HEADER KINASE 18-MAY-98 16PK
TITLE PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI BISUBSTRATE ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-PHOSPHOGLYCERATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PGK;
COMPND 5 EC: 2.7.2.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 VARIANT: GLYCOSOMAL VERSION;
SOURCE 5 ORGANELLE: GLYCOSOME;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS KINASE, PHOSPHOGLYCERATE, TERNARY COMPLEX, GLYCOLYSIS, TRANSFERASE,
KEYWDS 2 BISUBSTRATE, ANALOG
EXPDTA X-RAY DIFFRACTION
AUTHOR B.E.BERNSTEIN,J.BRESSI,M.BLACKBURN,M.GELB,W.G.J.HOL
REVDAT 4 02-AUG-23 16PK 1 REMARK SEQADV
REVDAT 3 24-FEB-09 16PK 1 VERSN
REVDAT 2 13-JAN-99 16PK 1 SOURCE REMARK HETNAM JRNL
REVDAT 1 25-NOV-98 16PK 0
JRNL AUTH B.E.BERNSTEIN,D.M.WILLIAMS,J.C.BRESSI,P.KUHN,M.H.GELB,
JRNL AUTH 2 G.M.BLACKBURN,W.G.HOL
JRNL TITL A BISUBSTRATE ANALOG INDUCES UNEXPECTED CONFORMATIONAL
JRNL TITL 2 CHANGES IN PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI.
JRNL REF J.MOL.BIOL. V. 279 1137 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9642090
JRNL DOI 10.1006/JMBI.1998.1835
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 65142
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4593
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 : 3127
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.50
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 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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.410
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 100 ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 2 POSITIONAL (A) : 50 ; NULL
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 16PK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170157.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60549
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 21.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: PDB ENTRY 13PK
REMARK 200
REMARK 200 REMARK: MR SOLUTION USED INDIVIDUAL DOMAINS SEPARATELY
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION BY MIXING, PH 7.7,
REMARK 280 VAPOR DIFFUSION
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 36.35500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.66000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.66000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.35500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.88000
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 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 ASN A 36 108.78 -161.68
REMARK 500 ASN A 115 59.80 -140.66
REMARK 500 ASN A 133 117.94 -38.04
REMARK 500 ASP A 165 38.73 -140.03
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 BIS A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 430
DBREF 16PK A 5 419 UNP P07378 PGKC_TRYBB 5 419
SEQADV 16PK ARG A 98 UNP P07378 ALA 98 CONFLICT
SEQADV 16PK ASP A 418 UNP P07378 GLU 418 CONFLICT
SEQRES 1 A 415 GLU LYS LYS SER ILE ASN GLU CYS ASP LEU LYS GLY LYS
SEQRES 2 A 415 LYS VAL LEU ILE ARG VAL ASP PHE ASN VAL PRO VAL LYS
SEQRES 3 A 415 ASN GLY LYS ILE THR ASN ASP TYR ARG ILE ARG SER ALA
SEQRES 4 A 415 LEU PRO THR LEU LYS LYS VAL LEU THR GLU GLY GLY SER
SEQRES 5 A 415 CYS VAL LEU MET SER HIS LEU GLY ARG PRO LYS GLY ILE
SEQRES 6 A 415 PRO MET ALA GLN ALA GLY LYS ILE ARG SER THR GLY GLY
SEQRES 7 A 415 VAL PRO GLY PHE GLN GLN LYS ALA THR LEU LYS PRO VAL
SEQRES 8 A 415 ALA LYS ARG LEU SER GLU LEU LEU LEU ARG PRO VAL THR
SEQRES 9 A 415 PHE ALA PRO ASP CYS LEU ASN ALA ALA ASP VAL VAL SER
SEQRES 10 A 415 LYS MET SER PRO GLY ASP VAL VAL LEU LEU GLU ASN VAL
SEQRES 11 A 415 ARG PHE TYR LYS GLU GLU GLY SER LYS LYS ALA LYS ASP
SEQRES 12 A 415 ARG GLU ALA MET ALA LYS ILE LEU ALA SER TYR GLY ASP
SEQRES 13 A 415 VAL TYR ILE SER ASP ALA PHE GLY THR ALA HIS ARG ASP
SEQRES 14 A 415 SER ALA THR MET THR GLY ILE PRO LYS ILE LEU GLY ASN
SEQRES 15 A 415 GLY ALA ALA GLY TYR LEU MET GLU LYS GLU ILE SER TYR
SEQRES 16 A 415 PHE ALA LYS VAL LEU GLY ASN PRO PRO ARG PRO LEU VAL
SEQRES 17 A 415 ALA ILE VAL GLY GLY ALA LYS VAL SER ASP LYS ILE GLN
SEQRES 18 A 415 LEU LEU ASP ASN MET LEU GLN ARG ILE ASP TYR LEU LEU
SEQRES 19 A 415 ILE GLY GLY ALA MET ALA TYR THR PHE LEU LYS ALA GLN
SEQRES 20 A 415 GLY TYR SER ILE GLY LYS SER LYS CYS GLU GLU SER LYS
SEQRES 21 A 415 LEU GLU PHE ALA ARG SER LEU LEU LYS LYS ALA GLU ASP
SEQRES 22 A 415 ARG LYS VAL GLN VAL ILE LEU PRO ILE ASP HIS VAL CYS
SEQRES 23 A 415 HIS THR GLU PHE LYS ALA VAL ASP SER PRO LEU ILE THR
SEQRES 24 A 415 GLU ASP GLN ASN ILE PRO GLU GLY HIS MET ALA LEU ASP
SEQRES 25 A 415 ILE GLY PRO LYS THR ILE GLU LYS TYR VAL GLN THR ILE
SEQRES 26 A 415 GLY LYS CYS LYS SER ALA ILE TRP ASN GLY PRO MET GLY
SEQRES 27 A 415 VAL PHE GLU MET VAL PRO TYR SER LYS GLY THR PHE ALA
SEQRES 28 A 415 ILE ALA LYS ALA MET GLY ARG GLY THR HIS GLU HIS GLY
SEQRES 29 A 415 LEU MET SER ILE ILE GLY GLY GLY ASP SER ALA SER ALA
SEQRES 30 A 415 ALA GLU LEU SER GLY GLU ALA LYS ARG MET SER HIS VAL
SEQRES 31 A 415 SER THR GLY GLY GLY ALA SER LEU GLU LEU LEU GLU GLY
SEQRES 32 A 415 LYS THR LEU PRO GLY VAL THR VAL LEU ASP ASP LYS
HET BIS A 499 39
HET EPE A 430 15
HETNAM BIS 1,1,5,5-TETRAFLUOROPHOSPHOPENTYLPHOSPHONIC ACID
HETNAM 2 BIS ADENYLATE ESTER
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 2 BIS C15 H22 F4 N5 O12 P3
FORMUL 3 EPE C8 H18 N2 O4 S
FORMUL 4 HOH *580(H2 O)
HELIX 1 1 ILE A 9 GLU A 11 5 3
HELIX 2 2 TYR A 38 THR A 52 1 15
HELIX 3 3 MET A 71 SER A 79 5 9
HELIX 4 4 GLN A 88 ALA A 90 5 3
HELIX 5 5 LYS A 93 LEU A 103 1 11
HELIX 6 6 ALA A 117 SER A 121 1 5
HELIX 7 7 VAL A 134 PHE A 136 5 3
HELIX 8 8 LYS A 138 GLY A 141 5 4
HELIX 9 9 ALA A 145 TYR A 158 1 14
HELIX 10 10 PHE A 167 THR A 169 5 3
HELIX 11 11 GLY A 179 LEU A 184 1 6
HELIX 12 12 TYR A 191 LEU A 204 1 14
HELIX 13 13 SER A 221 ARG A 233 5 13
HELIX 14 14 ALA A 242 GLN A 251 5 10
HELIX 15 15 GLU A 262 ASP A 277 5 16
HELIX 16 16 PRO A 319 LYS A 331 1 13
HELIX 17 17 VAL A 347 TYR A 349 5 3
HELIX 18 18 LYS A 351 HIS A 367 1 17
HELIX 19 19 GLY A 376 LEU A 384 1 9
HELIX 20 20 GLY A 398 LEU A 405 1 8
HELIX 21 21 PRO A 411 THR A 414 1 4
SHEET 1 A 5 VAL A 161 ASP A 165 0
SHEET 2 A 5 LYS A 18 VAL A 23 1 N LEU A 20 O VAL A 161
SHEET 3 A 5 SER A 56 MET A 60 1 N SER A 56 O VAL A 19
SHEET 4 A 5 VAL A 128 LEU A 131 1 N VAL A 129 O CYS A 57
SHEET 5 A 5 THR A 108 ALA A 110 1 N THR A 108 O LEU A 130
SHEET 1 B 5 GLN A 281 ILE A 283 0
SHEET 2 B 5 TYR A 236 ILE A 239 1 N LEU A 237 O GLN A 281
SHEET 3 B 5 LEU A 211 VAL A 215 1 N ALA A 213 O TYR A 236
SHEET 4 B 5 SER A 334 ASN A 338 1 N SER A 334 O VAL A 212
SHEET 5 B 5 MET A 370 ILE A 373 1 N MET A 370 O ALA A 335
SHEET 1 C 2 HIS A 288 HIS A 291 0
SHEET 2 C 2 MET A 313 ILE A 317 -1 N ASP A 316 O VAL A 289
CISPEP 1 ARG A 209 PRO A 210 0 0.07
SITE 1 AC1 34 GLY A 217 ALA A 218 LYS A 223 GLY A 241
SITE 2 AC1 34 ALA A 242 TYR A 245 ALA A 314 LEU A 315
SITE 3 AC1 34 GLY A 339 PRO A 340 GLY A 342 VAL A 343
SITE 4 AC1 34 GLU A 345 GLY A 397 GLY A 398 GLY A 399
SITE 5 AC1 34 HOH A 505 HOH A 514 HOH A 523 HOH A 571
SITE 6 AC1 34 HOH A 673 HOH A 766 HOH A 768 HOH A 779
SITE 7 AC1 34 HOH A 781 HOH A 799 HOH A 872 HOH A 874
SITE 8 AC1 34 HOH A 902 HOH A 981 HOH A1020 HOH A1032
SITE 9 AC1 34 HOH A1034 HOH A1037
SITE 1 AC2 15 LYS A 49 THR A 52 GLU A 53 GLN A 251
SITE 2 AC2 15 GLY A 252 TYR A 253 ALA A 296 GLU A 345
SITE 3 AC2 15 MET A 346 VAL A 347 PRO A 348 HOH A 567
SITE 4 AC2 15 HOH A 676 HOH A 809 HOH A 871
CRYST1 72.710 79.760 81.320 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 0.013753 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012297 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
