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HEADER HYDROXYLASE 29-SEP-04 1XKT
TITLE HUMAN FATTY ACID SYNTHASE: STRUCTURE AND SUBSTRATE
TITLE 2 SELECTIVITY OF THE THIOESTERASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PROEX
KEYWDS HUMAN FATTY ACID SYNTHASE, THIOESTERASE, STRUCTURE,
KEYWDS 2 SPECIFICITY, DRUG TARGET
EXPDTA X-RAY DIFFRACTION
AUTHOR B.CHAKRAVARTY,G.ZIWEI,S.S.CHIRALA,S.J.WAKIL,F.A.QUIOCHO
REVDAT 1 26-OCT-04 1XKT 0
JRNL AUTH B.CHAKRAVARTY,G.ZIWEI,S.S.CHIRALA,S.J.WAKIL,
JRNL AUTH 2 F.A.QUIOCHO
JRNL TITL HUMAN FATTY ACID SYNTHASE: STRUCTURE AND SUBSTRATE
JRNL TITL 2 SELECTIVITY OF THE THIOESTERASE DOMAIN
JRNL REF TO BE PUBLISHED
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 11.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 470097.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 21444
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) : 0.258
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1043
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3174
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 185
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 65
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.03000
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) : 0.41
REMARK 3 ESD FROM SIGMAA (A) : 0.41
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) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.86
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 : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 47.02
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ACTIVE SITE, SER 2308, HAS BAD
REMARK 3 PHI AND PSI VALUES, AS SEEN IN SERINE-LIKE PROTEASES.
REMARK 4
REMARK 4 1XKT COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-2004.
REMARK 100 THE RCSB ID CODE IS RCSB030468.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-2002
REMARK 200 TEMPERATURE (KELVIN) : 150.0
REMARK 200 PH : 6.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96865, 0.97930, 0.97910,
REMARK 200 0.96390
REMARK 200 MONOCHROMATOR : KOHZU DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21444
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES, GLYCEROL, PH
REMARK 280 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
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 3555 -Y,X,1/4+Z
REMARK 290 4555 Y,-X,3/4+Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,1/2-Z
REMARK 290 7555 Y,X,3/4-Z
REMARK 290 8555 -Y,-X,1/4-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 63.23000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.61500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 94.84500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 63.23000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 94.84500
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 31.61500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
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 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 GLY A 2214
REMARK 465 ALA A 2215
REMARK 465 MET A 2216
REMARK 465 GLN A 2325
REMARK 465 SER A 2326
REMARK 465 PRO A 2327
REMARK 465 ALA A 2328
REMARK 465 PRO A 2329
REMARK 465 THR A 2330
REMARK 465 VAL A 2344
REMARK 465 LEU A 2345
REMARK 465 ALA A 2346
REMARK 465 TYR A 2347
REMARK 465 THR A 2348
REMARK 465 GLN A 2349
REMARK 465 SER A 2350
REMARK 465 TYR A 2351
REMARK 465 ARG A 2352
REMARK 465 ALA A 2353
REMARK 465 LYS A 2354
REMARK 465 LEU A 2355
REMARK 465 THR A 2356
REMARK 465 GLY A 2452
REMARK 465 ALA A 2453
REMARK 465 TYR A 2454
REMARK 465 GLY A 2455
REMARK 465 GLU A 2456
REMARK 465 ASP A 2457
REMARK 465 GLY A 2487
REMARK 465 GLY B 2214
REMARK 465 ALA B 2215
REMARK 465 MET B 2216
REMARK 465 GLN B 2325
REMARK 465 SER B 2326
REMARK 465 PRO B 2327
REMARK 465 ALA B 2328
REMARK 465 PRO B 2329
REMARK 465 THR B 2330
REMARK 465 VAL B 2344
REMARK 465 LEU B 2345
REMARK 465 ALA B 2346
REMARK 465 TYR B 2347
REMARK 465 THR B 2348
REMARK 465 GLN B 2349
REMARK 465 SER B 2350
REMARK 465 TYR B 2351
REMARK 465 ARG B 2352
REMARK 465 ALA B 2353
REMARK 465 LYS B 2354
REMARK 465 LEU B 2355
REMARK 465 THR B 2356
REMARK 465 GLY B 2452
REMARK 465 ALA B 2453
REMARK 465 TYR B 2454
REMARK 465 GLY B 2455
REMARK 465 GLU B 2456
REMARK 465 ASP B 2457
REMARK 465 GLY B 2487
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A2226 CB PRO A2226 CG 0.053
REMARK 500 CYS A2312 CB CYS A2312 SG -0.047
REMARK 500 MET A2317 SD MET A2317 CE -0.056
REMARK 500 PRO B2229 CB PRO B2229 CG 0.048
REMARK 500 MET B2317 SD MET B2317 CE -0.095
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A2249 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLY A2252 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 GLU A2299 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLY A2300 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 GLY B2252 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 GLU B2299 N - CA - C ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLY B2300 N - CA - C ANGL. DEV. = 16.0 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A2308 -108.93 58.16
REMARK 500 SER B2308 -110.99 57.91
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS A MISMATCH IN POSTION 2440 FROM THE DATABASE
REMARK 999 REFERENCE SEQUENCE OF FATTY ACID SYNTHASE, WHICH IS
REMARK 999 DUE TO THE HETEREGENEITY OF THAT POSITION IN DIFFERENT
REMARK 999 CLONES.
DBREF 1XKT A 2218 2502 GB 41872631 NP_004095 2218 2502
DBREF 1XKT B 2218 2502 GB 41872631 NP_004095 2218 2502
SEQADV 1XKT GLY A 2214 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT ALA A 2215 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT MET A 2216 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT VAL A 2217 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT TYR A 2440 GB 41872631 HIS 2440 SEE REMARK 999
SEQADV 1XKT GLY B 2214 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT ALA B 2215 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT MET B 2216 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT VAL B 2217 GB 41872631 CLONING ARTIFACT
SEQADV 1XKT TYR B 2440 GB 41872631 HIS 2440 SEE REMARK 999
SEQRES 1 A 289 GLY ALA MET VAL ASN LEU ARG SER LEU LEU VAL ASN PRO
SEQRES 2 A 289 GLU GLY PRO THR LEU MET ARG LEU ASN SER VAL GLN SER
SEQRES 3 A 289 SER GLU ARG PRO LEU PHE LEU VAL HIS PRO ILE GLU GLY
SEQRES 4 A 289 SER THR THR VAL PHE HIS SER LEU ALA SER ARG LEU SER
SEQRES 5 A 289 ILE PRO THR TYR GLY LEU GLN CYS THR ARG ALA ALA PRO
SEQRES 6 A 289 LEU ASP SER ILE HIS SER LEU ALA ALA TYR TYR ILE ASP
SEQRES 7 A 289 CYS ILE ARG GLN VAL GLN PRO GLU GLY PRO TYR ARG VAL
SEQRES 8 A 289 ALA GLY TYR SER TYR GLY ALA CYS VAL ALA PHE GLU MET
SEQRES 9 A 289 CYS SER GLN LEU GLN ALA GLN GLN SER PRO ALA PRO THR
SEQRES 10 A 289 HIS ASN SER LEU PHE LEU PHE ASP GLY SER PRO THR TYR
SEQRES 11 A 289 VAL LEU ALA TYR THR GLN SER TYR ARG ALA LYS LEU THR
SEQRES 12 A 289 PRO GLY CYS GLU ALA GLU ALA GLU THR GLU ALA ILE CYS
SEQRES 13 A 289 PHE PHE VAL GLN GLN PHE THR ASP MET GLU HIS ASN ARG
SEQRES 14 A 289 VAL LEU GLU ALA LEU LEU PRO LEU LYS GLY LEU GLU GLU
SEQRES 15 A 289 ARG VAL ALA ALA ALA VAL ASP LEU ILE ILE LYS SER HIS
SEQRES 16 A 289 GLN GLY LEU ASP ARG GLN GLU LEU SER PHE ALA ALA ARG
SEQRES 17 A 289 SER PHE TYR TYR LYS LEU ARG ALA ALA GLU GLN TYR THR
SEQRES 18 A 289 PRO LYS ALA LYS TYR TYR GLY ASN VAL MET LEU LEU ARG
SEQRES 19 A 289 ALA LYS THR GLY GLY ALA TYR GLY GLU ASP LEU GLY ALA
SEQRES 20 A 289 ASP TYR ASN LEU SER GLN VAL CYS ASP GLY LYS VAL SER
SEQRES 21 A 289 VAL HIS VAL ILE GLU GLY ASP HIS ARG THR LEU LEU GLU
SEQRES 22 A 289 GLY SER GLY LEU GLU SER ILE ILE SER ILE ILE HIS SER
SEQRES 23 A 289 SER LEU ALA
SEQRES 1 B 289 GLY ALA MET VAL ASN LEU ARG SER LEU LEU VAL ASN PRO
SEQRES 2 B 289 GLU GLY PRO THR LEU MET ARG LEU ASN SER VAL GLN SER
SEQRES 3 B 289 SER GLU ARG PRO LEU PHE LEU VAL HIS PRO ILE GLU GLY
SEQRES 4 B 289 SER THR THR VAL PHE HIS SER LEU ALA SER ARG LEU SER
SEQRES 5 B 289 ILE PRO THR TYR GLY LEU GLN CYS THR ARG ALA ALA PRO
SEQRES 6 B 289 LEU ASP SER ILE HIS SER LEU ALA ALA TYR TYR ILE ASP
SEQRES 7 B 289 CYS ILE ARG GLN VAL GLN PRO GLU GLY PRO TYR ARG VAL
SEQRES 8 B 289 ALA GLY TYR SER TYR GLY ALA CYS VAL ALA PHE GLU MET
SEQRES 9 B 289 CYS SER GLN LEU GLN ALA GLN GLN SER PRO ALA PRO THR
SEQRES 10 B 289 HIS ASN SER LEU PHE LEU PHE ASP GLY SER PRO THR TYR
SEQRES 11 B 289 VAL LEU ALA TYR THR GLN SER TYR ARG ALA LYS LEU THR
SEQRES 12 B 289 PRO GLY CYS GLU ALA GLU ALA GLU THR GLU ALA ILE CYS
SEQRES 13 B 289 PHE PHE VAL GLN GLN PHE THR ASP MET GLU HIS ASN ARG
SEQRES 14 B 289 VAL LEU GLU ALA LEU LEU PRO LEU LYS GLY LEU GLU GLU
SEQRES 15 B 289 ARG VAL ALA ALA ALA VAL ASP LEU ILE ILE LYS SER HIS
SEQRES 16 B 289 GLN GLY LEU ASP ARG GLN GLU LEU SER PHE ALA ALA ARG
SEQRES 17 B 289 SER PHE TYR TYR LYS LEU ARG ALA ALA GLU GLN TYR THR
SEQRES 18 B 289 PRO LYS ALA LYS TYR TYR GLY ASN VAL MET LEU LEU ARG
SEQRES 19 B 289 ALA LYS THR GLY GLY ALA TYR GLY GLU ASP LEU GLY ALA
SEQRES 20 B 289 ASP TYR ASN LEU SER GLN VAL CYS ASP GLY LYS VAL SER
SEQRES 21 B 289 VAL HIS VAL ILE GLU GLY ASP HIS ARG THR LEU LEU GLU
SEQRES 22 B 289 GLY SER GLY LEU GLU SER ILE ILE SER ILE ILE HIS SER
SEQRES 23 B 289 SER LEU ALA
FORMUL 3 HOH *65(H2 O1)
HELIX 1 1 VAL A 2217 LEU A 2223 5 7
HELIX 2 2 PHE A 2257 ARG A 2263 1 7
HELIX 3 3 SER A 2281 GLN A 2297 1 17
HELIX 4 4 TYR A 2309 GLN A 2324 1 16
HELIX 5 5 CYS A 2359 THR A 2376 1 18
HELIX 6 6 GLU A 2379 LEU A 2388 1 10
HELIX 7 7 GLY A 2392 LYS A 2406 1 15
HELIX 8 8 ASP A 2412 GLU A 2431 1 20
HELIX 9 9 SER A 2488 LEU A 2501 1 14
HELIX 10 10 VAL B 2217 LEU B 2223 5 7
HELIX 11 11 PHE B 2257 ARG B 2263 1 7
HELIX 12 12 SER B 2281 GLN B 2297 1 17
HELIX 13 13 TYR B 2309 GLN B 2324 1 16
HELIX 14 14 CYS B 2359 THR B 2376 1 18
HELIX 15 15 GLU B 2379 LEU B 2388 1 10
HELIX 16 16 GLY B 2392 LYS B 2406 1 15
HELIX 17 17 ASP B 2412 GLU B 2431 1 20
HELIX 18 18 SER B 2488 LEU B 2501 1 14
SHEET 1 A 7 LEU A2231 ASN A2235 0
SHEET 2 A 7 LEU A2244 VAL A2247 1 N LEU A2244 O TYR A2269
SHEET 3 A 7 THR A2268 LEU A2271 -1 O GLY A2270 N MET A2232
SHEET 4 A 7 ARG A2303 TYR A2307 1 O ALA A2305 N PHE A2245
SHEET 5 A 7 SER A2333 PHE A2337 1 O SER A2333 N VAL A2304
SHEET 6 A 7 VAL A2443 ALA A2448 1 O MET A2444 N LEU A2336
SHEET 7 A 7 VAL A2472 ILE A2477 1 O ILE A2477 N ARG A2447
SHEET 1 B 7 LEU B2231 ASN B2235 0
SHEET 2 B 7 LEU B2244 VAL B2247 1 N LEU B2246 O LEU B2271
SHEET 3 B 7 THR B2268 LEU B2271 -1 O GLY B2270 N MET B2232
SHEET 4 B 7 ARG B2303 TYR B2307 1 O ALA B2305 N PHE B2245
SHEET 5 B 7 SER B2333 PHE B2337 1 O SER B2333 N VAL B2304
SHEET 6 B 7 VAL B2443 ALA B2448 1 O MET B2444 N LEU B2336
SHEET 7 B 7 VAL B2472 ILE B2477 1 O ILE B2477 N ARG B2447
CRYST1 104.783 104.783 126.460 90.00 90.00 90.00 P 41 2 2 16
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 0.009544 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009544 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007908 0.00000
TER 2024 ALA A2502
TER 4048 ALA B2502
MASTER 361 0 0 18 14 0 0 6 4111 2 0 46
END |