| content |
HEADER HYDROLASE 20-DEC-06 2OCI
TITLE CRYSTAL STRUCTURE OF VALACYCLOVIR HYDROLASE COMPLEXED WITH
TITLE 2 A PRODUCT ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VALACYCLOVIR HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VACVASE, BIPHENYL HYDROLASE-LIKE PROTEIN,
COMPND 5 BIPHENYL HYDROLASE-RELATED PROTEIN, BPH-RP, BREAST
COMPND 6 EPITHELIAL MUCIN-ASSOCIATED ANTIGEN, MCNAA;
COMPND 7 EC: 3.1.-.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: BPHL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS ALPHA BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LAI,Z.XU,G.L.AMIDON
REVDAT 1 05-FEB-08 2OCI 0
JRNL AUTH L.LAI,Z.XU,J.ZHOU,G.L.AMIDON
JRNL TITL MOLECULAR BASIS OF PRODRUG ACTIVATION BY HUMAN
JRNL TITL 2 VALACYCLOVIR HYDROLASE: A NEW DRUG DELIVERY TARGET
JRNL TITL 3 FOR IMPROVING ORAL ABSORPTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.36
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) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 30385
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2945
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 : 2032
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 268
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48700
REMARK 3 B22 (A**2) : 0.48700
REMARK 3 B33 (A**2) : -0.97400
REMARK 3 B12 (A**2) : -0.97200
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) : 1.201 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.768 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.082 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.035 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 60.75
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : YNH_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 5 : 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 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FRIEDEL PAIRS WERE USED IN REFINEMENT
REMARK 4
REMARK 4 2OCI COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB040962.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
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) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : DTREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30385
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 38.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 10.930
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.89
REMARK 200 R MERGE FOR SHELL (I) : 0.41700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2OCG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-16% PEG 4,000, 0.1 M MOPS, 0.1 M
REMARK 280 MNSO4, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,2/3+Z
REMARK 290 6555 X-Y,X,1/3+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 -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 57.80667
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 28.90333
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 0.00000
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 57.80667
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 28.90333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN. THE BIOLOGICAL UNIT OF THE
REMARK 300 PROTEIN IS NOT KNOWN
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 MG MG A 302 LIES ON A SPECIAL POSITION.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 187 CG CD NE CZ NH1 NH2
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 SER A 122 -119.03 57.78
REMARK 500 ASP A 204 12.04 59.25
REMARK 500 CYS A 208 29.66 -152.66
REMARK 500 LYS A 254 -153.14 -112.94
REMARK 500 ASN A 256 39.85 -96.27
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 301 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 57 OE1
REMARK 620 2 GLU A 57 OE2 56.0
REMARK 620 3 ASP A 78 OD2 106.4 161.9
REMARK 620 4 HOH A 506 O 85.4 83.1 91.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204 OD2
REMARK 620 2 HOH A 621 O 85.2
REMARK 620 3 HOH A 552 O 95.1 88.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE FOR RESIDUE A 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE FOR RESIDUE A 302
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: TYC BINDING SITE FOR RESIDUE A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OCG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN VALACYCLOVIR HYDROLASE
REMARK 900 RELATED ID: 2OCK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VALACYCLOVIR HYDROLASE D123N MUTANT
REMARK 900 RELATED ID: 2OCL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VALACYCLOVIR HYDROLASE S122A MUTANT
DBREF 2OCI A 21 274 UNP Q86WA6 BPHL_HUMAN 38 291
SEQRES 1 A 254 SER VAL THR SER ALA LYS VAL ALA VAL ASN GLY VAL GLN
SEQRES 2 A 254 LEU HIS TYR GLN GLN THR GLY GLU GLY ASP HIS ALA VAL
SEQRES 3 A 254 LEU LEU LEU PRO GLY MET LEU GLY SER GLY GLU THR ASP
SEQRES 4 A 254 PHE GLY PRO GLN LEU LYS ASN LEU ASN LYS LYS LEU PHE
SEQRES 5 A 254 THR VAL VAL ALA TRP ASP PRO ARG GLY TYR GLY HIS SER
SEQRES 6 A 254 ARG PRO PRO ASP ARG ASP PHE PRO ALA ASP PHE PHE GLU
SEQRES 7 A 254 ARG ASP ALA LYS ASP ALA VAL ASP LEU MET LYS ALA LEU
SEQRES 8 A 254 LYS PHE LYS LYS VAL SER LEU LEU GLY TRP SER ASP GLY
SEQRES 9 A 254 GLY ILE THR ALA LEU ILE ALA ALA ALA LYS TYR PRO SER
SEQRES 10 A 254 TYR ILE HIS LYS MET VAL ILE TRP GLY ALA ASN ALA TYR
SEQRES 11 A 254 VAL THR ASP GLU ASP SER MET ILE TYR GLU GLY ILE ARG
SEQRES 12 A 254 ASP VAL SER LYS TRP SER GLU ARG THR ARG LYS PRO LEU
SEQRES 13 A 254 GLU ALA LEU TYR GLY TYR ASP TYR PHE ALA ARG THR CYS
SEQRES 14 A 254 GLU LYS TRP VAL ASP GLY ILE ARG GLN PHE LYS HIS LEU
SEQRES 15 A 254 PRO ASP GLY ASN ILE CYS ARG HIS LEU LEU PRO ARG VAL
SEQRES 16 A 254 GLN CYS PRO ALA LEU ILE VAL HIS GLY GLU LYS ASP PRO
SEQRES 17 A 254 LEU VAL PRO ARG PHE HIS ALA ASP PHE ILE HIS LYS HIS
SEQRES 18 A 254 VAL LYS GLY SER ARG LEU HIS LEU MET PRO GLU GLY LYS
SEQRES 19 A 254 HIS ASN LEU HIS LEU ARG PHE ALA ASP GLU PHE ASN LYS
SEQRES 20 A 254 LEU ALA GLU ASP PHE LEU GLN
HET MN A 301 1
HET MG A 302 1
HET TYC A 401 13
HETNAM MN MANGANESE (II) ION
HETNAM MG MAGNESIUM ION
HETNAM TYC L-TYROSINAMIDE
FORMUL 2 MN MN 2+
FORMUL 3 MG MG 2+
FORMUL 4 TYC C9 H12 N2 O2
FORMUL 5 HOH *268(H2 O)
HELIX 1 1 SER A 55 PHE A 60 1 6
HELIX 2 2 PHE A 60 LEU A 67 1 8
HELIX 3 3 ASP A 95 LEU A 111 1 17
HELIX 4 4 SER A 122 TYR A 135 1 14
HELIX 5 5 THR A 152 GLY A 161 1 10
HELIX 6 6 SER A 169 GLY A 181 1 13
HELIX 7 7 GLY A 181 HIS A 201 1 21
HELIX 8 8 LEU A 202 ASN A 206 5 5
HELIX 9 9 LEU A 211 VAL A 215 5 5
HELIX 10 10 PRO A 231 VAL A 242 1 12
HELIX 11 11 ASN A 256 PHE A 261 1 6
HELIX 12 12 PHE A 261 GLN A 274 1 14
SHEET 1 A 8 THR A 23 VAL A 29 0
SHEET 2 A 8 VAL A 32 THR A 39 -1 O VAL A 32 N VAL A 29
SHEET 3 A 8 PHE A 72 TRP A 77 -1 O VAL A 74 N THR A 39
SHEET 4 A 8 HIS A 44 LEU A 49 1 N LEU A 48 O VAL A 75
SHEET 5 A 8 VAL A 116 TRP A 121 1 O LEU A 119 N LEU A 49
SHEET 6 A 8 ILE A 139 TRP A 145 1 O VAL A 143 N LEU A 118
SHEET 7 A 8 ALA A 219 GLY A 224 1 O VAL A 222 N ILE A 144
SHEET 8 A 8 ARG A 246 MET A 250 1 O ARG A 246 N ILE A 221
LINK OE1 GLU A 57 MN MN A 301 1555 1555 2.34
LINK OE2 GLU A 57 MN MN A 301 1555 1555 2.34
LINK OD2 ASP A 78 MN MN A 301 1555 1555 2.14
LINK OD2 ASP A 204 MG MG A 302 1555 1555 2.16
LINK MN MN A 301 O HOH A 506 1555 1555 2.30
LINK MG MG A 302 O HOH A 621 1555 1555 2.33
LINK MG MG A 302 O HOH A 552 1555 1555 1.95
CISPEP 1 ARG A 86 PRO A 87 0 -0.20
CISPEP 2 PRO A 87 PRO A 88 0 0.24
SITE 1 AC1 5 HIS A 35 GLU A 57 ASP A 78 HIS A 84
SITE 2 AC1 5 HOH A 506
SITE 1 AC2 3 ASP A 204 HOH A 552 HOH A 621
SITE 1 AC3 13 GLY A 51 MET A 52 SER A 122 ASP A 123
SITE 2 AC3 13 ASP A 155 ILE A 158 TYR A 159 ILE A 162
SITE 3 AC3 13 TRP A 192 HOH A 417 HOH A 457 HOH A 517
SITE 4 AC3 13 HOH A 519
CRYST1 88.600 88.600 86.710 90.00 90.00 120.00 P 62 6
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 0.011287 0.006516 0.000000 0.00000
SCALE2 0.000000 0.013033 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011533 0.00000
TER 2033 GLN A 274
MASTER 285 0 3 12 8 0 7 6 2315 1 22 20
END |