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HEADER HYDROLASE 09-JAN-15 4XJV
TITLE CRYSTAL STRUCTURE OF HUMAN THIOESTERASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-ACYL FATTY ACID SYNTHASE THIOESTERASE, MEDIUM CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AUGMENTED IN RHEUMATOID ARTHRITIS 1,AURA1,OLEOYL-ACP
COMPND 5 HYDROLASE,THIOESTERASE II,THIOESTERASE DOMAIN-CONTAINING PROTEIN 1;
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: OLAH, THEDC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41(DE3)
KEYWDS CLOSED CONFORMATION, FATTY ACID SYNTHASE, LIPID METABOLISM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.RITCHIE,S.J.KRIDEL,W.T.LOWTHER
REVDAT 1 16-DEC-15 4XJV 0
JRNL AUTH M.K.RITCHIE,L.C.JOHNSON,J.E.CLODFELTER,C.W.PEMBLE,B.E.FULP,
JRNL AUTH 2 C.M.FURDUI,S.J.KRIDEL,W.T.LOWTHER
JRNL TITL CRYSTAL STRUCTURE AND SUBSTRATE SPECIFICITY OF HUMAN
JRNL TITL 2 THIOESTERASE 2: INSIGHTS INTO THE MOLECULAR BASIS FOR THE
JRNL TITL 3 MODULATION OF FATTY ACID SYNTHASE
JRNL REF J.BIOL.CHEM. 2015
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M115.702597
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 9353
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.297
REMARK 3 R VALUE (WORKING SET) : 0.294
REMARK 3 FREE R VALUE : 0.345
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 473
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.8182 - 4.0347 0.99 3106 165 0.2613 0.2974
REMARK 3 2 4.0347 - 3.2046 0.95 2849 155 0.3279 0.4277
REMARK 3 3 3.2046 - 2.8002 0.98 2925 153 0.3739 0.4100
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 94.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 1745
REMARK 3 ANGLE : 0.725 2363
REMARK 3 CHIRALITY : 0.028 261
REMARK 3 PLANARITY : 0.003 301
REMARK 3 DIHEDRAL : 13.216 628
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 25:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0310 -30.3050 -22.3035
REMARK 3 T TENSOR
REMARK 3 T11: 0.8033 T22: 1.1736
REMARK 3 T33: 1.0683 T12: 0.3475
REMARK 3 T13: -0.0890 T23: -0.3986
REMARK 3 L TENSOR
REMARK 3 L11: 5.5432 L22: 4.1092
REMARK 3 L33: 7.5914 L12: 3.7442
REMARK 3 L13: -2.8168 L23: -4.7551
REMARK 3 S TENSOR
REMARK 3 S11: -0.0979 S12: -1.4206 S13: 0.1609
REMARK 3 S21: 0.1885 S22: 0.3378 S23: -1.4241
REMARK 3 S31: -0.5398 S32: 2.0960 S33: -0.2461
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 52:95)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9031 -20.1528 -28.5382
REMARK 3 T TENSOR
REMARK 3 T11: 1.3078 T22: 0.7777
REMARK 3 T33: 1.0498 T12: 0.1148
REMARK 3 T13: 0.1472 T23: -0.3253
REMARK 3 L TENSOR
REMARK 3 L11: 4.7702 L22: 5.7449
REMARK 3 L33: 6.2069 L12: -0.2833
REMARK 3 L13: -0.0272 L23: 2.3522
REMARK 3 S TENSOR
REMARK 3 S11: -0.2017 S12: -1.0324 S13: 1.2996
REMARK 3 S21: -0.6206 S22: 1.7752 S23: -1.0838
REMARK 3 S31: -0.0493 S32: 1.6565 S33: -1.4437
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 96:156)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1142 -26.4920 -19.3782
REMARK 3 T TENSOR
REMARK 3 T11: 0.6940 T22: 0.6396
REMARK 3 T33: 0.6597 T12: 0.3525
REMARK 3 T13: -0.0333 T23: -0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 5.3503 L22: 3.5141
REMARK 3 L33: 6.6016 L12: -2.0166
REMARK 3 L13: -5.2928 L23: 3.9579
REMARK 3 S TENSOR
REMARK 3 S11: -0.1201 S12: -0.1973 S13: 0.1603
REMARK 3 S21: 0.0562 S22: 0.3339 S23: 0.1910
REMARK 3 S31: -0.2189 S32: 0.0501 S33: -0.2488
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 157:173)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3599 -27.3732 2.7720
REMARK 3 T TENSOR
REMARK 3 T11: 1.2900 T22: 1.4747
REMARK 3 T33: 0.5421 T12: 0.2630
REMARK 3 T13: -0.1747 T23: 0.2492
REMARK 3 L TENSOR
REMARK 3 L11: 4.8681 L22: 4.3836
REMARK 3 L33: 5.7987 L12: 4.4084
REMARK 3 L13: 5.2909 L23: 4.9346
REMARK 3 S TENSOR
REMARK 3 S11: 0.7453 S12: -2.3702 S13: -0.4183
REMARK 3 S21: 0.7583 S22: -1.6954 S23: -0.5088
REMARK 3 S31: 1.2392 S32: -1.0463 S33: 0.9607
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 174:199)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9613 -20.9849 -14.9270
REMARK 3 T TENSOR
REMARK 3 T11: 0.7088 T22: 0.7733
REMARK 3 T33: 0.7403 T12: 0.2791
REMARK 3 T13: 0.0588 T23: -0.1454
REMARK 3 L TENSOR
REMARK 3 L11: 2.5505 L22: 9.0154
REMARK 3 L33: 2.8999 L12: 1.9155
REMARK 3 L13: 1.9011 L23: 4.7689
REMARK 3 S TENSOR
REMARK 3 S11: -0.5053 S12: -0.3965 S13: 0.6869
REMARK 3 S21: -0.9161 S22: -0.4721 S23: 0.7631
REMARK 3 S31: -1.4895 S32: -1.6173 S33: 0.9634
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 200:265)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1050 -39.4683 -24.9266
REMARK 3 T TENSOR
REMARK 3 T11: 0.7528 T22: 0.6561
REMARK 3 T33: 0.5452 T12: 0.3051
REMARK 3 T13: -0.0056 T23: -0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 8.0474 L22: 6.2844
REMARK 3 L33: 5.1125 L12: -3.5289
REMARK 3 L13: -1.0237 L23: 0.9548
REMARK 3 S TENSOR
REMARK 3 S11: -0.3833 S12: -0.6150 S13: -0.1185
REMARK 3 S21: 0.4272 S22: 0.4648 S23: 0.2126
REMARK 3 S31: 0.2396 S32: -0.0274 S33: -0.0950
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XJV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205795.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK 9.9.9.1L
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.9.9.1L
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9601
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 24.817
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.82
REMARK 200 R MERGE FOR SHELL (I) : 0.48700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.9-1692
REMARK 200 STARTING MODEL: 3FLB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ROD-SHAPED CRYSTALS OF TE2 (10 MG/ML
REMARK 280 WITH 10 MM FRESH DTT) WERE GROWN USING THE VAPOR DIFFUSION
REMARK 280 METHOD AT 25 C, USING A 1:1 DROP TO WELL RATIO. THE WELL
REMARK 280 SOLUTIONS CONTAINED 1.64 M NAH2PO4, 0.42 M K2HPO4 AND 50 MM
REMARK 280 HEPES. CRYSTALS WERE CRYOPROTECTED BY TRANSFER TO PARATONE., PH
REMARK 280 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 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 0.00000
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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 48.03500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 79.98000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 48.03500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 79.98000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 48.03500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 79.98000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 48.03500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 79.98000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 48.03500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 79.98000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 48.03500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 79.98000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 48.03500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 79.98000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 48.03500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 48.03500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 79.98000
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 -5
REMARK 465 ILE A -4
REMARK 465 ASP A -3
REMARK 465 PRO A -2
REMARK 465 PHE A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ARG A 3
REMARK 465 GLY A 4
REMARK 465 ASP A 5
REMARK 465 GLN A 6
REMARK 465 PRO A 7
REMARK 465 LYS A 8
REMARK 465 ARG A 9
REMARK 465 THR A 10
REMARK 465 ARG A 11
REMARK 465 ASN A 12
REMARK 465 GLU A 13
REMARK 465 ASN A 14
REMARK 465 ILE A 15
REMARK 465 PHE A 16
REMARK 465 ASN A 17
REMARK 465 CYS A 18
REMARK 465 LEU A 19
REMARK 465 TYR A 20
REMARK 465 LYS A 21
REMARK 465 ASN A 22
REMARK 465 PRO A 23
REMARK 465 GLU A 24
REMARK 465 ARG A 59
REMARK 465 LEU A 60
REMARK 465 PRO A 61
REMARK 465 GLY A 62
REMARK 465 ARG A 63
REMARK 465 GLU A 64
REMARK 465 SER A 65
REMARK 465 ARG A 66
REMARK 465 VAL A 67
REMARK 465 GLU A 68
REMARK 465 GLU A 69
REMARK 465 PRO A 70
REMARK 465 LEU A 71
REMARK 465 GLU A 72
REMARK 465 ASN A 73
REMARK 465 ASP A 74
REMARK 465 ILE A 75
REMARK 465 SER A 76
REMARK 465 PHE A 159
REMARK 465 GLY A 160
REMARK 465 GLY A 161
REMARK 465 THR A 162
REMARK 465 PRO A 163
REMARK 465 LYS A 164
REMARK 465 HIS A 165
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 39 10.68 59.39
REMARK 500 PHE A 42 36.92 -87.56
REMARK 500 ALA A 43 36.77 -93.87
REMARK 500 GLN A 47 35.07 -144.73
REMARK 500 SER A 57 111.45 69.53
REMARK 500 GLN A 91 -123.26 56.79
REMARK 500 SER A 101 -103.62 53.51
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 301
DBREF 4XJV A 1 265 UNP Q9NV23 SAST_HUMAN 1 265
SEQADV 4XJV GLY A -5 UNP Q9NV23 EXPRESSION TAG
SEQADV 4XJV ILE A -4 UNP Q9NV23 EXPRESSION TAG
SEQADV 4XJV ASP A -3 UNP Q9NV23 EXPRESSION TAG
SEQADV 4XJV PRO A -2 UNP Q9NV23 EXPRESSION TAG
SEQADV 4XJV PHE A -1 UNP Q9NV23 EXPRESSION TAG
SEQADV 4XJV THR A 0 UNP Q9NV23 EXPRESSION TAG
SEQRES 1 A 271 GLY ILE ASP PRO PHE THR MET GLU ARG GLY ASP GLN PRO
SEQRES 2 A 271 LYS ARG THR ARG ASN GLU ASN ILE PHE ASN CYS LEU TYR
SEQRES 3 A 271 LYS ASN PRO GLU ALA THR PHE LYS LEU ILE CYS PHE PRO
SEQRES 4 A 271 TRP MET GLY GLY GLY SER THR HIS PHE ALA LYS TRP GLY
SEQRES 5 A 271 GLN ASP THR HIS ASP LEU LEU GLU VAL HIS SER LEU ARG
SEQRES 6 A 271 LEU PRO GLY ARG GLU SER ARG VAL GLU GLU PRO LEU GLU
SEQRES 7 A 271 ASN ASP ILE SER GLN LEU VAL ASP GLU VAL VAL CYS ALA
SEQRES 8 A 271 LEU GLN PRO VAL ILE GLN ASP LYS PRO PHE ALA PHE PHE
SEQRES 9 A 271 GLY HIS SER MET GLY SER TYR ILE ALA PHE ARG THR ALA
SEQRES 10 A 271 LEU GLY LEU LYS GLU ASN ASN GLN PRO GLU PRO LEU HIS
SEQRES 11 A 271 LEU PHE LEU SER SER ALA THR PRO VAL HIS SER LYS ALA
SEQRES 12 A 271 TRP HIS ARG ILE PRO LYS ASP ASP GLU LEU SER GLU GLU
SEQRES 13 A 271 GLN ILE SER HIS TYR LEU MET GLU PHE GLY GLY THR PRO
SEQRES 14 A 271 LYS HIS PHE ALA GLU ALA LYS GLU PHE VAL LYS GLN CYS
SEQRES 15 A 271 SER PRO ILE ILE ARG ALA ASP LEU ASN ILE VAL ARG SER
SEQRES 16 A 271 CYS THR SER ASN VAL PRO SER LYS ALA VAL LEU SER CYS
SEQRES 17 A 271 ASP LEU THR CYS PHE VAL GLY SER GLU ASP ILE ALA LYS
SEQRES 18 A 271 ASP MET GLU ALA TRP LYS ASP VAL THR SER GLY ASN ALA
SEQRES 19 A 271 LYS ILE TYR GLN LEU PRO GLY GLY HIS PHE TYR LEU LEU
SEQRES 20 A 271 ASP PRO ALA ASN GLU LYS LEU ILE LYS ASN TYR ILE ILE
SEQRES 21 A 271 LYS CYS LEU GLU VAL SER SER ILE SER ASN PHE
HET CL A 301 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
HELIX 1 AA1 LEU A 78 CYS A 84 1 7
HELIX 2 AA2 LEU A 86 GLN A 91 1 6
HELIX 3 AA3 SER A 101 ASN A 117 1 17
HELIX 4 AA4 LYS A 143 LEU A 147 5 5
HELIX 5 AA5 SER A 148 GLU A 158 1 11
HELIX 6 AA6 PHE A 172 THR A 191 1 20
HELIX 7 AA7 ASP A 216 THR A 224 5 9
HELIX 8 AA8 PHE A 238 LEU A 241 5 4
HELIX 9 AA9 ASP A 242 SER A 260 1 19
SHEET 1 AA1 6 GLU A 54 VAL A 55 0
SHEET 2 AA1 6 LYS A 28 PHE A 32 1 N LEU A 29 O GLU A 54
SHEET 3 AA1 6 PHE A 95 HIS A 100 1 O ALA A 96 N ILE A 30
SHEET 4 AA1 6 HIS A 124 SER A 128 1 O PHE A 126 N PHE A 97
SHEET 5 AA1 6 ASP A 203 GLY A 209 1 O PHE A 207 N LEU A 127
SHEET 6 AA1 6 ALA A 228 LEU A 233 1 O LYS A 229 N CYS A 206
CISPEP 1 GLN A 47 ASP A 48 0 -6.31
SITE 1 AC1 4 MET A 35 SER A 101 MET A 102 GLU A 158
CRYST1 96.070 96.070 159.960 90.00 90.00 90.00 I 4 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 0.010409 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010409 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006252 0.00000
TER 3371 PHE A 265
MASTER 424 0 1 9 6 0 1 6 1703 1 0 21
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