HEADER OXIDOREDUCTASE 09-AUG-13 4M6K
TITLE CRYSTAL STRUCTURE OF HUMAN DIHYDROFOLATE REDUCTASE (DHFR) BOUND TO
TITLE 2 NADP+ AND FOLATE
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: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DHFR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PDNAY;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS ROSSMANN FOLD, NADPH BINDING, FOLATE BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BHABHA,D.C.EKIERT,P.E.WRIGHT,I.A.WILSON
REVDAT 4 20-SEP-23 4M6K 1 REMARK
REVDAT 3 20-NOV-13 4M6K 1 JRNL
REVDAT 2 16-OCT-13 4M6K 1 JRNL
REVDAT 1 25-SEP-13 4M6K 0
JRNL AUTH G.BHABHA,D.C.EKIERT,M.JENNEWEIN,C.M.ZMASEK,L.M.TUTTLE,
JRNL AUTH 2 G.KROON,H.J.DYSON,A.GODZIK,I.A.WILSON,P.E.WRIGHT
JRNL TITL DIVERGENT EVOLUTION OF PROTEIN CONFORMATIONAL DYNAMICS IN
JRNL TITL 2 DIHYDROFOLATE REDUCTASE.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 20 1243 2013
JRNL REFN ISSN 1545-9993
JRNL PMID 24077226
JRNL DOI 10.1038/NSMB.2676
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 44348
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2276
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 23.7730 - 3.5152 1.00 2943 140 0.1673 0.1931
REMARK 3 2 3.5152 - 2.7915 1.00 2755 140 0.1491 0.1805
REMARK 3 3 2.7915 - 2.4391 1.00 2666 154 0.1396 0.1689
REMARK 3 4 2.4391 - 2.2162 1.00 2664 158 0.1274 0.1695
REMARK 3 5 2.2162 - 2.0575 1.00 2659 140 0.1153 0.1511
REMARK 3 6 2.0575 - 1.9362 1.00 2639 131 0.1063 0.1516
REMARK 3 7 1.9362 - 1.8393 1.00 2614 151 0.1092 0.1549
REMARK 3 8 1.8393 - 1.7593 1.00 2600 154 0.1134 0.1738
REMARK 3 9 1.7593 - 1.6916 1.00 2639 132 0.1183 0.1681
REMARK 3 10 1.6916 - 1.6332 1.00 2609 124 0.1277 0.1963
REMARK 3 11 1.6332 - 1.5821 1.00 2600 135 0.1335 0.2014
REMARK 3 12 1.5821 - 1.5369 1.00 2576 152 0.1495 0.2349
REMARK 3 13 1.5369 - 1.4965 1.00 2580 156 0.1724 0.2429
REMARK 3 14 1.4965 - 1.4600 1.00 2591 145 0.2148 0.2682
REMARK 3 15 1.4600 - 1.4268 1.00 2574 125 0.2418 0.3326
REMARK 3 16 1.4268 - 1.3960 0.91 2363 139 0.2834 0.3372
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.50
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 : 0.009 1780
REMARK 3 ANGLE : 1.410 2435
REMARK 3 CHIRALITY : 0.084 254
REMARK 3 PLANARITY : 0.006 311
REMARK 3 DIHEDRAL : 14.484 717
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 4M6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44528
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.396
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 19.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 19.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.79000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4M6J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 100 MM
REMARK 280 PHOSPHATE/CITRATE, PH 4.2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.08150
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 80.08150
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.08150
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 80.08150
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 80.08150
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 80.08150
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 348 LIES ON A SPECIAL POSITION.
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 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 ASP A 110 -95.98 -99.08
REMARK 500 MET A 139 50.81 -90.85
REMARK 500 MET A 139 54.46 -93.70
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 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 GOL A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M6J RELATED DB: PDB
REMARK 900 RELATED ID: 4M6L RELATED DB: PDB
DBREF 4M6K A 0 186 UNP P00374 DYR_HUMAN 1 187
SEQRES 1 A 187 MET VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN
SEQRES 2 A 187 ASN MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO
SEQRES 3 A 187 PRO LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR
SEQRES 4 A 187 THR THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE
SEQRES 5 A 187 MET GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN
SEQRES 6 A 187 ARG PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG
SEQRES 7 A 187 GLU LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER
SEQRES 8 A 187 ARG SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO
SEQRES 9 A 187 GLU LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY
SEQRES 10 A 187 GLY SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY
SEQRES 11 A 187 HIS LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE
SEQRES 12 A 187 GLU SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS
SEQRES 13 A 187 TYR LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP
SEQRES 14 A 187 VAL GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL
SEQRES 15 A 187 TYR GLU LYS ASN ASP
HET FOL A 201 32
HET NAP A 202 48
HET GOL A 203 6
HETNAM FOL FOLIC ACID
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM GOL GLYCEROL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 FOL C19 H19 N7 O6
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *206(H2 O)
HELIX 1 1 LEU A 27 THR A 40 1 14
HELIX 2 2 LYS A 54 ILE A 60 1 7
HELIX 3 3 PRO A 61 ARG A 65 5 5
HELIX 4 4 SER A 92 GLN A 102 1 11
HELIX 5 5 GLN A 102 ASN A 107 1 6
HELIX 6 6 GLY A 117 HIS A 127 1 11
SHEET 1 A 8 PHE A 88 SER A 90 0
SHEET 2 A 8 ILE A 71 LEU A 75 1 N VAL A 74 O PHE A 88
SHEET 3 A 8 GLN A 47 GLY A 53 1 N VAL A 50 O ILE A 71
SHEET 4 A 8 VAL A 109 ILE A 114 1 O TRP A 113 N LEU A 49
SHEET 5 A 8 LEU A 4 SER A 11 1 N ASN A 5 O ILE A 114
SHEET 6 A 8 LEU A 131 ILE A 138 1 O THR A 136 N VAL A 10
SHEET 7 A 8 ILE A 175 LYS A 184 -1 O LYS A 178 N ARG A 137
SHEET 8 A 8 LYS A 157 LEU A 158 -1 N LYS A 157 O GLU A 183
SHEET 1 B 8 PHE A 88 SER A 90 0
SHEET 2 B 8 ILE A 71 LEU A 75 1 N VAL A 74 O PHE A 88
SHEET 3 B 8 GLN A 47 GLY A 53 1 N VAL A 50 O ILE A 71
SHEET 4 B 8 VAL A 109 ILE A 114 1 O TRP A 113 N LEU A 49
SHEET 5 B 8 LEU A 4 SER A 11 1 N ASN A 5 O ILE A 114
SHEET 6 B 8 LEU A 131 ILE A 138 1 O THR A 136 N VAL A 10
SHEET 7 B 8 ILE A 175 LYS A 184 -1 O LYS A 178 N ARG A 137
SHEET 8 B 8 GLN A 170 GLU A 172 -1 N GLN A 170 O TYR A 177
SHEET 1 C 2 GLY A 15 GLY A 17 0
SHEET 2 C 2 THR A 146 PHE A 147 -1 O THR A 146 N ILE A 16
CISPEP 1 ARG A 65 PRO A 66 0 -7.85
CISPEP 2 GLY A 116 GLY A 117 0 7.29
SITE 1 AC1 20 ILE A 7 VAL A 8 ALA A 9 LEU A 22
SITE 2 AC1 20 GLU A 30 PHE A 31 ARG A 32 PHE A 34
SITE 3 AC1 20 GLN A 35 ASN A 64 LEU A 67 ARG A 70
SITE 4 AC1 20 VAL A 115 THR A 136 NAP A 202 HOH A 314
SITE 5 AC1 20 HOH A 324 HOH A 361 HOH A 380 HOH A 435
SITE 1 AC2 32 VAL A 8 ALA A 9 ILE A 16 GLY A 17
SITE 2 AC2 32 GLY A 20 ASP A 21 LEU A 22 GLY A 53
SITE 3 AC2 32 LYS A 54 LYS A 55 THR A 56 LEU A 75
SITE 4 AC2 32 SER A 76 ARG A 77 GLU A 78 ARG A 91
SITE 5 AC2 32 VAL A 115 GLY A 117 SER A 118 SER A 119
SITE 6 AC2 32 TYR A 121 THR A 146 FOL A 201 HOH A 324
SITE 7 AC2 32 HOH A 329 HOH A 340 HOH A 360 HOH A 382
SITE 8 AC2 32 HOH A 414 HOH A 434 HOH A 451 HOH A 465
SITE 1 AC3 10 SER A 3 ASN A 5 MET A 111 LYS A 132
SITE 2 AC3 10 PHE A 134 TYR A 162 ASP A 186 HOH A 365
SITE 3 AC3 10 HOH A 368 HOH A 440
CRYST1 68.213 68.213 160.163 90.00 90.00 120.00 P 63 2 2 12
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 0.014660 0.008464 0.000000 0.00000
SCALE2 0.000000 0.016928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006244 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
