HEADER ISOMERASE 19-JUL-00 1E59
TITLE E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE COMPLEXED WITH
TITLE 2 VANADATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOGLYCERATE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.4.2.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: PGM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS INHIBITOR, VANDATE, GLYCOLYSIS AND GLUCONEOGENESIS, PHOSPHOGLYCERATE
KEYWDS 2 MUTASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.BOND,W.N.HUNTER
REVDAT 5 13-DEC-23 1E59 1 REMARK
REVDAT 4 22-MAY-19 1E59 1 REMARK
REVDAT 3 24-FEB-09 1E59 1 VERSN
REVDAT 2 15-MAR-02 1E59 1 JRNL
REVDAT 1 05-FEB-02 1E59 0
JRNL AUTH C.S.BOND,M.WHITE,W.N.HUNTER
JRNL TITL MECHANISTIC IMPLICATIONS FOR ESCHERICHIA COLI
JRNL TITL 2 COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE BASED ON THE
JRNL TITL 3 HIGH-RESOLUTION CRYSTAL STRUCTURE OF A VANADATE COMPLEX.
JRNL REF J.MOL.BIOL. V. 316 1071 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11884145
JRNL DOI 10.1006/JMBI.2002.5418
REMARK 2
REMARK 2 RESOLUTION. 1.30 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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
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) : 0.159
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.155
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2061
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 65738
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.145
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.141
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1578
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 48908
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1945
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 264
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2210.5
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 4
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 20185
REMARK 3 NUMBER OF RESTRAINTS : 24690
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.029
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.059
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.066
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.016
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.049
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.087
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: VO3 VALUES EXTRACTED FROM CSDS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1290005179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : 105.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.89
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68073
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40100
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: SHELX
REMARK 200 STARTING MODEL: PDB ENTRY 1E58
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL (PH 8.0), 200 MM
REMARK 280 LI2SO4, 20% PEG 4000, 100 MM NAVO3, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 30.62450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.07100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.62450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.07100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 61.24900
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 CATALYTIC ACTIVITY: 2-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE =
REMARK 400 3-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE.
REMARK 400 PATHWAY: GLYCOLYSIS.
REMARK 400 SIMILARITY: BELONGS TO THE PHOSPHOGLYCERATE MUTASE FAMILY.
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 ALA A 1
REMARK 465 ALA A 241
REMARK 465 VAL A 242
REMARK 465 ALA A 243
REMARK 465 ASN A 244
REMARK 465 GLN A 245
REMARK 465 GLY A 246
REMARK 465 LYS A 247
REMARK 465 ALA A 248
REMARK 465 LYS A 249
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 9 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 28 CB - CG - OD1 ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASP A 28 CB - CG - OD2 ANGL. DEV. = -13.6 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 4.9 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 GLU A 88 155.66 -48.77
REMARK 500 THR A 150 153.83 177.23
REMARK 500 THR A 167 -57.35 -131.01
REMARK 500 ALA A 182 -146.46 -150.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 VO3 A 1001
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO3 A1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E58 RELATED DB: PDB
REMARK 900 E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE
DBREF 1E59 A 1 249 UNP P31217 PMG1_ECOLI 1 249
SEQRES 1 A 249 ALA VAL THR LYS LEU VAL LEU VAL ARG HIS GLY GLU SER
SEQRES 2 A 249 GLN TRP ASN LYS GLU ASN ARG PHE THR GLY TRP TYR ASP
SEQRES 3 A 249 VAL ASP LEU SER GLU LYS GLY VAL SER GLU ALA LYS ALA
SEQRES 4 A 249 ALA GLY LYS LEU LEU LYS GLU GLU GLY TYR SER PHE ASP
SEQRES 5 A 249 PHE ALA TYR THR SER VAL LEU LYS ARG ALA ILE HIS THR
SEQRES 6 A 249 LEU TRP ASN VAL LEU ASP GLU LEU ASP GLN ALA TRP LEU
SEQRES 7 A 249 PRO VAL GLU LYS SER TRP LYS LEU ASN GLU ARG HIS TYR
SEQRES 8 A 249 GLY ALA LEU GLN GLY LEU ASN LYS ALA GLU THR ALA GLU
SEQRES 9 A 249 LYS TYR GLY ASP GLU GLN VAL LYS GLN TRP ARG ARG GLY
SEQRES 10 A 249 PHE ALA VAL THR PRO PRO GLU LEU THR LYS ASP ASP GLU
SEQRES 11 A 249 ARG TYR PRO GLY HIS ASP PRO ARG TYR ALA LYS LEU SER
SEQRES 12 A 249 GLU LYS GLU LEU PRO LEU THR GLU SER LEU ALA LEU THR
SEQRES 13 A 249 ILE ASP ARG VAL ILE PRO TYR TRP ASN GLU THR ILE LEU
SEQRES 14 A 249 PRO ARG MET LYS SER GLY GLU ARG VAL ILE ILE ALA ALA
SEQRES 15 A 249 HIS GLY ASN SER LEU ARG ALA LEU VAL LYS TYR LEU ASP
SEQRES 16 A 249 ASN MET SER GLU GLU GLU ILE LEU GLU LEU ASN ILE PRO
SEQRES 17 A 249 THR GLY VAL PRO LEU VAL TYR GLU PHE ASP GLU ASN PHE
SEQRES 18 A 249 LYS PRO LEU LYS ARG TYR TYR LEU GLY ASN ALA ASP GLU
SEQRES 19 A 249 ILE ALA ALA LYS ALA ALA ALA VAL ALA ASN GLN GLY LYS
SEQRES 20 A 249 ALA LYS
HET VO3 A1001 17
HET CL A3001 1
HETNAM VO3 TETRAMETAVANADATE
HETNAM CL CHLORIDE ION
FORMUL 2 VO3 O13 V4 6-
FORMUL 3 CL CL 1-
FORMUL 4 HOH *264(H2 O)
HELIX 1 1 SER A 13 GLU A 18 1 6
HELIX 2 2 SER A 30 GLU A 47 1 18
HELIX 3 3 LEU A 59 ASP A 74 1 16
HELIX 4 4 TRP A 84 ASN A 87 5 4
HELIX 5 5 TYR A 91 GLN A 95 5 5
HELIX 6 6 ASN A 98 GLY A 107 1 10
HELIX 7 7 GLY A 107 GLY A 117 1 11
HELIX 8 8 TYR A 132 ASP A 136 5 5
HELIX 9 9 ASP A 136 ALA A 140 5 5
HELIX 10 10 SER A 152 THR A 167 1 16
HELIX 11 11 THR A 167 SER A 174 1 8
HELIX 12 12 HIS A 183 ASP A 195 1 13
HELIX 13 13 SER A 198 LEU A 205 1 8
HELIX 14 14 ASN A 231 ALA A 240 1 10
SHEET 1 A 6 VAL A 80 LYS A 82 0
SHEET 2 A 6 PHE A 53 THR A 56 1 N ALA A 54 O GLU A 81
SHEET 3 A 6 VAL A 178 ALA A 182 1 N ILE A 179 O PHE A 53
SHEET 4 A 6 THR A 3 ARG A 9 1 N VAL A 6 O VAL A 178
SHEET 5 A 6 LEU A 213 PHE A 217 -1 N PHE A 217 O THR A 3
SHEET 6 A 6 PRO A 223 TYR A 228 -1 N TYR A 227 O VAL A 214
SITE 1 AC1 2 TRP A 67 LYS A 82
SITE 1 AC2 19 ARG A 9 ASN A 16 ARG A 20 PHE A 21
SITE 2 AC2 19 THR A 22 GLY A 23 GLU A 88 ARG A 89
SITE 3 AC2 19 TYR A 91 LYS A 99 ARG A 115 ARG A 116
SITE 4 AC2 19 ASN A 185 HOH A2009 HOH A2114 HOH A2115
SITE 5 AC2 19 HOH A2116 HOH A2262 HOH A2263
CRYST1 61.249 112.142 40.948 90.00 90.00 90.00 P 21 21 2 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 0.016327 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008917 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
