HEADER OXIDOREDUCTASE 07-MAR-14 4PST
TITLE MULTICONFORMER MODEL FOR ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE AT
TITLE 2 277 K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 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 D.A.KEEDY,H.VAN DEN BEDEM,D.A.SIVAK,G.A.PETSKO,D.RINGE,M.A.WILSON,
AUTHOR 2 J.S.FRASER
REVDAT 4 20-SEP-23 4PST 1 REMARK LINK
REVDAT 3 19-NOV-14 4PST 1 HET HETATM HETSYN
REVDAT 2 25-JUN-14 4PST 1 JRNL
REVDAT 1 04-JUN-14 4PST 0
JRNL AUTH D.A.KEEDY,H.VAN DEN BEDEM,D.A.SIVAK,G.A.PETSKO,D.RINGE,
JRNL AUTH 2 M.A.WILSON,J.S.FRASER
JRNL TITL CRYSTAL CRYOCOOLING DISTORTS CONFORMATIONAL HETEROGENEITY IN
JRNL TITL 2 A MODEL MICHAELIS COMPLEX OF DHFR.
JRNL REF STRUCTURE V. 22 899 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 24882744
JRNL DOI 10.1016/J.STR.2014.04.016
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4-1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 71709
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.121
REMARK 3 R VALUE (WORKING SET) : 0.121
REMARK 3 FREE R VALUE : 0.142
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3666
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 1.0640 - 1.0500 0.97 0 135 0.1270 0.1490
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.50
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 15.285 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085176.
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) : 49.400
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HH TYR A 128 O HOH A 457 1.36
REMARK 500 HE2 HIS A 124 O HOH A 367 1.40
REMARK 500 HZ3 LYS A 106 O HOH A 497 1.46
REMARK 500 HD1 HIS A 124 O HOH A 331 1.53
REMARK 500 HZ3 LYS A 106 O HOH A 451 1.56
REMARK 500 HE22 GLN A 102 O HOH A 452 1.59
REMARK 500 HG SER A 135 OE2 GLU A 154 1.59
REMARK 500 HD1 HIS A 45 O HOH A 336 1.60
REMARK 500 OD2 ASP A 79 O HOH A 333 1.99
REMARK 500 OH TYR A 128 O HOH A 457 2.01
REMARK 500 O HOH A 416 O HOH A 464 2.02
REMARK 500 OE1 GLN A 108 O HOH A 401 2.03
REMARK 500 NH1 ARG A 52 O HOH A 498 2.07
REMARK 500 O HOH A 457 O HOH A 482 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 116 O HOH A 386 3745 1.95
REMARK 500 OD1 ASP A 87 O HOH A 458 4475 2.06
REMARK 500 O HOH A 458 O HOH A 483 4475 2.15
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 12 18.41 55.64
REMARK 500 PRO A 21 55.73 -95.51
REMARK 500 ASP A 69 108.45 -167.98
REMARK 500 ASP A 69 112.11 -164.83
REMARK 500 ASP A 69 117.23 -165.44
REMARK 500 GLU A 139 110.22 -163.46
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 ASP A 116 O 11.1
REMARK 620 3 ASP A 116 O 11.0 11.2
REMARK 620 4 ASP A 116 O 12.0 8.9 18.5
REMARK 620 5 HIS A 149 ND1 94.4 93.6 103.7 85.3
REMARK 620 6 HIS A 149 ND1 87.3 87.8 97.2 79.1 9.0
REMARK 620 7 HOH A 396 O 88.8 77.9 81.9 82.1 97.1 102.6
REMARK 620 8 HOH A 459 O 80.5 81.4 71.3 89.7 174.9 166.6 83.0
REMARK 620 9 HOH A 463 O 164.1 155.8 153.1 161.6 97.7 105.6 79.5 87.3
REMARK 620 N 1 2 3 4 5 6 7 8
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 462 O 155.9
REMARK 620 N 1
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: 4PSS RELATED DB: PDB
REMARK 900 MULTICONFORMER MODEL FOR ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE
REMARK 900 AT 100K
DBREF 4PST 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 4PST CSD A 152 CYS 3-SULFINOALANINE
HET CSD A 152 11
HET FOL A 201 101
HET NAP A 202 146
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 *199(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 GLY A 86 1 10
HELIX 5 5 GLY A 96 LEU A 104 1 9
HELIX 6 6 GLU A 129 ASP A 131 5 3
SHEET 1 A 8 THR A 73 VAL A 75 0
SHEET 2 A 8 LYS A 58 LEU A 62 1 N ILE A 61 O THR A 73
SHEET 3 A 8 PRO A 39 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 ILE A 115 N LEU A 8
SHEET 7 A 8 TYR A 151 ARG A 158 -1 O LEU A 156 N LEU A 110
SHEET 8 A 8 TRP A 133 HIS A 141 -1 N GLU A 139 O PHE A 153
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 DTYR A 151 N CSD A 152 1555 1555 1.33
LINK C CSD A 152 N PHE A 153 1555 1555 1.33
LINK O AASP A 116 MN MN A 203 1555 1555 2.06
LINK O BASP A 116 MN MN A 203 1555 1555 2.22
LINK O CASP A 116 MN MN A 203 1555 1555 2.27
LINK O DASP A 116 MN MN A 203 1555 1555 2.36
LINK ND1CHIS A 149 MN MN A 203 1555 1555 2.08
LINK ND1AHIS A 149 MN MN A 203 1555 1555 2.43
LINK OE2 GLU A 154 MN MN A 204 1555 1555 2.33
LINK MN MN A 203 O HOH A 396 1555 1555 2.31
LINK MN MN A 203 O HOH A 459 1555 1555 2.20
LINK MN MN A 203 O HOH A 463 1555 1555 2.09
LINK MN MN A 204 O HOH A 462 1555 1555 2.48
CISPEP 1 GLY A 95 GLY A 96 0 7.93
SITE 1 AC1 22 ILE A 5 ALA A 6 ALA A 7 MET A 20
SITE 2 AC1 22 ASP A 27 LEU A 28 PHE A 31 LYS A 32
SITE 3 AC1 22 ILE A 50 LEU A 54 ARG A 57 ILE A 94
SITE 4 AC1 22 THR A 113 NAP A 202 HOH A 301 HOH A 308
SITE 5 AC1 22 HOH A 342 HOH A 373 HOH A 392 HOH A 470
SITE 6 AC1 22 HOH A 492 HOH A 493
SITE 1 AC2 38 ALA A 6 ALA A 7 ILE A 14 GLY A 15
SITE 2 AC2 38 ASN A 18 ALA A 19 MET A 20 GLY A 43
SITE 3 AC2 38 ARG A 44 HIS A 45 THR A 46 SER A 49
SITE 4 AC2 38 LEU A 62 SER A 63 SER A 64 GLN A 65
SITE 5 AC2 38 LYS A 76 ILE A 94 GLY A 96 GLY A 97
SITE 6 AC2 38 ARG A 98 VAL A 99 TYR A 100 GLN A 102
SITE 7 AC2 38 THR A 123 ASP A 131 FOL A 201 HOH A 302
SITE 8 AC2 38 HOH A 312 HOH A 337 HOH A 373 HOH A 378
SITE 9 AC2 38 HOH A 383 HOH A 419 HOH A 420 HOH A 434
SITE 10 AC2 38 HOH A 445 HOH A 461
SITE 1 AC3 6 ASP A 116 HIS A 149 ARG A 159 HOH A 396
SITE 2 AC3 6 HOH A 459 HOH A 463
SITE 1 AC4 3 GLU A 154 HOH A 460 HOH A 462
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