HEADER CHAPERONE 12-OCT-11 3U67
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF HSP90 FROM LEISHMANIA
TITLE 2 MAJOR(LMJF33.0312)IN COMPLEX WITH ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN 83-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-213;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;
SOURCE 3 ORGANISM_TAXID: 347515;
SOURCE 4 STRAIN: FRIEDLIN;
SOURCE 5 GENE: HSP83, HSP83-10, HSP83-11, HSP83-12, HSP83-13, HSP83-14,
SOURCE 6 HSP83-15, HSP83-16, HSP83-17, HSP83-2, HSP83-3, HSP83-5, HSP83-6,
SOURCE 7 HSP83-7, HSP83-9, LMJF_33_0312, LMJF_33_0314, LMJF_33_0316,
SOURCE 8 LMJF_33_0320, LMJF_33_0323, LMJF_33_0326, LMJF_33_0333,
SOURCE 9 LMJF_33_0336, LMJF_33_0340, LMJF_33_0343, LMJF_33_0346,
SOURCE 10 LMJF_33_0350, LMJF_33_0355, LMJF_33_0360, LMJF_33_0365;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PET15
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, ATPASE,
KEYWDS 2 CHAPERONE, ATP BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.PIZARRO,A.K.WERNIMONT,A.HUTCHINSON,F.MACKENZIE,A.FAIRLAMB,
AUTHOR 2 C.H.ARROWSMITH,C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,M.A.J.FERGUSON,R.HUI,
AUTHOR 3 T.HILLS,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 13-SEP-23 3U67 1 REMARK SEQADV LINK
REVDAT 2 29-NOV-17 3U67 1 JRNL
REVDAT 1 30-MAY-12 3U67 0
JRNL AUTH J.C.PIZARRO,T.HILLS,G.SENISTERRA,A.K.WERNIMONT,C.MACKENZIE,
JRNL AUTH 2 N.R.NORCROSS,M.A.FERGUSON,P.G.WYATT,I.H.GILBERT,R.HUI
JRNL TITL EXPLORING THE TRYPANOSOMA BRUCEI HSP83 POTENTIAL AS A TARGET
JRNL TITL 2 FOR STRUCTURE GUIDED DRUG DESIGN.
JRNL REF PLOS NEGL TROP DIS V. 7 E2492 2013
JRNL REFN ESSN 1935-2735
JRNL PMID 24147171
JRNL DOI 10.1371/JOURNAL.PNTD.0002492
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26855
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 + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1349
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 : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.84
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2792
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2263
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2656
REMARK 3 BIN R VALUE (WORKING SET) : 0.2252
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.87
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
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 : 1664
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 187
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.28690
REMARK 3 B22 (A**2) : 7.31680
REMARK 3 B33 (A**2) : -14.60370
REMARK 3 B12 (A**2) : 0.00000
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) : 0.217
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1800 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2446 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 661 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 49 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 272 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1800 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : 4 ; 0.000 ; HARMONIC
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 248 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2268 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.14
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.67
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3U67 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068356.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 158
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26898
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49200
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3H80
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M NH4SO4, 0.1M BIS
REMARK 280 -TRIS, 4.15MM ADP, 5MM MGCL2 , PH 5.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291K
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 60.93250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.49550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.93250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.49550
REMARK 290 SMTRY3 4 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 42.99100
REMARK 350 BIOMT3 2 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 -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 ASP A 164
REMARK 465 THR A 210
REMARK 465 THR A 211
REMARK 465 GLU A 212
REMARK 465 LYS A 213
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 -7 CG CD NE CZ NH1 NH2
REMARK 470 GLU A -6 CG CD OE1 OE2
REMARK 470 GLU A 70 CG CD OE1 OE2
REMARK 470 LYS A 101 CG CD CE NZ
REMARK 470 GLU A 108 CG CD OE1 OE2
REMARK 470 GLU A 162 CG CD OE1 OE2
REMARK 470 LYS A 166 CG CD CE NZ
REMARK 470 LYS A 189 CG CD CE NZ
REMARK 470 SER A 196 OG
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 PHE A 198 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 209 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
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 196 11.66 -148.74
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 MG A 215 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 36 OD1
REMARK 620 2 ADP A 214 O1A 90.6
REMARK 620 3 ADP A 214 O1B 94.6 88.9
REMARK 620 4 HOH A 356 O 168.9 93.0 95.9
REMARK 620 5 HOH A 357 O 87.4 89.7 177.6 82.1
REMARK 620 6 HOH A 358 O 88.0 177.4 88.9 88.8 92.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 218
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3H80 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH AMPPNP
DBREF 3U67 A 1 213 UNP Q4Q4I6 Q4Q4I6_LEIMA 1 213
SEQADV 3U67 MET A -17 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 HIS A -16 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 HIS A -15 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 HIS A -14 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 HIS A -13 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 HIS A -12 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 HIS A -11 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 SER A -10 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 SER A -9 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 GLY A -8 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 ARG A -7 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 GLU A -6 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 ASN A -5 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 LEU A -4 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 TYR A -3 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 PHE A -2 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 GLN A -1 UNP Q4Q4I6 EXPRESSION TAG
SEQADV 3U67 GLY A 0 UNP Q4Q4I6 EXPRESSION TAG
SEQRES 1 A 231 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 231 LEU TYR PHE GLN GLY MET THR GLU THR PHE ALA PHE GLN
SEQRES 3 A 231 ALA GLU ILE ASN GLN LEU MET SER LEU ILE ILE ASN THR
SEQRES 4 A 231 PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE
SEQRES 5 A 231 SER ASN ALA SER ASP ALA CYS ASP LYS ILE ARG TYR GLN
SEQRES 6 A 231 SER LEU THR ASP PRO SER VAL LEU GLY GLU SER PRO ARG
SEQRES 7 A 231 LEU CYS ILE ARG VAL VAL PRO ASP LYS GLU ASN LYS THR
SEQRES 8 A 231 LEU THR VAL GLU ASP ASN GLY ILE GLY MET THR LYS ALA
SEQRES 9 A 231 ASP LEU VAL ASN ASN LEU GLY THR ILE ALA ARG SER GLY
SEQRES 10 A 231 THR LYS ALA PHE MET GLU ALA LEU GLU ALA GLY GLY ASP
SEQRES 11 A 231 MET SER MET ILE GLY GLN PHE GLY VAL GLY PHE TYR SER
SEQRES 12 A 231 ALA TYR LEU VAL ALA ASP ARG VAL THR VAL THR SER LYS
SEQRES 13 A 231 ASN ASN SER ASP GLU SER TYR VAL TRP GLU SER SER ALA
SEQRES 14 A 231 GLY GLY THR PHE THR ILE THR SER THR PRO GLU SER ASP
SEQRES 15 A 231 MET LYS ARG GLY THR ARG ILE THR LEU HIS LEU LYS GLU
SEQRES 16 A 231 ASP GLN MET GLU TYR LEU GLU PRO ARG ARG LEU LYS GLU
SEQRES 17 A 231 LEU ILE LYS LYS HIS SER GLU PHE ILE GLY TYR ASP ILE
SEQRES 18 A 231 GLU LEU MET VAL GLU LYS THR THR GLU LYS
HET ADP A 214 27
HET MG A 215 1
HET EDO A 216 4
HET EDO A 217 4
HET EDO A 218 4
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 7 HOH *187(H2 O)
HELIX 1 1 GLN A 8 THR A 21 1 14
HELIX 2 2 GLU A 27 ASP A 51 1 25
HELIX 3 3 PRO A 52 GLY A 56 5 5
HELIX 4 4 THR A 84 LEU A 92 1 9
HELIX 5 5 GLY A 99 ALA A 109 1 11
HELIX 6 6 ASP A 112 GLY A 120 5 9
HELIX 7 7 VAL A 121 TYR A 124 5 4
HELIX 8 8 SER A 125 VAL A 129 1 5
HELIX 9 9 GLU A 177 LEU A 183 5 7
HELIX 10 10 GLU A 184 HIS A 195 1 12
SHEET 1 A 8 MET A 1 ALA A 6 0
SHEET 2 A 8 THR A 154 SER A 159 -1 O PHE A 155 N PHE A 5
SHEET 3 A 8 TYR A 145 SER A 149 -1 N VAL A 146 O THR A 158
SHEET 4 A 8 ALA A 130 LYS A 138 -1 N VAL A 135 O TRP A 147
SHEET 5 A 8 GLY A 168 LEU A 175 -1 O THR A 172 N THR A 134
SHEET 6 A 8 THR A 73 ASP A 78 -1 N LEU A 74 O LEU A 173
SHEET 7 A 8 CYS A 62 ASP A 68 -1 N VAL A 66 O THR A 75
SHEET 8 A 8 ASP A 202 LEU A 205 1 O ASP A 202 N ILE A 63
LINK OD1 ASN A 36 MG MG A 215 1555 1555 2.00
LINK O1A ADP A 214 MG MG A 215 1555 1555 2.07
LINK O1B ADP A 214 MG MG A 215 1555 1555 2.08
LINK MG MG A 215 O HOH A 356 1555 1555 2.09
LINK MG MG A 215 O HOH A 357 1555 1555 2.16
LINK MG MG A 215 O HOH A 358 1555 1555 2.15
SITE 1 AC1 26 ASN A 36 ALA A 40 ASP A 78 MET A 83
SITE 2 AC1 26 ASN A 91 LEU A 92 ARG A 97 VAL A 121
SITE 3 AC1 26 GLY A 122 PHE A 123 THR A 169 MG A 215
SITE 4 AC1 26 HOH A 220 HOH A 223 HOH A 225 HOH A 230
SITE 5 AC1 26 HOH A 234 HOH A 280 HOH A 289 HOH A 290
SITE 6 AC1 26 HOH A 293 HOH A 295 HOH A 327 HOH A 356
SITE 7 AC1 26 HOH A 357 HOH A 358
SITE 1 AC2 5 ASN A 36 ADP A 214 HOH A 356 HOH A 357
SITE 2 AC2 5 HOH A 358
SITE 1 AC3 5 SER A 144 THR A 158 SER A 159 THR A 160
SITE 2 AC3 5 SER A 163
SITE 1 AC4 2 LEU A 61 TYR A 201
SITE 1 AC5 4 SER A 53 VAL A 54 GLY A 56 HOH A 229
CRYST1 121.865 42.991 51.253 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 0.008206 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023261 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019511 0.00000
(ATOM LINES ARE NOT SHOWN.)
END