTR1 FROM LEISHMANIA MAJOR COMPLEX WITH DHB
DBREF 1P33 A 0 288 UNP P42556 PTR1_LEITA 1 289
DBREF 1P33 B 0 288 UNP P42556 PTR1_LEITA 1 289
DBREF 1P33 C 0 288 UNP P42556 PTR1_LEITA 1 289
DBREF 1P33 D 0 288 UNP P42556 PTR1_LEITA 1 289
SEQRES 1 A 289 MET THR THR SER PRO THR ALA PRO VAL ALA LEU VAL THR
SEQRES 2 A 289 GLY ALA ALA LYS ARG LEU GLY SER SER ILE ALA GLU ALA
SEQRES 3 A 289 LEU HIS ALA GLU GLY TYR THR VAL CYS LEU HIS TYR HIS
SEQRES 4 A 289 ARG SER ALA ALA ASP ALA SER THR LEU ALA ALA THR LEU
SEQRES 5 A 289 ASN ALA ARG ARG PRO ASN SER ALA ILE THR VAL GLN ALA
SEQRES 6 A 289 ASP LEU SER ASN VAL ALA THR ALA SER PHE SER GLU THR
SEQRES 7 A 289 ASP GLY SER VAL PRO VAL THR LEU PHE SER ARG CYS SER
SEQRES 8 A 289 ALA LEU VAL ASP ALA CYS TYR MET HIS TRP GLY ARG CYS
SEQRES 9 A 289 ASP VAL LEU VAL ASN ASN ALA SER SER PHE TYR PRO THR
SEQRES 10 A 289 PRO LEU LEU ARG LYS ASP ALA GLY GLU GLY GLY SER SER
SEQRES 11 A 289 VAL GLY ASP LYS GLU SER LEU GLU VAL ALA ALA ALA ASP
SEQRES 12 A 289 LEU PHE GLY SER ASN ALA ILE ALA PRO TYR PHE LEU ILE
SEQRES 13 A 289 LYS ALA PHE ALA GLN ARG VAL ALA ASP THR ARG ALA GLU
SEQRES 14 A 289 GLN ARG GLY THR SER TYR SER ILE VAL ASN MET VAL ASP
SEQRES 15 A 289 ALA MET THR SER GLN PRO LEU LEU GLY TYR THR MET TYR
SEQRES 16 A 289 THR MET ALA LYS GLU ALA LEU GLU GLY LEU THR ARG SER
SEQRES 17 A 289 ALA ALA LEU GLU LEU ALA SER LEU GLN ILE ARG VAL ASN
SEQRES 18 A 289 GLY VAL SER PRO GLY LEU SER VAL LEU PRO ASP ASP MET
SEQRES 19 A 289 PRO PHE SER VAL GLN GLU ASP TYR ARG ARG LYS VAL PRO
SEQRES 20 A 289 LEU TYR GLN ARG ASN SER SER ALA GLU GLU VAL SER ASP
SEQRES 21 A 289 VAL VAL ILE PHE LEU CYS SER PRO LYS ALA LYS TYR ILE
SEQRES 22 A 289 THR GLY THR CYS ILE LYS VAL ASP GLY GLY TYR SER LEU
SEQRES 23 A 289 THR ARG ALA
SEQRES 1 B 289 MET THR THR SER PRO THR ALA PRO VAL ALA LEU VAL THR
SEQRES 2 B 289 GLY ALA ALA LYS ARG LEU GLY SER SER ILE ALA GLU ALA
SEQRES 3 B 289 LEU HIS ALA GLU GLY TYR THR VAL CYS LEU HIS TYR HIS
SEQRES 4 B 289 ARG SER ALA ALA ASP ALA SER THR LEU ALA ALA THR LEU
SEQRES 5 B 289 ASN ALA ARG ARG PRO ASN SER ALA ILE THR VAL GLN ALA
SEQRES 6 B 289 ASP LEU SER ASN VAL ALA THR ALA SER PHE SER GLU THR
SEQRES 7 B 289 ASP GLY SER VAL PRO VAL THR LEU PHE SER ARG CYS SER
SEQRES 8 B 289 ALA LEU VAL ASP ALA CYS TYR MET HIS TRP GLY ARG CYS
SEQRES 9 B 289 ASP VAL LEU VAL ASN ASN ALA SER SER PHE TYR PRO THR
SEQRES 10 B 289 PRO LEU LEU ARG LYS ASP ALA GLY GLU GLY GLY SER SER
SEQRES 11 B 289 VAL GLY ASP LYS GLU SER LEU GLU VAL ALA ALA ALA ASP
SEQRES 12 B 289 LEU PHE GLY SER ASN ALA ILE ALA PRO TYR PHE LEU ILE
SEQRES 13 B 289 LYS ALA PHE ALA GLN ARG VAL ALA ASP THR ARG ALA GLU
SEQRES 14 B 289 GLN ARG GLY THR SER TYR SER ILE VAL ASN MET VAL ASP
SEQRES 15 B 289 ALA MET THR SER GLN PRO LEU LEU GLY TYR THR MET TYR
SEQRES 16 B 289 THR MET ALA LYS GLU ALA LEU GLU GLY LEU THR ARG SER
SEQRES 17 B 289 ALA ALA LEU GLU LEU ALA SER LEU GLN ILE ARG VAL ASN
SEQRES 18 B 289 GLY VAL SER PRO GLY LEU SER VAL LEU PRO ASP ASP MET
SEQRES 19 B 289 PRO PHE SER VAL GLN GLU ASP TYR ARG ARG LYS VAL PRO
SEQRES 20 B 289 LEU TYR GLN ARG ASN SER SER ALA GLU GLU VAL SER ASP
SEQRES 21 B 289 VAL VAL ILE PHE LEU CYS SER PRO LYS ALA LYS TYR ILE
SEQRES 22 B 289 THR GLY THR CYS ILE LYS VAL ASP GLY GLY TYR SER LEU
SEQRES 23 B 289 THR ARG ALA
SEQRES 1 C 289 MET THR THR SER PRO THR ALA PRO VAL ALA LEU VAL THR
SEQRES 2 C 289 GLY ALA ALA LYS ARG LEU GLY SER SER ILE ALA GLU ALA
SEQRES 3 C 289 LEU HIS ALA GLU GLY TYR THR VAL CYS LEU HIS TYR HIS
SEQRES 4 C 289 ARG SER ALA ALA ASP ALA SER THR LEU ALA ALA THR LEU
SEQRES 5 C 289 ASN ALA ARG ARG PRO ASN SER ALA ILE THR VAL GLN ALA
SEQRES 6 C 289 ASP LEU SER ASN VAL ALA THR ALA SER PHE SER GLU THR
SEQRES 7 C 289 ASP GLY SER VAL PRO VAL THR LEU PHE SER ARG CYS SER
SEQRES 8 C 289 ALA LEU VAL ASP ALA CYS TYR MET HIS TRP GLY ARG CYS
SEQRES 9 C 289 ASP VAL LEU VAL ASN ASN ALA SER SER PHE TYR PRO THR
SEQRES 10 C 289 PRO LEU LEU ARG LYS ASP ALA GLY GLU GLY GLY SER SER
SEQRES 11 C 289 VAL GLY ASP LYS GLU SER LEU GLU VAL ALA ALA ALA ASP
SEQRES 12 C 289 LEU PHE GLY SER ASN ALA ILE ALA PRO TYR PHE LEU ILE
SEQRES 13 C 289 LYS ALA PHE ALA GLN ARG VAL ALA ASP THR ARG ALA GLU
SEQRES 14 C 289 GLN ARG GLY THR SER TYR SER ILE VAL ASN MET VAL ASP
SEQRES 15 C 289 ALA MET THR SER GLN PRO LEU LEU GLY TYR THR MET TYR
SEQRES 16 C 289 THR MET ALA LYS GLU ALA LEU GLU GLY LEU THR ARG SER
SEQRES 17 C 289 ALA ALA LEU GLU LEU ALA SER LEU GLN ILE ARG VAL ASN
SEQRES 18 C 289 GLY VAL SER PRO GLY LEU SER VAL LEU PRO ASP ASP MET
SEQRES 19 C 289 PRO PHE SER VAL GLN GLU ASP TYR ARG ARG LYS VAL PRO
SEQRES 20 C 289 LEU TYR GLN ARG ASN SER SER ALA GLU GLU VAL SER ASP
SEQRES 21 C 289 VAL VAL ILE PHE LEU CYS SER PRO LYS ALA LYS TYR ILE
SEQRES 22 C 289 THR GLY THR CYS ILE LYS VAL ASP GLY GLY TYR SER LEU
SEQRES 23 C 289 THR ARG ALA
SEQRES 1 D 289 MET THR THR SER PRO THR ALA PRO VAL ALA LEU VAL THR
SEQRES 2 D 289 GLY ALA ALA LYS ARG LEU GLY SER SER ILE ALA GLU ALA
SEQRES 3 D 289 LEU HIS ALA GLU GLY TYR THR VAL CYS LEU HIS TYR HIS
SEQRES 4 D 289 ARG SER ALA ALA ASP ALA SER THR LEU ALA ALA THR LEU
SEQRES 5 D 289 ASN ALA ARG ARG PRO ASN SER ALA ILE THR VAL GLN ALA
SEQRES 6 D 289 ASP LEU SER ASN VAL ALA THR ALA SER PHE SER GLU THR
SEQRES 7 D 289 ASP GLY SER VAL PRO VAL THR LEU PHE SER ARG CYS SER
SEQRES 8 D 289 ALA LEU VAL ASP ALA CYS TYR MET HIS TRP GLY ARG CYS
SEQRES 9 D 289 ASP VAL LEU VAL ASN ASN ALA SER SER PHE TYR PRO THR
SEQRES 10 D 289 PRO LEU LEU ARG LYS ASP ALA GLY GLU GLY GLY SER SER
SEQRES 11 D 289 VAL GLY ASP LYS GLU SER LEU GLU VAL ALA ALA ALA ASP
SEQRES 12 D 289 LEU PHE GLY SER ASN ALA ILE ALA PRO TYR PHE LEU ILE
SEQRES 13 D 289 LYS ALA PHE ALA GLN ARG VAL ALA ASP THR ARG ALA GLU
SEQRES 14 D 289 GLN ARG GLY THR SER TYR SER ILE VAL ASN MET VAL ASP
SEQRES 15 D 289 ALA MET THR SER GLN PRO LEU LEU GLY TYR THR MET TYR
SEQRES 16 D 289 THR MET ALA LYS GLU ALA LEU GLU GLY LEU THR ARG SER
SEQRES 17 D 289 ALA ALA LEU GLU LEU ALA SER LEU GLN ILE ARG VAL ASN
SEQRES 18 D 289 GLY VAL SER PRO GLY LEU SER VAL LEU PRO ASP ASP MET
SEQRES 19 D 289 PRO PHE SER VAL GLN GLU ASP TYR ARG ARG LYS VAL PRO
SEQRES 20 D 289 LEU TYR GLN ARG ASN SER SER ALA GLU GLU VAL SER ASP
SEQRES 21 D 289 VAL VAL ILE PHE LEU CYS SER PRO LYS ALA LYS TYR ILE
SEQRES 22 D 289 THR GLY THR CYS ILE LYS VAL ASP GLY GLY TYR SER LEU
SEQRES 23 D 289 THR ARG ALA
HET NDP A 300 48
HET MTX A 351 33
HET NDP B 301 48
HET MTX B 352 33
HET NDP C 302 48
HET MTX C 353 33
HET NDP D 303 48
HET MTX D 354 33
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM MTX METHOTREXATE
FORMUL 5 NDP 4(C21 H30 N7 O17 P3)
FORMUL 6 MTX 4(C20 H22 N8 O5)
FORMUL 13 HOH *173(H2 O)
HELIX 1 1 LYS A 16 GLU A 29 1 14
HELIX 2 2 SER A 40 ARG A 55 1 16
HELIX 3 3 THR A 84 GLY A 101 1 18
HELIX 4 4 GLU A 134 ALA A 148 1 15
HELIX 5 5 ALA A 148 ASP A 164 1 17
HELIX 6 6 ARG A 166 ARG A 170 5 5
HELIX 7 7 TYR A 191 ALA A 213 1 23
HELIX 8 8 PRO A 234 ARG A 243 1 10
HELIX 9 9 SER A 253 SER A 266 1 14
HELIX 10 10 PRO A 267 LYS A 270 5 4
HELIX 11 11 GLY A 282 THR A 286 5 5
HELIX 12 12 LYS B 16 GLU B 29 1 14
HELIX 13 13 SER B 40 ARG B 55 1 16
HELIX 14 14 LEU B 85 GLY B 101 1 17
HELIX 15 15 GLU B 134 ALA B 148 1 15
HELIX 16 16 ALA B 148 ASP B 164 1 17
HELIX 17 17 ARG B 166 ARG B 170 5 5
HELIX 18 18 TYR B 191 ALA B 213 1 23
HELIX 19 19 SER B 214 GLN B 216 5 3
HELIX 20 20 PRO B 234 ARG B 243 1 10
HELIX 21 21 SER B 253 SER B 266 1 14
HELIX 22 22 GLY B 282 THR B 286 5 5
HELIX 23 23 LYS C 16 GLU C 29 1 14
HELIX 24 24 SER C 40 ARG C 55 1 16
HELIX 25 25 THR C 84 GLY C 101 1 18
HELIX 26 26 LYS C 133 ALA C 148 1 16
HELIX 27 27 ALA C 148 ASP C 164 1 17
HELIX 28 28 TYR C 191 ALA C 213 1 23
HELIX 29 29 PRO C 234 ARG C 243 1 10
HELIX 30 30 SER C 253 CYS C 265 1 13
HELIX 31 31 SER C 266 LYS C 270 5 5
HELIX 32 32 GLY C 282 THR C 286 5 5
HELIX 33 33 LYS D 16 GLU D 29 1 14
HELIX 34 34 SER D 40 ARG D 55 1 16
HELIX 35 35 THR D 84 MET D 98 1 15
HELIX 36 36 ASP D 132 ALA D 148 1 17
HELIX 37 37 ALA D 148 THR D 165 1 18
HELIX 38 38 ARG D 166 ARG D 170 5 5
HELIX 39 39 TYR D 191 ALA D 213 1 23
HELIX 40 40 PRO D 234 ARG D 243 1 10
HELIX 41 41 SER D 253 SER D 266 1 14
HELIX 42 42 PRO D 267 LYS D 270 5 4
HELIX 43 43 GLY D 282 THR D 286 5 5
SHEET 1 A 7 ALA A 59 GLN A 63 0
SHEET 2 A 7 THR A 32 TYR A 37 1 N LEU A 35 O ILE A 60
SHEET 3 A 7 VAL A 8 VAL A 11 1 N ALA A 9 O CYS A 34
SHEET 4 A 7 VAL A 105 ASN A 108 1 O VAL A 105 N LEU A 10
SHEET 5 A 7 SER A 175 MET A 179 1 O VAL A 177 N LEU A 106
SHEET 6 A 7 ARG A 218 PRO A 224 1 O ASN A 220 N ASN A 178
SHEET 7 A 7 CYS A 276 VAL A 279 1 O ILE A 277 N GLY A 221
SHEET 1 B 7 ALA B 59 GLN B 63 0
SHEET 2 B 7 THR B 32 TYR B 37 1 N LEU B 35 O ILE B 60
SHEET 3 B 7 VAL B 8 VAL B 11 1 N ALA B 9 O CYS B 34
SHEET 4 B 7 VAL B 105 ASN B 108 1 O VAL B 105 N LEU B 10
SHEET 5 B 7 SER B 175 MET B 179 1 O VAL B 177 N LEU B 106
SHEET 6 B 7 ARG B 218 PRO B 224 1 O ASN B 220 N ASN B 178
SHEET 7 B 7 CYS B 276 VAL B 279 1 O ILE B 277 N SER B 223
SHEET 1 C 2 ALA B 70 THR B 71 0
SHEET 2 C 2 VAL B 83 THR B 84 -1 O VAL B 83 N THR B 71
SHEET 1 D 7 ALA C 59 GLN C 63 0
SHEET 2 D 7 THR C 32 TYR C 37 1 N LEU C 35 O ILE C 60
SHEET 3 D 7 VAL C 8 VAL C 11 1 N ALA C 9 O CYS C 34
SHEET 4 D 7 VAL C 105 ASN C 108 1 O VAL C 105 N LEU C 10
SHEET 5 D 7 TYR C 174 MET C 179 1 O VAL C 177 N LEU C 106
SHEET 6 D 7 ILE C 217 PRO C 224 1 O ARG C 218 N ILE C 176
SHEET 7 D 7 CYS C 276 VAL C 279 1 O ILE C 277 N SER C 223
SHEET 1 E 7 ALA D 59 ILE D 60 0
SHEET 2 E 7 THR D 32 LEU D 35 1 N VAL D 33 O ILE D 60
SHEET 3 E 7 VAL D 8 VAL D 11 1 N ALA D 9 O CYS D 34
SHEET 4 E 7 VAL D 105 ASN D 108 1 O VAL D 105 N LEU D 10
SHEET 5 E 7 SER D 175 MET D 179 1 O VAL D 177 N LEU D 106
SHEET 6 E 7 ARG D 218 PRO D 224 1 O ASN D 220 N ILE D 176
SHEET 7 E 7 CYS D 276 VAL D 279 1 O ILE D 277 N GLY D 221
SITE 1 AC1 28 GLY A 13 ARG A 17 LEU A 18 HIS A 38
SITE 2 AC1 28 ARG A 39 SER A 40 ALA A 64 ASP A 65
SITE 3 AC1 28 LEU A 66 SER A 67 ASN A 109 ALA A 110
SITE 4 AC1 28 SER A 111 SER A 112 ASP A 142 MET A 179
SITE 5 AC1 28 VAL A 180 ASP A 181 TYR A 194 LYS A 198
SITE 6 AC1 28 PRO A 224 GLY A 225 LEU A 226 SER A 227
SITE 7 AC1 28 MTX A 351 HOH A 400 HOH A 473 HOH A 541
SITE 1 AC2 27 GLY B 13 LYS B 16 ARG B 17 LEU B 18
SITE 2 AC2 27 HIS B 36 HIS B 38 ARG B 39 SER B 40
SITE 3 AC2 27 ALA B 64 ASP B 65 LEU B 66 SER B 67
SITE 4 AC2 27 ASN B 109 ALA B 110 SER B 111 SER B 112
SITE 5 AC2 27 ASP B 142 MET B 179 VAL B 180 TYR B 194
SITE 6 AC2 27 LYS B 198 PRO B 224 GLY B 225 SER B 227
SITE 7 AC2 27 VAL B 228 MTX B 352 HOH B 412
SITE 1 AC3 27 GLY C 13 ALA C 15 ARG C 17 LEU C 18
SITE 2 AC3 27 TYR C 37 HIS C 38 ARG C 39 SER C 40
SITE 3 AC3 27 ASP C 65 LEU C 66 SER C 67 ASN C 109
SITE 4 AC3 27 ALA C 110 SER C 111 SER C 112 ASP C 142
SITE 5 AC3 27 SER C 146 MET C 179 VAL C 180 TYR C 194
SITE 6 AC3 27 LYS C 198 PRO C 224 GLY C 225 LEU C 226
SITE 7 AC3 27 SER C 227 VAL C 228 MTX C 353
SITE 1 AC4 24 GLY D 13 ALA D 15 ARG D 17 LEU D 18
SITE 2 AC4 24 HIS D 38 ARG D 39 SER D 40 LEU D 66
SITE 3 AC4 24 SER D 67 ASN D 109 ALA D 110 SER D 111
SITE 4 AC4 24 SER D 112 ASP D 142 MET D 179 VAL D 180
SITE 5 AC4 24 TYR D 194 LYS D 198 PRO D 224 GLY D 225
SITE 6 AC4 24 SER D 227 VAL D 228 MTX D 354 HOH D 428
SITE 1 AC5 14 ARG A 17 SER A 111 PHE A 113 PRO A 115
SITE 2 AC5 14 ASP A 181 LEU A 188 TYR A 191 TYR A 194
SITE 3 AC5 14 LEU A 226 LEU A 229 PRO A 230 TYR A 241
SITE 4 AC5 14 NDP A 300 HOH A 484
SITE 1 AC6 13 ARG B 17 SER B 111 PHE B 113 PRO B 115
SITE 2 AC6 13 ASP B 181 LEU B 188 TYR B 191 TYR B 194
SITE 3 AC6 13 LEU B 226 PRO B 230 MET B 233 TYR B 241
SITE 4 AC6 13 NDP B 301
SITE 1 AC7 14 ARG C 17 SER C 111 PHE C 113 PRO C 115
SITE 2 AC7 14 ASP C 181 LEU C 188 TYR C 191 TYR C 194
SITE 3 AC7 14 LEU C 226 LEU C 229 PRO C 230 MET C 233
SITE 4 AC7 14 TYR C 241 NDP C 302
SITE 1 AC8 13 ARG D 17 SER D 111 PHE D 113 PRO D 115
SITE 2 AC8 13 ASP D 181 TYR D 191 TYR D 194 LEU D 229
SITE 3 AC8 13 PRO D 230 MET D 233 TYR D 241 NDP D 303
SITE 4 AC8 13 HOH D 509
CRYST1 91.301 96.103 195.545 90.00 90.00 90.00 P 21 21 21 16
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 0.010953 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010406 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005114 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
