HEADER MOTOR PROTEIN 08-JUN-08 2VVG
TITLE CRYSTAL STRUCTURE OF THE G.INTESTINALIS KINESIN 2 GIKIN2A
TITLE 2 MOTOR DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINESIN-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: MOTOR DOMAIN, RESIDUES 1-350;
COMPND 5 SYNONYM: KINESIN 2 GIKIN2A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GIARDIA INTESTINALIS;
SOURCE 3 ORGANISM_TAXID: 5741
KEYWDS MOTOR PROTEIN, NUCLEOTIDE-BINDING, KINESIN MOTOR DOMAIN,
KEYWDS 2 MICROTUBULE, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.HOENG,J.LOEWE,S.C.DAWSON,W.Z.CANDE,M.S.SAGOLLA,
AUTHOR 2 J.J.MANCUSO
REVDAT 3 29-SEP-09 2VVG 1 REMARK
REVDAT 2 24-FEB-09 2VVG 1 VERSN
REVDAT 1 08-JUL-08 2VVG 0
JRNL AUTH J.C.HOENG,S.C.DAWSON,S.A.HOUSE,M.S.SAGOLLA,
JRNL AUTH 2 J.K.PHAM,J.J.MANCUSO,J.LOEWE,W.Z.CANDE
JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURE AND IN VIVO
JRNL TITL 2 FUNCTION OF A KINESIN-2 HOMOLOGUE IN GIARDIA
JRNL TITL 3 INTESTINALIS.
JRNL REF MOL.BIOL.CELL V. 19 3124 2008
JRNL REFN ISSN 1059-1524
JRNL PMID 18463165
JRNL DOI 10.1091/MBC.E07-11-1156
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 75883
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) : 0.2029
REMARK 3 FREE R VALUE : 0.2239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8
REMARK 3 FREE R VALUE TEST SET COUNT : 3804
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 : 4782
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 582
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.701
REMARK 3 B22 (A**2) : 0.464
REMARK 3 B33 (A**2) : 1.237
REMARK 3 B12 (A**2) : 0.307
REMARK 3 B13 (A**2) : 2.179
REMARK 3 B23 (A**2) : -1.668
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.215
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) : 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 : NULL
REMARK 3 KSOL : 0.373206
REMARK 3 BSOL : 54.8685
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 : ADP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
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: NULL
REMARK 4
REMARK 4 2VVG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-08.
REMARK 100 THE PDBE ID CODE IS EBI-36476.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75883
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.2
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 2.0
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.80
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 2
REMARK 465 SER A 3
REMARK 465 PRO A 42
REMARK 465 GLU A 43
REMARK 465 GLN A 44
REMARK 465 GLU A 45
REMARK 465 LYS A 46
REMARK 465 SER A 47
REMARK 465 ALA A 48
REMARK 465 THR A 49
REMARK 465 GLN A 50
REMARK 465 ALA A 51
REMARK 465 LYS A 52
REMARK 465 LYS A 53
REMARK 465 VAL A 54
REMARK 465 VAL A 200
REMARK 465 ALA A 201
REMARK 465 ALA A 202
REMARK 465 THR A 203
REMARK 465 GLN A 204
REMARK 465 MET A 205
REMARK 465 ASN A 206
REMARK 465 ASP A 207
REMARK 465 THR A 208
REMARK 465 GLU A 227
REMARK 465 ASN A 228
REMARK 465 LYS A 229
REMARK 465 SER A 249
REMARK 465 LYS A 250
REMARK 465 THR A 251
REMARK 465 GLY A 252
REMARK 465 ALA A 253
REMARK 465 THR A 254
REMARK 465 GLY A 255
REMARK 465 GLU A 256
REMARK 465 THR A 257
REMARK 465 LEU A 258
REMARK 465 VAL A 259
REMARK 465 GLU A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 GLN B 44
REMARK 465 GLU B 45
REMARK 465 LYS B 46
REMARK 465 SER B 47
REMARK 465 ALA B 48
REMARK 465 THR B 49
REMARK 465 GLN B 50
REMARK 465 ALA B 51
REMARK 465 LYS B 52
REMARK 465 LYS B 53
REMARK 465 VAL B 54
REMARK 465 VAL B 200
REMARK 465 ALA B 201
REMARK 465 ALA B 202
REMARK 465 THR B 203
REMARK 465 GLN B 204
REMARK 465 MET B 205
REMARK 465 ASN B 206
REMARK 465 ASP B 207
REMARK 465 THR B 208
REMARK 465 SER B 249
REMARK 465 LYS B 250
REMARK 465 THR B 251
REMARK 465 GLY B 252
REMARK 465 ALA B 253
REMARK 465 THR B 254
REMARK 465 GLY B 255
REMARK 465 GLU B 256
REMARK 465 THR B 257
REMARK 465 LEU B 258
REMARK 465 VAL B 259
REMARK 465 GLU B 260
REMARK 465 GLY B 261
REMARK 465 ALA 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 PRO A 41 CA C O CB CG CD
REMARK 470 HIS A 199 CA C O CB CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 226 CA C O CB CG1 CG2 CD1
REMARK 470 GLN A 248 CA C O CB CG CD OE1 NE2
REMARK 470 LYS A 277 CG CD CE NZ
REMARK 470 GLU B 43 CA C O CB CG CD OE1 OE2
REMARK 470 HIS B 199 CA C O CB CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 228 CA C O CB CG OD1 ND2
REMARK 470 GLN B 248 CA C O CB CG CD OE1 NE2
REMARK 470 LYS B 277 CG CD CE NZ
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 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 PHE A 60 -168.51 -127.33
REMARK 500 THR A 168 43.77 -100.63
REMARK 500 PRO A 286 49.93 -69.44
REMARK 500 LYS A 346 7.25 -68.06
REMARK 500 PHE B 60 -167.79 -127.21
REMARK 500 SER B 133 3.63 -69.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
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 MG A1352 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2083 O
REMARK 620 2 HOH A2293 O 91.1
REMARK 620 3 HOH A2290 O 85.6 91.1
REMARK 620 4 ADP A1351 O1B 170.9 95.3 87.8
REMARK 620 5 THR A 104 OG1 87.2 178.0 89.9 86.5
REMARK 620 6 HOH A2200 O 95.2 91.3 177.4 91.1 87.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1352 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2282 O
REMARK 620 2 HOH B2285 O 92.0
REMARK 620 3 THR B 104 OG1 177.6 85.9
REMARK 620 4 HOH B2085 O 96.2 84.9 84.8
REMARK 620 5 ADP B1351 O1B 96.0 85.7 82.6 164.8
REMARK 620 6 HOH B2197 O 96.5 170.3 85.5 98.7 88.8
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1352
DBREF 2VVG A 1 350 UNP A8BKD1 A8BKD1_GIALA 1 350
DBREF 2VVG B 1 350 UNP A8BKD1 A8BKD1_GIALA 1 350
SEQRES 1 A 350 MET SER SER ASP ASN ILE LYS VAL ILE VAL ARG CYS ARG
SEQRES 2 A 350 PRO LEU ASN ALA ARG GLU THR ARG GLU ASN ALA LEU ASN
SEQRES 3 A 350 ILE ILE ARG MET ASP GLU ALA SER ALA GLN VAL ILE VAL
SEQRES 4 A 350 ASP PRO PRO GLU GLN GLU LYS SER ALA THR GLN ALA LYS
SEQRES 5 A 350 LYS VAL PRO ARG THR PHE THR PHE ASP ALA VAL TYR ASP
SEQRES 6 A 350 GLN THR SER CYS ASN TYR GLY ILE PHE GLN ALA SER PHE
SEQRES 7 A 350 LYS PRO LEU ILE ASP ALA VAL LEU GLU GLY PHE ASN SER
SEQRES 8 A 350 THR ILE PHE ALA TYR GLY GLN THR GLY ALA GLY LYS THR
SEQRES 9 A 350 TRP THR MET GLY GLY ASN LYS GLU GLU PRO GLY ALA ILE
SEQRES 10 A 350 PRO ASN SER PHE LYS HIS LEU PHE ASP ALA ILE ASN SER
SEQRES 11 A 350 SER SER SER ASN GLN ASN PHE LEU VAL ILE GLY SER TYR
SEQRES 12 A 350 LEU GLU LEU TYR ASN GLU GLU ILE ARG ASP LEU ILE LYS
SEQRES 13 A 350 ASN ASN THR LYS LEU PRO LEU LYS GLU ASP LYS THR ARG
SEQRES 14 A 350 GLY ILE TYR VAL ASP GLY LEU SER MET HIS ARG VAL THR
SEQRES 15 A 350 THR ALA ALA GLU LEU SER ALA LEU MET ASP LYS GLY PHE
SEQRES 16 A 350 ALA ASN ARG HIS VAL ALA ALA THR GLN MET ASN ASP THR
SEQRES 17 A 350 SER SER ARG SER HIS SER ILE PHE MET VAL ARG ILE GLU
SEQRES 18 A 350 CYS SER GLU VAL ILE GLU ASN LYS GLU VAL ILE ARG VAL
SEQRES 19 A 350 GLY LYS LEU ASN LEU VAL ASP LEU ALA GLY SER GLU ARG
SEQRES 20 A 350 GLN SER LYS THR GLY ALA THR GLY GLU THR LEU VAL GLU
SEQRES 21 A 350 GLY ALA LYS ILE ASN LEU SER LEU SER ALA LEU GLY LEU
SEQRES 22 A 350 VAL ILE SER LYS LEU VAL GLU GLY ALA THR HIS ILE PRO
SEQRES 23 A 350 TYR ARG ASP SER LYS LEU THR ARG LEU LEU GLN ASP SER
SEQRES 24 A 350 LEU GLY GLY ASN SER LYS THR LEU MET CYS ALA ASN ILE
SEQRES 25 A 350 SER PRO ALA SER THR ASN TYR ASP GLU THR MET SER THR
SEQRES 26 A 350 LEU ARG TYR ALA ASP ARG ALA LYS GLN ILE LYS ASN LYS
SEQRES 27 A 350 PRO ARG ILE ASN GLU ASP PRO LYS ASP ALA GLN ILE
SEQRES 1 B 350 MET SER SER ASP ASN ILE LYS VAL ILE VAL ARG CYS ARG
SEQRES 2 B 350 PRO LEU ASN ALA ARG GLU THR ARG GLU ASN ALA LEU ASN
SEQRES 3 B 350 ILE ILE ARG MET ASP GLU ALA SER ALA GLN VAL ILE VAL
SEQRES 4 B 350 ASP PRO PRO GLU GLN GLU LYS SER ALA THR GLN ALA LYS
SEQRES 5 B 350 LYS VAL PRO ARG THR PHE THR PHE ASP ALA VAL TYR ASP
SEQRES 6 B 350 GLN THR SER CYS ASN TYR GLY ILE PHE GLN ALA SER PHE
SEQRES 7 B 350 LYS PRO LEU ILE ASP ALA VAL LEU GLU GLY PHE ASN SER
SEQRES 8 B 350 THR ILE PHE ALA TYR GLY GLN THR GLY ALA GLY LYS THR
SEQRES 9 B 350 TRP THR MET GLY GLY ASN LYS GLU GLU PRO GLY ALA ILE
SEQRES 10 B 350 PRO ASN SER PHE LYS HIS LEU PHE ASP ALA ILE ASN SER
SEQRES 11 B 350 SER SER SER ASN GLN ASN PHE LEU VAL ILE GLY SER TYR
SEQRES 12 B 350 LEU GLU LEU TYR ASN GLU GLU ILE ARG ASP LEU ILE LYS
SEQRES 13 B 350 ASN ASN THR LYS LEU PRO LEU LYS GLU ASP LYS THR ARG
SEQRES 14 B 350 GLY ILE TYR VAL ASP GLY LEU SER MET HIS ARG VAL THR
SEQRES 15 B 350 THR ALA ALA GLU LEU SER ALA LEU MET ASP LYS GLY PHE
SEQRES 16 B 350 ALA ASN ARG HIS VAL ALA ALA THR GLN MET ASN ASP THR
SEQRES 17 B 350 SER SER ARG SER HIS SER ILE PHE MET VAL ARG ILE GLU
SEQRES 18 B 350 CYS SER GLU VAL ILE GLU ASN LYS GLU VAL ILE ARG VAL
SEQRES 19 B 350 GLY LYS LEU ASN LEU VAL ASP LEU ALA GLY SER GLU ARG
SEQRES 20 B 350 GLN SER LYS THR GLY ALA THR GLY GLU THR LEU VAL GLU
SEQRES 21 B 350 GLY ALA LYS ILE ASN LEU SER LEU SER ALA LEU GLY LEU
SEQRES 22 B 350 VAL ILE SER LYS LEU VAL GLU GLY ALA THR HIS ILE PRO
SEQRES 23 B 350 TYR ARG ASP SER LYS LEU THR ARG LEU LEU GLN ASP SER
SEQRES 24 B 350 LEU GLY GLY ASN SER LYS THR LEU MET CYS ALA ASN ILE
SEQRES 25 B 350 SER PRO ALA SER THR ASN TYR ASP GLU THR MET SER THR
SEQRES 26 B 350 LEU ARG TYR ALA ASP ARG ALA LYS GLN ILE LYS ASN LYS
SEQRES 27 B 350 PRO ARG ILE ASN GLU ASP PRO LYS ASP ALA GLN ILE
HET ADP B1351 27
HET ADP A1351 27
HET MG A1352 1
HET MG B1352 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 HOH *582(H2 O1)
HELIX 1 1 ASN A 16 GLU A 22 1 7
HELIX 2 2 GLU A 32 SER A 34 5 3
HELIX 3 3 CYS A 69 SER A 77 1 9
HELIX 4 4 PHE A 78 GLU A 87 1 10
HELIX 5 5 GLY A 102 GLY A 108 1 7
HELIX 6 6 GLY A 115 SER A 130 1 16
HELIX 7 7 THR A 183 ARG A 198 1 16
HELIX 8 8 ASN A 265 GLY A 281 1 17
HELIX 9 9 PRO A 286 ASP A 289 5 4
HELIX 10 10 SER A 290 LEU A 296 1 7
HELIX 11 11 ASN A 318 LYS A 333 1 16
HELIX 12 12 ASN B 16 GLU B 22 1 7
HELIX 13 13 GLU B 32 SER B 34 5 3
HELIX 14 14 CYS B 69 SER B 77 1 9
HELIX 15 15 PHE B 78 GLY B 88 1 11
HELIX 16 16 GLY B 102 GLY B 108 1 7
HELIX 17 17 GLY B 115 SER B 130 1 16
HELIX 18 18 THR B 183 ARG B 198 1 16
HELIX 19 19 ASN B 265 GLU B 280 1 16
HELIX 20 20 PRO B 286 ASP B 289 5 4
HELIX 21 21 SER B 290 LEU B 296 1 7
HELIX 22 22 ASN B 318 LYS B 333 1 16
SHEET 1 AA 8 ALA A 62 TYR A 64 0
SHEET 2 AA 8 LYS A 7 CYS A 12 1 O VAL A 10 N TYR A 64
SHEET 3 AA 8 LYS A 305 ILE A 312 1 O THR A 306 N LYS A 7
SHEET 4 AA 8 SER A 91 TYR A 96 1 O THR A 92 N LEU A 307
SHEET 5 AA 8 VAL A 231 ASP A 241 1 O LYS A 236 N SER A 91
SHEET 6 AA 8 HIS A 213 GLU A 224 -1 O SER A 214 N ASP A 241
SHEET 7 AA 8 GLN A 135 TYR A 147 -1 O ASN A 136 N SER A 223
SHEET 8 AA 8 HIS A 179 VAL A 181 -1 O HIS A 179 N GLY A 141
SHEET 1 AB 9 ALA A 62 TYR A 64 0
SHEET 2 AB 9 LYS A 7 CYS A 12 1 O VAL A 10 N TYR A 64
SHEET 3 AB 9 LYS A 305 ILE A 312 1 O THR A 306 N LYS A 7
SHEET 4 AB 9 SER A 91 TYR A 96 1 O THR A 92 N LEU A 307
SHEET 5 AB 9 VAL A 231 ASP A 241 1 O LYS A 236 N SER A 91
SHEET 6 AB 9 HIS A 213 GLU A 224 -1 O SER A 214 N ASP A 241
SHEET 7 AB 9 GLN A 135 TYR A 147 -1 O ASN A 136 N SER A 223
SHEET 8 AB 9 GLU A 150 ASP A 153 -1 O GLU A 150 N TYR A 147
SHEET 9 AB 9 ASN A 158 LEU A 161 -1 O ASN A 158 N ASP A 153
SHEET 1 AC 3 ILE A 28 ASP A 31 0
SHEET 2 AC 3 GLN A 36 VAL A 39 -1 O GLN A 36 N ASP A 31
SHEET 3 AC 3 ARG A 56 THR A 59 -1 O ARG A 56 N VAL A 39
SHEET 1 AD 2 LEU A 163 ASP A 166 0
SHEET 2 AD 2 GLY A 170 VAL A 173 -1 O GLY A 170 N ASP A 166
SHEET 1 BA 8 ALA B 62 TYR B 64 0
SHEET 2 BA 8 LYS B 7 CYS B 12 1 O VAL B 10 N TYR B 64
SHEET 3 BA 8 LYS B 305 ILE B 312 1 O THR B 306 N LYS B 7
SHEET 4 BA 8 SER B 91 TYR B 96 1 O THR B 92 N LEU B 307
SHEET 5 BA 8 GLU B 230 ASP B 241 1 O LYS B 236 N SER B 91
SHEET 6 BA 8 HIS B 213 VAL B 225 -1 O SER B 214 N ASP B 241
SHEET 7 BA 8 ASN B 136 TYR B 147 -1 O ASN B 136 N SER B 223
SHEET 8 BA 8 HIS B 179 VAL B 181 -1 O HIS B 179 N GLY B 141
SHEET 1 BB 8 ALA B 62 TYR B 64 0
SHEET 2 BB 8 LYS B 7 CYS B 12 1 O VAL B 10 N TYR B 64
SHEET 3 BB 8 LYS B 305 ILE B 312 1 O THR B 306 N LYS B 7
SHEET 4 BB 8 SER B 91 TYR B 96 1 O THR B 92 N LEU B 307
SHEET 5 BB 8 GLU B 230 ASP B 241 1 O LYS B 236 N SER B 91
SHEET 6 BB 8 HIS B 213 VAL B 225 -1 O SER B 214 N ASP B 241
SHEET 7 BB 8 ASN B 136 TYR B 147 -1 O ASN B 136 N SER B 223
SHEET 8 BB 8 GLU B 150 ASP B 153 -1 O GLU B 150 N TYR B 147
SHEET 1 BC 3 ILE B 28 ASP B 31 0
SHEET 2 BC 3 GLN B 36 VAL B 39 -1 O GLN B 36 N ASP B 31
SHEET 3 BC 3 ARG B 56 THR B 59 -1 O ARG B 56 N VAL B 39
SHEET 1 BD 2 LEU B 163 ASP B 166 0
SHEET 2 BD 2 GLY B 170 VAL B 173 -1 O GLY B 170 N ASP B 166
LINK MG MG A1352 O HOH A2083 1555 1555 2.21
LINK MG MG A1352 O HOH A2293 1555 1555 2.30
LINK MG MG A1352 O HOH A2290 1555 1555 2.26
LINK MG MG A1352 O1B ADP A1351 1555 1555 2.17
LINK MG MG A1352 OG1 THR A 104 1555 1555 2.13
LINK MG MG A1352 O HOH A2200 1555 1555 2.22
LINK MG MG B1352 O HOH B2285 1555 1555 2.43
LINK MG MG B1352 OG1 THR B 104 1555 1555 2.25
LINK MG MG B1352 O HOH B2085 1555 1555 2.41
LINK MG MG B1352 O1B ADP B1351 1555 1555 2.29
LINK MG MG B1352 O HOH B2197 1555 1555 2.24
LINK MG MG B1352 O HOH B2282 1555 1555 2.33
SITE 1 AC1 21 ARG B 11 ARG B 13 PRO B 14 GLN B 98
SITE 2 AC1 21 THR B 99 GLY B 100 ALA B 101 GLY B 102
SITE 3 AC1 21 LYS B 103 THR B 104 TRP B 105 MG B1352
SITE 4 AC1 21 HOH B2081 HOH B2278 HOH B2280 HOH B2281
SITE 5 AC1 21 HOH B2282 HOH B2283 HOH B2284 HOH B2285
SITE 6 AC1 21 HOH B2286
SITE 1 AC2 19 ARG A 11 ARG A 13 PRO A 14 GLN A 98
SITE 2 AC2 19 THR A 99 GLY A 100 ALA A 101 GLY A 102
SITE 3 AC2 19 LYS A 103 THR A 104 TRP A 105 MG A1352
SITE 4 AC2 19 HOH A2290 HOH A2291 HOH A2292 HOH A2293
SITE 5 AC2 19 HOH A2294 HOH A2295 HOH A2296
SITE 1 AC3 6 THR A 104 ADP A1351 HOH A2083 HOH A2200
SITE 2 AC3 6 HOH A2290 HOH A2293
SITE 1 AC4 6 THR B 104 ADP B1351 HOH B2085 HOH B2197
SITE 2 AC4 6 HOH B2282 HOH B2285
CRYST1 44.875 48.223 72.021 89.30 87.52 84.29 P 1 2
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 0.022284 -0.002228 -0.000947 0.00000
SCALE2 0.000000 0.020840 -0.000166 0.00000
SCALE3 0.000000 0.000000 0.013898 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
