HEADER HYDROLASE 03-MAY-06 2GVU
TITLE CRYSTAL STRUCTURE OF DIISOPROPYL FLUOROPHOSPHATASE (DFPASE), MUTANT
TITLE 2 D229N / N120D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOTRIESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIISOPROPYL PHOSPHATASE, DFPASE;
COMPND 5 EC: 3.1.8.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LOLIGO VULGARIS;
SOURCE 3 ORGANISM_TAXID: 6622;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTRIESTERASE, BETA-PROPELLER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.H.CHEN,M.M.BLUM
REVDAT 4 20-OCT-21 2GVU 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2GVU 1 VERSN
REVDAT 2 10-OCT-06 2GVU 1 JRNL
REVDAT 1 19-SEP-06 2GVU 0
JRNL AUTH M.M.BLUM,F.LOHR,A.RICHARDT,H.RUTERJANS,J.C.CHEN
JRNL TITL BINDING OF A DESIGNED SUBSTRATE ANALOGUE TO DIISOPROPYL
JRNL TITL 2 FLUOROPHOSPHATASE: IMPLICATIONS FOR THE PHOSPHOTRIESTERASE
JRNL TITL 3 MECHANISM.
JRNL REF J.AM.CHEM.SOC. V. 128 12750 2006
JRNL REFN ISSN 0002-7863
JRNL PMID 17002369
JRNL DOI 10.1021/JA061887N
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.7
REMARK 3 NUMBER OF REFLECTIONS : 18472
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1357
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2451
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.31100
REMARK 3 B22 (A**2) : 5.17400
REMARK 3 B33 (A**2) : 3.13700
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.412 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.255 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.224 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.317 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 37.42
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GVU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 6.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19829
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 21.71500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.65000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.65000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.71500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.11500
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 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 1
REMARK 465 GLU A 2
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 ALA A 20 120.04 -25.01
REMARK 500 ALA A 45 41.24 -152.98
REMARK 500 ALA A 82 146.50 178.88
REMARK 500 SER A 147 43.67 -80.89
REMARK 500 ALA A 170 32.22 72.49
REMARK 500 PHE A 173 71.75 64.60
REMARK 500 ASN A 175 -95.18 -126.83
REMARK 500 THR A 195 -72.92 -42.38
REMARK 500 ASN A 229 -104.71 -116.92
REMARK 500 ASN A 237 30.22 72.60
REMARK 500 PRO A 266 32.67 -82.66
REMARK 500 LYS A 269 64.78 -116.60
REMARK 500 HIS A 274 143.64 -170.19
REMARK 500 PHE A 311 40.96 -106.47
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 CA A 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 21 OE2
REMARK 620 2 ASP A 120 OD1 127.9
REMARK 620 3 ASN A 175 OD1 150.9 74.2
REMARK 620 4 ASN A 229 OD1 82.0 146.3 72.6
REMARK 620 5 HOH A 523 O 80.1 69.2 128.7 139.5
REMARK 620 6 HOH A 524 O 85.3 81.8 79.3 86.5 127.5
REMARK 620 7 HOH A 578 O 121.1 93.6 68.6 79.7 79.0 147.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 232 OD1
REMARK 620 2 ASP A 232 OD2 38.4
REMARK 620 3 LEU A 273 O 118.3 80.6
REMARK 620 4 HIS A 274 ND1 94.0 96.1 102.6
REMARK 620 5 HOH A 527 O 154.6 164.6 84.6 91.2
REMARK 620 6 HOH A 555 O 55.1 93.2 172.6 82.1 101.2
REMARK 620 7 HOH A 613 O 84.4 87.4 84.7 172.3 87.0 90.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GVV RELATED DB: PDB
REMARK 900 STRUCTURE OF DIISOPROPYL FLUOROPHOSPHATASE IN COMPLEX WITH
REMARK 900 DICYCLOPENTYLPHOSPHOROAMIDATE (DCPPA)
REMARK 900 RELATED ID: 2GVW RELATED DB: PDB
REMARK 900 STRUCTURE OF DIISOPROPYL FLUOROPHOSPHATASE HOLOENZYME (RT)
DBREF 2GVU A 1 314 UNP Q7SIG4 DFPA_LOLVU 1 314
SEQADV 2GVU ASP A 120 UNP Q7SIG4 ASN 120 ENGINEERED MUTATION
SEQADV 2GVU ASN A 229 UNP Q7SIG4 ASP 229 ENGINEERED MUTATION
SEQRES 1 A 314 MET GLU ILE PRO VAL ILE GLU PRO LEU PHE THR LYS VAL
SEQRES 2 A 314 THR GLU ASP ILE PRO GLY ALA GLU GLY PRO VAL PHE ASP
SEQRES 3 A 314 LYS ASN GLY ASP PHE TYR ILE VAL ALA PRO GLU VAL GLU
SEQRES 4 A 314 VAL ASN GLY LYS PRO ALA GLY GLU ILE LEU ARG ILE ASP
SEQRES 5 A 314 LEU LYS THR GLY LYS LYS THR VAL ILE CYS LYS PRO GLU
SEQRES 6 A 314 VAL ASN GLY TYR GLY GLY ILE PRO ALA GLY CYS GLN CYS
SEQRES 7 A 314 ASP ARG ASP ALA ASN GLN LEU PHE VAL ALA ASP MET ARG
SEQRES 8 A 314 LEU GLY LEU LEU VAL VAL GLN THR ASP GLY THR PHE GLU
SEQRES 9 A 314 GLU ILE ALA LYS LYS ASP SER GLU GLY ARG ARG MET GLN
SEQRES 10 A 314 GLY CYS ASP ASP CYS ALA PHE ASP TYR GLU GLY ASN LEU
SEQRES 11 A 314 TRP ILE THR ALA PRO ALA GLY GLU VAL ALA PRO ALA ASP
SEQRES 12 A 314 TYR THR ARG SER MET GLN GLU LYS PHE GLY SER ILE TYR
SEQRES 13 A 314 CYS PHE THR THR ASP GLY GLN MET ILE GLN VAL ASP THR
SEQRES 14 A 314 ALA PHE GLN PHE PRO ASN GLY ILE ALA VAL ARG HIS MET
SEQRES 15 A 314 ASN ASP GLY ARG PRO TYR GLN LEU ILE VAL ALA GLU THR
SEQRES 16 A 314 PRO THR LYS LYS LEU TRP SER TYR ASP ILE LYS GLY PRO
SEQRES 17 A 314 ALA LYS ILE GLU ASN LYS LYS VAL TRP GLY HIS ILE PRO
SEQRES 18 A 314 GLY THR HIS GLU GLY GLY ALA ASN GLY MET ASP PHE ASP
SEQRES 19 A 314 GLU ASP ASN ASN LEU LEU VAL ALA ASN TRP GLY SER SER
SEQRES 20 A 314 HIS ILE GLU VAL PHE GLY PRO ASP GLY GLY GLN PRO LYS
SEQRES 21 A 314 MET ARG ILE ARG CYS PRO PHE GLU LYS PRO SER ASN LEU
SEQRES 22 A 314 HIS PHE LYS PRO GLN THR LYS THR ILE PHE VAL THR GLU
SEQRES 23 A 314 HIS GLU ASN ASN ALA VAL TRP LYS PHE GLU TRP GLN ARG
SEQRES 24 A 314 ASN GLY LYS LYS GLN TYR CYS GLU THR LEU LYS PHE GLY
SEQRES 25 A 314 ILE PHE
HET CA A 500 1
HET CA A 501 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
FORMUL 4 HOH *137(H2 O)
HELIX 1 1 GLN A 304 THR A 308 5 5
SHEET 1 A 5 VAL A 5 ILE A 6 0
SHEET 2 A 5 MET A 261 ARG A 264 1 O ARG A 264 N ILE A 6
SHEET 3 A 5 HIS A 248 PHE A 252 -1 N VAL A 251 O MET A 261
SHEET 4 A 5 LEU A 239 TRP A 244 -1 N VAL A 241 O GLU A 250
SHEET 5 A 5 GLY A 227 PHE A 233 -1 N GLY A 230 O ALA A 242
SHEET 1 B 4 THR A 11 GLU A 15 0
SHEET 2 B 4 ALA A 291 GLU A 296 -1 O VAL A 292 N VAL A 13
SHEET 3 B 4 THR A 281 GLU A 286 -1 N VAL A 284 O TRP A 293
SHEET 4 B 4 PRO A 270 PHE A 275 -1 N HIS A 274 O PHE A 283
SHEET 1 C 4 GLU A 21 PHE A 25 0
SHEET 2 C 4 PHE A 31 ALA A 35 -1 O TYR A 32 N VAL A 24
SHEET 3 C 4 GLU A 47 ILE A 51 -1 O GLU A 47 N ALA A 35
SHEET 4 C 4 LYS A 58 CYS A 62 -1 O THR A 59 N ARG A 50
SHEET 1 D 2 GLU A 39 VAL A 40 0
SHEET 2 D 2 LYS A 43 PRO A 44 -1 O LYS A 43 N VAL A 40
SHEET 1 E 2 GLU A 65 VAL A 66 0
SHEET 2 E 2 TYR A 69 GLY A 70 -1 O TYR A 69 N VAL A 66
SHEET 1 F 4 PRO A 73 CYS A 78 0
SHEET 2 F 4 GLN A 84 ASP A 89 -1 O ALA A 88 N ALA A 74
SHEET 3 F 4 GLY A 93 GLN A 98 -1 O VAL A 97 N LEU A 85
SHEET 4 F 4 PHE A 103 GLU A 105 -1 O GLU A 104 N VAL A 96
SHEET 1 G 4 ASP A 121 PHE A 124 0
SHEET 2 G 4 LEU A 130 ALA A 134 -1 O TRP A 131 N ALA A 123
SHEET 3 G 4 GLY A 153 PHE A 158 -1 O PHE A 158 N LEU A 130
SHEET 4 G 4 MET A 164 PHE A 171 -1 O PHE A 171 N GLY A 153
SHEET 1 H 4 PRO A 174 HIS A 181 0
SHEET 2 H 4 PRO A 187 GLU A 194 -1 O GLN A 189 N ARG A 180
SHEET 3 H 4 LYS A 199 GLY A 207 -1 O TRP A 201 N VAL A 192
SHEET 4 H 4 LYS A 210 HIS A 219 -1 O GLU A 212 N ASP A 204
SSBOND 1 CYS A 78 CYS A 306 1555 1555 2.03
LINK OE2 GLU A 21 CA CA A 500 1555 1555 2.36
LINK OD1 ASP A 120 CA CA A 500 1555 1555 2.36
LINK OD1 ASN A 175 CA CA A 500 1555 1555 2.37
LINK OD1 ASN A 229 CA CA A 500 1555 1555 2.40
LINK OD1 ASP A 232 CA CA A 501 1555 1555 3.40
LINK OD2 ASP A 232 CA CA A 501 1555 1555 2.05
LINK O LEU A 273 CA CA A 501 1555 1555 2.31
LINK ND1 HIS A 274 CA CA A 501 1555 1555 2.30
LINK CA CA A 500 O HOH A 523 1555 1555 2.50
LINK CA CA A 500 O HOH A 524 1555 1555 2.40
LINK CA CA A 500 O HOH A 578 1555 1555 2.41
LINK CA CA A 501 O HOH A 527 1555 1555 2.25
LINK CA CA A 501 O HOH A 555 1555 1555 2.32
LINK CA CA A 501 O HOH A 613 1555 1555 2.25
CISPEP 1 ALA A 140 PRO A 141 0 0.42
SITE 1 AC1 7 GLU A 21 ASP A 120 ASN A 175 ASN A 229
SITE 2 AC1 7 HOH A 523 HOH A 524 HOH A 578
SITE 1 AC2 6 ASP A 232 LEU A 273 HIS A 274 HOH A 527
SITE 2 AC2 6 HOH A 555 HOH A 613
CRYST1 43.430 82.230 87.300 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 0.023026 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012161 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011455 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
