HEADER OXIDOREDUCTASE 24-OCT-96 1RF7
TITLE STRUCTURE OF DIHYDROFOLATE REDUCTASE COMPLEXED WITH DIHYDROFOLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DHFR;
COMPND 5 EC: 1.5.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: RT500;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PRWA-1
KEYWDS OXIDOREDUCTASE, NADP, TRIMETHOPRIM RESISTANCE, METHOTREXATE
KEYWDS 2 RESISTANCE, ONE-CARBON METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.SAWAYA
REVDAT 3 09-AUG-23 1RF7 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1RF7 1 VERSN
REVDAT 1 12-MAR-97 1RF7 0
JRNL AUTH M.R.SAWAYA,J.KRAUT
JRNL TITL LOOP AND SUBDOMAIN MOVEMENTS IN THE MECHANISM OF ESCHERICHIA
JRNL TITL 2 COLI DIHYDROFOLATE REDUCTASE: CRYSTALLOGRAPHIC EVIDENCE.
JRNL REF BIOCHEMISTRY V. 36 586 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9012674
JRNL DOI 10.1021/BI962337C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.M.REYES,M.R.SAWAYA,K.A.BROWN,J.KRAUT
REMARK 1 TITL ISOMORPHOUS CRYSTAL STRUCTURES OF ESCHERICHIA COLI
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE,
REMARK 1 TITL 3 5-DEAZAFOLATE, AND 5,10-DIDEAZATETRAHYDROFOLATE: MECHANISTIC
REMARK 1 TITL 4 IMPLICATIONS
REMARK 1 REF BIOCHEMISTRY V. 34 2710 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.BYSTROFF,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL
REMARK 1 TITL 3 CHANGES AND COOPERATIVITY IN BINDING
REMARK 1 REF BIOCHEMISTRY V. 30 2227 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.BYSTROFF,S.J.OATLEY,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE
REMARK 1 TITL 2 REDUCTASE: THE NADP+ HOLOENZYME AND THE FOLATE.NADP+ TERNARY
REMARK 1 TITL 3 COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION
REMARK 1 TITL 4 STATE
REMARK 1 REF BIOCHEMISTRY V. 29 3263 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT 5D
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 14125
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
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) : 0.170
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 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1700
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) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1268
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 134
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.018 ; 0.020 ; 1367
REMARK 3 BOND ANGLES (DEGREES) : 3.010 ; 3.000 ; 1851
REMARK 3 TORSION ANGLES (DEGREES) : 23.100; NULL ; 765
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.018 ; 0.020 ; 41
REMARK 3 GENERAL PLANES (A) : 0.007 ; 0.020 ; 191
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 5.900 ; NULL ; 1367
REMARK 3 NON-BONDED CONTACTS (A) : 0.014 ; 0.100 ; 21
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : MOEWS AND KRETSINGER
REMARK 3 KSOL : 0.81
REMARK 3 BSOL : 191.0
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RF7 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_1000176064.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NOV-95
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.6
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 : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : UCSD
REMARK 200 DATA SCALING SOFTWARE : UCSD
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14125
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.14300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.210
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT
REMARK 200 STARTING MODEL: PDB ENTRY 1RX7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.6
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 17.35250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.41350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.45850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.41350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.35250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 19.45850
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 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 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 ASP A 11 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 ASP A 27 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ASP A 37 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 37 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 SER A 64 CB - CA - C ANGL. DEV. = -14.3 DEGREES
REMARK 500 ASP A 79 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 79 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 87 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 98 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 116 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLU A 120 N - CA - CB ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP A 122 CB - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP A 122 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP A 127 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 132 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 SER A 138 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 142 CB - CG - OD2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASP A 144 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 144 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 5.7 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 GLU A 139 119.61 -160.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THERE ARE TWO MOLECULES OF DIHYDROFOLATE IN THIS
REMARK 600 COORDINATE SET. ONE MOLECULE IS BOUND IN THE ACTIVE SITE
REMARK 600 THE OTHER MOLECULE IS BOUND IN THE INTERSTICES. IT
REMARK 600 APPEARS TO HAVE REACTED WITH CYS 152.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DHF A 161
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 MN A 300 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 17 OE1
REMARK 620 2 ASN A 18 OD1 80.2
REMARK 620 3 ASP A 70 OD2 110.5 113.0
REMARK 620 4 HOH A 360 O 153.3 86.0 95.9
REMARK 620 5 HOH A 377 O 73.3 153.3 80.7 116.5
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 CL A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHF A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHF A 163
DBREF 1RF7 A 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
SEQADV 1RF7 ASP A 37 UNP P0ABQ4 ASN 37 CONFLICT
SEQRES 1 A 159 MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL
SEQRES 2 A 159 ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA
SEQRES 3 A 159 ASP LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO
SEQRES 4 A 159 VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG
SEQRES 5 A 159 PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN
SEQRES 6 A 159 PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL
SEQRES 7 A 159 ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE
SEQRES 8 A 159 MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU
SEQRES 9 A 159 PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA
SEQRES 10 A 159 GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO
SEQRES 11 A 159 ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA
SEQRES 12 A 159 ASP ALA GLN ASN SER HIS SER TYR CYS PHE GLU ILE LEU
SEQRES 13 A 159 GLU ARG ARG
HET CL A 299 1
HET MN A 300 1
HET DHF A 161 29
HET DHF A 163 32
HETNAM CL CHLORIDE ION
HETNAM MN MANGANESE (II) ION
HETNAM DHF DIHYDROFOLIC ACID
FORMUL 2 CL CL 1-
FORMUL 3 MN MN 2+
FORMUL 4 DHF 2(C19 H21 N7 O6)
FORMUL 6 HOH *134(H2 O)
HELIX 1 2 PRO A 25 THR A 35 1 11
HELIX 2 3 ARG A 44 ILE A 50 1 7
HELIX 3 4 VAL A 78 CYS A 85 1 8
HELIX 4 5 GLY A 97 LYS A 106 1 10
SHEET 1 A 8 TRP A 133 SER A 135 0
SHEET 2 A 8 TYR A 151 ARG A 158 -1 N GLU A 157 O GLU A 134
SHEET 3 A 8 ALA A 107 ILE A 115 -1 N HIS A 114 O CYS A 152
SHEET 4 A 8 ILE A 2 ILE A 5 1 N ILE A 2 N TYR A 111
SHEET 5 A 8 ILE A 91 GLY A 95 1 N ILE A 91 O SER A 3
SHEET 6 A 8 PRO A 39 GLY A 43 1 N PRO A 39 O MET A 92
SHEET 7 A 8 LYS A 58 LEU A 62 1 N LYS A 58 O VAL A 40
SHEET 8 A 8 THR A 73 VAL A 75 1 N THR A 73 O ILE A 61
LINK SG CYS A 152 C9 DHF A 163 1555 1555 2.01
LINK OE1 GLU A 17 MN MN A 300 4475 1555 2.56
LINK OD1 ASN A 18 MN MN A 300 4475 1555 2.06
LINK OD2 ASP A 70 MN MN A 300 1555 1555 2.39
LINK MN MN A 300 O HOH A 360 1555 4575 2.68
LINK MN MN A 300 O HOH A 377 1555 4575 2.42
CISPEP 1 GLY A 95 GLY A 96 0 3.28
SITE 1 AC1 4 GLY A 43 HIS A 45 THR A 46 GLY A 96
SITE 1 AC2 6 GLU A 17 ASN A 18 ASP A 70 GLY A 86
SITE 2 AC2 6 HOH A 360 HOH A 377
SITE 1 AC3 16 ILE A 5 ALA A 6 ALA A 7 ASP A 27
SITE 2 AC3 16 LEU A 28 PHE A 31 LYS A 32 ARG A 52
SITE 3 AC3 16 ARG A 57 ILE A 94 TYR A 100 THR A 113
SITE 4 AC3 16 HOH A 302 HOH A 308 HOH A 354 HOH A 425
SITE 1 AC4 16 VAL A 10 ASP A 11 ARG A 12 HIS A 114
SITE 2 AC4 16 ASP A 122 HIS A 124 PHE A 140 CYS A 152
SITE 3 AC4 16 GLU A 154 HOH A 323 HOH A 358 HOH A 376
SITE 4 AC4 16 HOH A 387 HOH A 398 HOH A 417 HOH A 423
CRYST1 34.705 38.917 108.827 90.00 90.00 90.00 P 21 21 21 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 0.028814 0.000000 0.000000 0.00000
SCALE2 0.000000 0.025696 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009189 0.00000
(ATOM LINES ARE NOT SHOWN.)
END