HEADER OXIDOREDUCTASE 29-SEP-14 4RGC
TITLE 277K CRYSTAL STRUCTURE OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 1403831;
SOURCE 4 GENE: BN896_0046, FOLA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.WILSON,Q.WAN,B.C.BENNETT,C.DEALWIS
REVDAT 5 20-SEP-23 4RGC 1 REMARK LINK
REVDAT 4 25-FEB-15 4RGC 1 JRNL
REVDAT 3 17-DEC-14 4RGC 1 JRNL
REVDAT 2 19-NOV-14 4RGC 1 HET HETATM HETNAM
REVDAT 1 15-OCT-14 4RGC 0
SPRSDE 15-OCT-14 4RGC 4PSZ
JRNL AUTH Q.WAN,B.C.BENNETT,M.A.WILSON,A.KOVALEVSKY,P.LANGAN,
JRNL AUTH 2 E.E.HOWELL,C.DEALWIS
JRNL TITL TOWARD RESOLVING THE CATALYTIC MECHANISM OF DIHYDROFOLATE
JRNL TITL 2 REDUCTASE USING NEUTRON AND ULTRAHIGH-RESOLUTION X-RAY
JRNL TITL 3 CRYSTALLOGRAPHY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 18225 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 25453083
JRNL DOI 10.1073/PNAS.1415856111
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.108
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.108
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.134
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3589
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 71709
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.104
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.103
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.127
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3205
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 64509
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1270
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1570.3
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1191.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 82
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 18313
REMARK 3 NUMBER OF RESTRAINTS : 30509
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.031
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.373
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.082
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.096
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.019
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.049
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.172
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: BABINET
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4RGC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000087311.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71782
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
REMARK 200 RESOLUTION RANGE LOW (A) : 49.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : 0.45800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: 1RX2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 400, 20 MM IMIDAZOLE PH 7.0,
REMARK 280 125 MM MNCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 17.14950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.35550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.76050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.35550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.14950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.76050
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: 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 12 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 33 CD - NE - CZ ANGL. DEV. = 19.9 DEGREES
REMARK 500 ARG A 44 CD - NE - CZ ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 87 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 159 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 4.1 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 ASN A 18 30.49 77.87
REMARK 500 PRO A 21 48.92 -82.94
REMARK 500 ASP A 69 115.11 -167.86
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 MN A 203 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 116 O
REMARK 620 2 HIS A 149 ND1 95.9
REMARK 620 3 HIS A 149 ND1 87.1 13.1
REMARK 620 4 HOH A 396 O 80.3 96.5 104.6
REMARK 620 5 HOH A 458 O 84.6 178.7 166.3 84.7
REMARK 620 6 HOH A 462 O 157.5 88.7 100.5 77.3 91.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 204 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 154 OE2
REMARK 620 2 HOH A 459 O 83.5
REMARK 620 3 HOH A 461 O 163.8 80.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PSY RELATED DB: PDB
REMARK 900 100K CRYSTAL STRUCTURE OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE
REMARK 900 RELATED ID: 4PST RELATED DB: PDB
REMARK 900 MULTICONFORMER MODEL AGAINST SAME DATASET
REMARK 900 RELATED ID: 4PTJ RELATED DB: PDB
REMARK 900 ENSEMBLE MODEL AGAINST SAME DATASET
DBREF 4RGC A 1 159 UNP U6N356 U6N356_ECOLI 1 159
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 ASN 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 CSD PHE GLU ILE LEU
SEQRES 13 A 159 GLU ARG ARG
MODRES 4RGC CSD A 152 CYS 3-SULFINOALANINE
HET CSD A 152 8
HET FOL A 201 32
HET NAP A 202 48
HET MN A 203 1
HET MN A 204 1
HETNAM CSD 3-SULFINOALANINE
HETNAM FOL FOLIC ACID
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM MN MANGANESE (II) ION
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 1 CSD C3 H7 N O4 S
FORMUL 2 FOL C19 H19 N7 O6
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 MN 2(MN 2+)
FORMUL 6 HOH *230(H2 O)
HELIX 1 1 ALA A 9 ASP A 11 5 3
HELIX 2 2 LEU A 24 LEU A 36 1 13
HELIX 3 3 ARG A 44 GLY A 51 1 8
HELIX 4 4 SER A 77 CYS A 85 1 9
HELIX 5 5 GLY A 96 LEU A 104 1 9
HELIX 6 6 PRO A 105 ALA A 107 5 3
HELIX 7 7 GLU A 129 ASP A 131 5 3
SHEET 1 A 8 THR A 73 VAL A 75 0
SHEET 2 A 8 ASN A 59 LEU A 62 1 N ILE A 61 O THR A 73
SHEET 3 A 8 VAL A 40 GLY A 43 1 N VAL A 40 O ILE A 60
SHEET 4 A 8 ILE A 91 VAL A 93 1 O MET A 92 N ILE A 41
SHEET 5 A 8 ILE A 2 LEU A 8 1 N SER A 3 O VAL A 93
SHEET 6 A 8 LYS A 109 ILE A 115 1 O THR A 113 N LEU A 8
SHEET 7 A 8 TYR A 151 ARG A 158 -1 O GLU A 154 N LEU A 112
SHEET 8 A 8 TRP A 133 HIS A 141 -1 N GLU A 134 O GLU A 157
SHEET 1 B 2 VAL A 13 GLY A 15 0
SHEET 2 B 2 THR A 123 HIS A 124 -1 O THR A 123 N ILE A 14
LINK C ATYR A 151 N CSD A 152 1555 1555 1.33
LINK C BTYR A 151 N CSD A 152 1555 1555 1.33
LINK C CSD A 152 N PHE A 153 1555 1555 1.30
LINK O ASP A 116 MN MN A 203 1555 1555 2.19
LINK ND1AHIS A 149 MN MN A 203 1555 1555 2.14
LINK ND1BHIS A 149 MN MN A 203 1555 1555 2.40
LINK OE2 GLU A 154 MN MN A 204 1555 1555 2.25
LINK MN MN A 203 O HOH A 396 1555 1555 2.29
LINK MN MN A 203 O HOH A 458 1555 1555 2.15
LINK MN MN A 203 O HOH A 462 1555 1555 1.98
LINK MN MN A 204 O HOH A 459 1555 1555 2.61
LINK MN MN A 204 O HOH A 461 1555 1555 2.15
CISPEP 1 GLY A 95 GLY A 96 0 6.90
SITE 1 AC1 20 ILE A 5 ALA A 6 ALA A 7 MET A 20
SITE 2 AC1 20 ASP A 27 LEU A 28 PHE A 31 LYS A 32
SITE 3 AC1 20 ILE A 50 ARG A 57 ILE A 94 THR A 113
SITE 4 AC1 20 NAP A 202 HOH A 301 HOH A 308 HOH A 342
SITE 5 AC1 20 HOH A 373 HOH A 392 HOH A 488 HOH A 495
SITE 1 AC2 35 ALA A 6 ALA A 7 ILE A 14 GLY A 15
SITE 2 AC2 35 ASN A 18 ALA A 19 MET A 20 GLY A 43
SITE 3 AC2 35 ARG A 44 HIS A 45 THR A 46 SER A 49
SITE 4 AC2 35 LEU A 62 SER A 63 SER A 64 LYS A 76
SITE 5 AC2 35 ILE A 94 GLY A 96 GLY A 97 ARG A 98
SITE 6 AC2 35 VAL A 99 TYR A 100 GLN A 102 ASP A 131
SITE 7 AC2 35 FOL A 201 HOH A 302 HOH A 312 HOH A 337
SITE 8 AC2 35 HOH A 373 HOH A 378 HOH A 383 HOH A 419
SITE 9 AC2 35 HOH A 444 HOH A 460 HOH A 496
SITE 1 AC3 6 ASP A 116 HIS A 149 ARG A 159 HOH A 396
SITE 2 AC3 6 HOH A 458 HOH A 462
SITE 1 AC4 3 GLU A 154 HOH A 459 HOH A 461
CRYST1 34.299 45.521 98.711 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 0.029155 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021968 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010131 0.00000
(ATOM LINES ARE NOT SHOWN.)
END