| content |
HEADER HYDROLASE/INHIBITOR 15-APR-21 7MHD
TITLE THIOESTERASE DOMAIN OF HUMAN FATTY ACID SYNTHASE (FASN-TE) BINDING A
TITLE 2 COMPETITIVE INHIBITOR SBP-7635
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIOESTERASE;
COMPND 5 SYNONYM: TYPE I FATTY ACID SYNTHASE;
COMPND 6 EC: 3.1.2.14;
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 GENE: FASN, FAS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE DOMAIN, FATTY ACID SYNTHASE, HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.ALESHIN,L.LAMBERT,R.C.LIDDINGTON,N.COSFORD
REVDAT 1 20-APR-22 7MHD 0
JRNL AUTH A.E.ALESHIN,L.LAMBERT,R.C.LIDDINGTON,N.COSFORD
JRNL TITL THIOESTERASE DOMAIN OF HUMAN FATTY ACID SYNTHASE (FASN-TE)
JRNL TITL 2 BINDING A COMPETITIVE INHIBITOR SBP-7635
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 16028
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 824
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 991
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2189
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 106
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61000
REMARK 3 B22 (A**2) : -1.91000
REMARK 3 B33 (A**2) : 1.31000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.242
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.197
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.130
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2321 ; 0.007 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2114 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3158 ; 1.526 ; 1.658
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4909 ; 1.289 ; 1.577
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 291 ; 6.308 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 121 ;34.782 ;21.901
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 379 ;15.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.184 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 298 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2632 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 492 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7MHD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-21.
REMARK 100 THE DEPOSITION ID IS D_1000256263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : PH 6.0-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16885
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.61800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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: 3TJM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 UL OF 8 MG/ML FASN-TE IN 100 MM
REMARK 280 NACL, 50 MM BISTRIS PH 6.0, 10 MM DTT, 0.5 MM OF THE INHIBITOR
REMARK 280 AND 1% DMSO WERE MIXED WITH 0.2 UL OF WELL SOLUTION 10% PEG400,
REMARK 280 50 MM TRIS-CL PH 8.5, 1 MM DTT, 1 MM ETHYLENEDIAMINETETRAACETIC
REMARK 280 ACID DISODIUM SALT (EDTA), 300 MM NACL., VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 26.94300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.72500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.74300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.72500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.94300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.74300
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 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 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 207
REMARK 465 SER A 208
REMARK 465 GLY A 209
REMARK 465 GLY A 210
REMARK 465 GLY A 211
REMARK 465 GLY A 212
REMARK 465 GLY A 213
REMARK 465 SER A 214
REMARK 465 THR A 215
REMARK 465 GLY A 452
REMARK 465 ALA A 453
REMARK 465 TYR A 454
REMARK 465 GLY A 455
REMARK 465 GLU A 456
REMARK 465 GLU A 503
REMARK 465 HIS A 504
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 385 O HOH A 701 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 308 -126.52 59.75
REMARK 500 CYS A 359 76.66 -108.29
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 ZEP A 601
DBREF 7MHD A 215 503 UNP P49327 FAS_HUMAN 2215 2503
SEQADV 7MHD GLY A 207 UNP P49327 EXPRESSION TAG
SEQADV 7MHD SER A 208 UNP P49327 EXPRESSION TAG
SEQADV 7MHD GLY A 209 UNP P49327 EXPRESSION TAG
SEQADV 7MHD GLY A 210 UNP P49327 EXPRESSION TAG
SEQADV 7MHD GLY A 211 UNP P49327 EXPRESSION TAG
SEQADV 7MHD GLY A 212 UNP P49327 EXPRESSION TAG
SEQADV 7MHD GLY A 213 UNP P49327 EXPRESSION TAG
SEQADV 7MHD SER A 214 UNP P49327 EXPRESSION TAG
SEQADV 7MHD HIS A 504 UNP P49327 EXPRESSION TAG
SEQRES 1 A 298 GLY SER GLY GLY GLY GLY GLY SER THR GLN LEU ASN LEU
SEQRES 2 A 298 ARG SER LEU LEU VAL ASN PRO GLU GLY PRO THR LEU MET
SEQRES 3 A 298 ARG LEU ASN SER VAL GLN SER SER GLU ARG PRO LEU PHE
SEQRES 4 A 298 LEU VAL HIS PRO ILE GLU GLY SER THR THR VAL PHE HIS
SEQRES 5 A 298 SER LEU ALA SER ARG LEU SER ILE PRO THR TYR GLY LEU
SEQRES 6 A 298 GLN CYS THR ARG ALA ALA PRO LEU ASP SER ILE HIS SER
SEQRES 7 A 298 LEU ALA ALA TYR TYR ILE ASP CYS ILE ARG GLN VAL GLN
SEQRES 8 A 298 PRO GLU GLY PRO TYR ARG VAL ALA GLY TYR SER TYR GLY
SEQRES 9 A 298 ALA CYS VAL ALA PHE GLU MET CYS SER GLN LEU GLN ALA
SEQRES 10 A 298 GLN GLN SER PRO ALA PRO THR HIS ASN SER LEU PHE LEU
SEQRES 11 A 298 PHE ASP GLY SER PRO THR TYR VAL LEU ALA TYR THR GLN
SEQRES 12 A 298 SER TYR ARG ALA LYS LEU THR PRO GLY CYS GLU ALA GLU
SEQRES 13 A 298 ALA GLU THR GLU ALA ILE CYS PHE PHE VAL GLN GLN PHE
SEQRES 14 A 298 THR ASP MET GLU HIS ASN ARG VAL LEU GLU ALA LEU LEU
SEQRES 15 A 298 PRO LEU LYS GLY LEU GLU GLU ARG VAL ALA ALA ALA VAL
SEQRES 16 A 298 ASP LEU ILE ILE LYS SER HIS GLN GLY LEU ASP ARG GLN
SEQRES 17 A 298 GLU LEU SER PHE ALA ALA ARG SER PHE TYR TYR LYS LEU
SEQRES 18 A 298 ARG ALA ALA GLU GLN TYR THR PRO LYS ALA LYS TYR HIS
SEQRES 19 A 298 GLY ASN VAL MET LEU LEU ARG ALA LYS THR GLY GLY ALA
SEQRES 20 A 298 TYR GLY GLU ASP LEU GLY ALA ASP TYR ASN LEU SER GLN
SEQRES 21 A 298 VAL CYS ASP GLY LYS VAL SER VAL HIS VAL ILE GLU GLY
SEQRES 22 A 298 ASP HIS ARG THR LEU LEU GLU GLY SER GLY LEU GLU SER
SEQRES 23 A 298 ILE ILE SER ILE ILE HIS SER SER LEU ALA GLU HIS
HET ZEP A 601 27
HETNAM ZEP N,N-DIETHYL-4-{2-[(2-FLUOROPHENYL)METHYL]-1,3-THIAZOL-
HETNAM 2 ZEP 4-YL}BENZENE-1-SULFONAMIDE
FORMUL 2 ZEP C20 H21 F N2 O2 S2
FORMUL 3 HOH *106(H2 O)
HELIX 1 AA1 ASN A 218 LEU A 222 5 5
HELIX 2 AA2 THR A 254 VAL A 256 5 3
HELIX 3 AA3 PHE A 257 LEU A 264 1 8
HELIX 4 AA4 SER A 281 ARG A 294 1 14
HELIX 5 AA5 SER A 308 SER A 326 1 19
HELIX 6 AA6 SER A 340 ALA A 353 1 14
HELIX 7 AA7 CYS A 359 GLN A 374 1 16
HELIX 8 AA8 GLU A 379 LEU A 388 1 10
HELIX 9 AA9 GLY A 392 HIS A 408 1 17
HELIX 10 AB1 ASP A 412 GLN A 432 1 21
HELIX 11 AB2 ASN A 463 VAL A 467 5 5
HELIX 12 AB3 GLU A 486 LEU A 501 1 16
SHEET 1 AA1 7 LEU A 231 ARG A 233 0
SHEET 2 AA1 7 THR A 268 LEU A 271 -1 O GLY A 270 N MET A 232
SHEET 3 AA1 7 LEU A 244 VAL A 247 1 N LEU A 246 O LEU A 271
SHEET 4 AA1 7 ARG A 303 TYR A 307 1 O ALA A 305 N VAL A 247
SHEET 5 AA1 7 SER A 333 PHE A 337 1 O SER A 333 N VAL A 304
SHEET 6 AA1 7 VAL A 443 ALA A 448 1 O MET A 444 N LEU A 336
SHEET 7 AA1 7 VAL A 472 ILE A 477 1 O SER A 473 N LEU A 445
CISPEP 1 GLY A 300 PRO A 301 0 -0.92
CISPEP 2 SER A 326 PRO A 327 0 -1.33
SITE 1 AC1 15 ILE A 250 SER A 308 TYR A 343 VAL A 344
SITE 2 AC1 15 TYR A 347 TYR A 351 ARG A 352 ALA A 363
SITE 3 AC1 15 GLU A 366 ALA A 367 TYR A 424 LEU A 427
SITE 4 AC1 15 GLU A 431 HIS A 481 HOH A 720
CRYST1 53.886 61.486 77.450 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 0.018558 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016264 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012912 0.00000
TER 2242 ALA A 502
MASTER 297 0 1 12 7 0 4 6 2322 1 27 23
END |