HEADER ISOMERASE, HYDROLASE 02-JAN-05 1YFK
TITLE CRYSTAL STRUCTURE OF HUMAN B TYPE PHOSPHOGLYCERATE MUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOGLYCERATE MUTASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOGLYCERATE MUTASE ISOZYME B, PGAM-B, BPG-DEPENDENT
COMPND 5 PGAM 1;
COMPND 6 EC: 5.4.2.1, 5.4.2.4, 3.1.3.13;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA, ISOMERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WANG,Z.WEI,L.LIU,W.GONG
REVDAT 3 25-OCT-23 1YFK 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1YFK 1 VERSN
REVDAT 1 17-MAY-05 1YFK 0
JRNL AUTH Y.WANG,Z.WEI,L.LIU,Z.CHENG,Y.LIN,F.JI,W.GONG
JRNL TITL CRYSTAL STRUCTURE OF HUMAN B-TYPE PHOSPHOGLYCERATE MUTASE
JRNL TITL 2 BOUND WITH CITRATE.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 331 1207 2005
JRNL REFN ISSN 0006-291X
JRNL PMID 15883004
JRNL DOI 10.1016/J.BBRC.2005.03.243
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 216724.150
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 17105
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) : 0.216
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.900
REMARK 3 FREE R VALUE TEST SET COUNT : 671
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2389
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 97
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3801
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 17.01000
REMARK 3 B22 (A**2) : -1.68000
REMARK 3 B33 (A**2) : -15.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 12.34000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.49
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 23.82
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 : CIT_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CIT_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : WATER.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031458.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 3W1A
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 : CCD
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 : 17981
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12900
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) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43600
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 5PGM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, ISO-PROPANOL, TRI-SODIUM
REMARK 280 CITRATE DEHYDRATE, (NH4)2SO4, PH 5.7, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 32.87250
REMARK 290 SMTRY3 2 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ALA A 2
REMARK 465 VAL A 246
REMARK 465 ALA A 247
REMARK 465 ALA A 248
REMARK 465 GLN A 249
REMARK 465 GLY A 250
REMARK 465 LYS A 251
REMARK 465 ALA A 252
REMARK 465 LYS A 253
REMARK 465 LYS A 254
REMARK 465 LEU A 255
REMARK 465 GLU A 256
REMARK 465 HIS A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 MET B 243
REMARK 465 GLU B 244
REMARK 465 ALA B 245
REMARK 465 VAL B 246
REMARK 465 ALA B 247
REMARK 465 ALA B 248
REMARK 465 GLN B 249
REMARK 465 GLY B 250
REMARK 465 LYS B 251
REMARK 465 ALA B 252
REMARK 465 LYS B 253
REMARK 465 LYS B 254
REMARK 465 LEU B 255
REMARK 465 GLU B 256
REMARK 465 HIS B 257
REMARK 465 HIS B 258
REMARK 465 HIS B 259
REMARK 465 HIS B 260
REMARK 465 HIS B 261
REMARK 465 HIS B 262
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 40 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 106 CG CD CE NZ
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 SER A 137 OG
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 GLU A 203 CG CD OE1 OE2
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 ASP A 235 CG OD1 OD2
REMARK 470 GLU A 244 CG CD OE1 OE2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 GLN B 43 CG CD OE1 NE2
REMARK 470 LYS B 113 CG CD CE NZ
REMARK 470 ARG B 117 CG CD NE CZ NH1 NH2
REMARK 470 SER B 137 OG
REMARK 470 GLU B 147 CG CD OE1 OE2
REMARK 470 GLU B 203 CG CD OE1 OE2
REMARK 470 GLU B 207 CG CD OE1 OE2
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 LYS B 228 CG CD CE NZ
REMARK 470 GLU B 236 CG CD OE1 OE2
REMARK 470 GLU B 237 CG CD OE1 OE2
REMARK 470 ARG B 240 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 58 -156.61 -86.65
REMARK 500 TYR A 92 22.34 -79.09
REMARK 500 ILE A 114 -73.18 -55.28
REMARK 500 ARG A 116 -32.41 -156.73
REMARK 500 CYS A 153 154.96 176.77
REMARK 500 ALA A 185 -147.49 -140.49
REMARK 500 SER B 58 -155.80 -88.88
REMARK 500 TYR B 92 21.73 -78.44
REMARK 500 ILE B 114 -73.68 -55.16
REMARK 500 ARG B 116 -31.59 -158.30
REMARK 500 PRO B 131 -17.24 -49.93
REMARK 500 LYS B 138 74.02 -110.86
REMARK 500 ARG B 141 -48.34 -29.28
REMARK 500 ASP B 148 -73.68 -67.63
REMARK 500 GLN B 149 -43.82 -25.30
REMARK 500 CYS B 153 157.72 179.59
REMARK 500 ALA B 185 -148.25 -141.93
REMARK 500 LYS B 222 -4.19 -53.96
REMARK 500 LYS B 241 4.95 -54.57
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 CL A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1500
DBREF 1YFK A 1 254 UNP P18669 PGAM1_HUMAN 0 253
DBREF 1YFK B 1 254 UNP P18669 PGAM1_HUMAN 0 253
SEQADV 1YFK LEU A 255 UNP P18669 EXPRESSION TAG
SEQADV 1YFK GLU A 256 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS A 257 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS A 258 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS A 259 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS A 260 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS A 261 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS A 262 UNP P18669 EXPRESSION TAG
SEQADV 1YFK LEU B 255 UNP P18669 EXPRESSION TAG
SEQADV 1YFK GLU B 256 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS B 257 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS B 258 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS B 259 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS B 260 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS B 261 UNP P18669 EXPRESSION TAG
SEQADV 1YFK HIS B 262 UNP P18669 EXPRESSION TAG
SEQRES 1 A 262 MET ALA ALA TYR LYS LEU VAL LEU ILE ARG HIS GLY GLU
SEQRES 2 A 262 SER ALA TRP ASN LEU GLU ASN ARG PHE SER GLY TRP TYR
SEQRES 3 A 262 ASP ALA ASP LEU SER PRO ALA GLY HIS GLU GLU ALA LYS
SEQRES 4 A 262 ARG GLY GLY GLN ALA LEU ARG ASP ALA GLY TYR GLU PHE
SEQRES 5 A 262 ASP ILE CYS PHE THR SER VAL GLN LYS ARG ALA ILE ARG
SEQRES 6 A 262 THR LEU TRP THR VAL LEU ASP ALA ILE ASP GLN MET TRP
SEQRES 7 A 262 LEU PRO VAL VAL ARG THR TRP ARG LEU ASN GLU ARG HIS
SEQRES 8 A 262 TYR GLY GLY LEU THR GLY LEU ASN LYS ALA GLU THR ALA
SEQRES 9 A 262 ALA LYS HIS GLY GLU ALA GLN VAL LYS ILE TRP ARG ARG
SEQRES 10 A 262 SER TYR ASP VAL PRO PRO PRO PRO MET GLU PRO ASP HIS
SEQRES 11 A 262 PRO PHE TYR SER ASN ILE SER LYS ASP ARG ARG TYR ALA
SEQRES 12 A 262 ASP LEU THR GLU ASP GLN LEU PRO SER CYS GLU SER LEU
SEQRES 13 A 262 LYS ASP THR ILE ALA ARG ALA LEU PRO PHE TRP ASN GLU
SEQRES 14 A 262 GLU ILE VAL PRO GLN ILE LYS GLU GLY LYS ARG VAL LEU
SEQRES 15 A 262 ILE ALA ALA HIS GLY ASN SER LEU ARG GLY ILE VAL LYS
SEQRES 16 A 262 HIS LEU GLU GLY LEU SER GLU GLU ALA ILE MET GLU LEU
SEQRES 17 A 262 ASN LEU PRO THR GLY ILE PRO ILE VAL TYR GLU LEU ASP
SEQRES 18 A 262 LYS ASN LEU LYS PRO ILE LYS PRO MET GLN PHE LEU GLY
SEQRES 19 A 262 ASP GLU GLU THR VAL ARG LYS ALA MET GLU ALA VAL ALA
SEQRES 20 A 262 ALA GLN GLY LYS ALA LYS LYS LEU GLU HIS HIS HIS HIS
SEQRES 21 A 262 HIS HIS
SEQRES 1 B 262 MET ALA ALA TYR LYS LEU VAL LEU ILE ARG HIS GLY GLU
SEQRES 2 B 262 SER ALA TRP ASN LEU GLU ASN ARG PHE SER GLY TRP TYR
SEQRES 3 B 262 ASP ALA ASP LEU SER PRO ALA GLY HIS GLU GLU ALA LYS
SEQRES 4 B 262 ARG GLY GLY GLN ALA LEU ARG ASP ALA GLY TYR GLU PHE
SEQRES 5 B 262 ASP ILE CYS PHE THR SER VAL GLN LYS ARG ALA ILE ARG
SEQRES 6 B 262 THR LEU TRP THR VAL LEU ASP ALA ILE ASP GLN MET TRP
SEQRES 7 B 262 LEU PRO VAL VAL ARG THR TRP ARG LEU ASN GLU ARG HIS
SEQRES 8 B 262 TYR GLY GLY LEU THR GLY LEU ASN LYS ALA GLU THR ALA
SEQRES 9 B 262 ALA LYS HIS GLY GLU ALA GLN VAL LYS ILE TRP ARG ARG
SEQRES 10 B 262 SER TYR ASP VAL PRO PRO PRO PRO MET GLU PRO ASP HIS
SEQRES 11 B 262 PRO PHE TYR SER ASN ILE SER LYS ASP ARG ARG TYR ALA
SEQRES 12 B 262 ASP LEU THR GLU ASP GLN LEU PRO SER CYS GLU SER LEU
SEQRES 13 B 262 LYS ASP THR ILE ALA ARG ALA LEU PRO PHE TRP ASN GLU
SEQRES 14 B 262 GLU ILE VAL PRO GLN ILE LYS GLU GLY LYS ARG VAL LEU
SEQRES 15 B 262 ILE ALA ALA HIS GLY ASN SER LEU ARG GLY ILE VAL LYS
SEQRES 16 B 262 HIS LEU GLU GLY LEU SER GLU GLU ALA ILE MET GLU LEU
SEQRES 17 B 262 ASN LEU PRO THR GLY ILE PRO ILE VAL TYR GLU LEU ASP
SEQRES 18 B 262 LYS ASN LEU LYS PRO ILE LYS PRO MET GLN PHE LEU GLY
SEQRES 19 B 262 ASP GLU GLU THR VAL ARG LYS ALA MET GLU ALA VAL ALA
SEQRES 20 B 262 ALA GLN GLY LYS ALA LYS LYS LEU GLU HIS HIS HIS HIS
SEQRES 21 B 262 HIS HIS
HET CL A 263 1
HET CIT A 500 13
HET CIT B1500 13
HETNAM CL CHLORIDE ION
HETNAM CIT CITRIC ACID
FORMUL 3 CL CL 1-
FORMUL 4 CIT 2(C6 H8 O7)
FORMUL 6 HOH *121(H2 O)
HELIX 1 1 SER A 31 GLY A 49 1 19
HELIX 2 2 GLN A 60 ILE A 74 1 15
HELIX 3 3 TRP A 85 ASN A 88 5 4
HELIX 4 4 TYR A 92 THR A 96 5 5
HELIX 5 5 ASN A 99 GLY A 108 1 10
HELIX 6 6 GLY A 108 SER A 118 1 11
HELIX 7 7 PHE A 132 LYS A 138 1 7
HELIX 8 8 ASP A 139 ALA A 143 5 5
HELIX 9 9 SER A 155 GLU A 177 1 23
HELIX 10 10 HIS A 186 GLY A 199 1 14
HELIX 11 11 SER A 201 GLU A 207 1 7
HELIX 12 12 ASP A 235 GLU A 244 1 10
HELIX 13 13 SER B 31 GLY B 49 1 19
HELIX 14 14 GLN B 60 ILE B 74 1 15
HELIX 15 15 TRP B 85 ASN B 88 5 4
HELIX 16 16 TYR B 92 THR B 96 5 5
HELIX 17 17 ASN B 99 GLY B 108 1 10
HELIX 18 18 GLY B 108 SER B 118 1 11
HELIX 19 19 PHE B 132 LYS B 138 1 7
HELIX 20 20 ASP B 139 ALA B 143 5 5
HELIX 21 21 SER B 155 GLU B 177 1 23
HELIX 22 22 HIS B 186 GLY B 199 1 14
HELIX 23 23 SER B 201 GLU B 207 1 7
HELIX 24 24 ASP B 235 ARG B 240 1 6
SHEET 1 A 6 VAL A 81 ARG A 83 0
SHEET 2 A 6 ILE A 54 THR A 57 1 N CYS A 55 O VAL A 82
SHEET 3 A 6 VAL A 181 ALA A 185 1 O LEU A 182 N PHE A 56
SHEET 4 A 6 TYR A 4 ARG A 10 1 N VAL A 7 O ILE A 183
SHEET 5 A 6 ILE A 216 LEU A 220 -1 O ILE A 216 N LEU A 8
SHEET 6 A 6 GLN A 231 PHE A 232 -1 O GLN A 231 N VAL A 217
SHEET 1 B 6 VAL B 81 ARG B 83 0
SHEET 2 B 6 ILE B 54 THR B 57 1 N CYS B 55 O VAL B 82
SHEET 3 B 6 VAL B 181 ALA B 185 1 O LEU B 182 N PHE B 56
SHEET 4 B 6 TYR B 4 ARG B 10 1 N VAL B 7 O ILE B 183
SHEET 5 B 6 ILE B 216 LEU B 220 -1 O ILE B 216 N LEU B 8
SHEET 6 B 6 GLN B 231 PHE B 232 -1 O GLN B 231 N VAL B 217
SITE 1 AC1 4 TRP A 68 ARG A 83 TRP B 68 ARG B 83
SITE 1 AC2 8 ASN A 17 PHE A 22 SER A 23 GLY A 24
SITE 2 AC2 8 GLU A 89 TYR A 92 LYS A 100 ARG A 116
SITE 1 AC3 9 ASN B 17 ARG B 21 SER B 23 GLY B 24
SITE 2 AC3 9 ARG B 62 GLU B 89 TYR B 92 LYS B 100
SITE 3 AC3 9 ARG B 116
CRYST1 42.861 65.745 124.812 90.00 94.36 90.00 P 1 21 1 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 0.023331 0.000000 0.001779 0.00000
SCALE2 0.000000 0.015210 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008035 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
