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HEADER HYDROLASE 28-NOV-16 5MIF
TITLE CRYSTAL STRUCTURE OF CARBOXYL ESTERASE 2 (TMELEST2) FROM MYCORRHIZAL
TITLE 2 FUNGUS TUBER MELANOSPORUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 'CARBOXYL ESTERASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TUBER MELANOSPORUM MEL28;
SOURCE 3 ORGANISM_TAXID: 656061;
SOURCE 4 GENE: GSTUM_00003552001;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: CODONPLUS RIL
KEYWDS LIPASE ALPHA/BETA HYDROLASE FOLD ARCHAEBACTERIAL-LIKE ENZYMES,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.ZANOTTI,F.VALESSE,D.CAVAZZINI,S.OTTONELLO
REVDAT 1 23-AUG-17 5MIF 0
JRNL AUTH D.CAVAZZINI,G.GROSSI,E.LEVATI,F.VALLESE,B.MONTANINI,
JRNL AUTH 2 A.BOLCHI,G.ZANOTTI,S.OTTONELLO
JRNL TITL A FAMILY OF ARCHAEA-LIKE CARBOXYLESTERASES PREFERENTIALLY
JRNL TITL 2 EXPRESSED IN THE SYMBIOTIC PHASE OF THE MYCHORRIZAL FUNGUS
JRNL TITL 3 TUBER MELANOSPORUM.
JRNL REF SCI REP V. 7 7628 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28794466
JRNL DOI 10.1038/S41598-017-08007-9
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1647
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 176177
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 8795
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 47.2880 - 6.6456 0.99 5570 291 0.1489 0.1535
REMARK 3 2 6.6456 - 5.2771 1.00 5599 297 0.1484 0.1627
REMARK 3 3 5.2771 - 4.6107 1.00 5592 293 0.1363 0.1623
REMARK 3 4 4.6107 - 4.1894 1.00 5561 293 0.1328 0.1468
REMARK 3 5 4.1894 - 3.8893 1.00 5604 300 0.1487 0.1719
REMARK 3 6 3.8893 - 3.6601 1.00 5617 288 0.1719 0.2170
REMARK 3 7 3.6601 - 3.4768 1.00 5579 288 0.1848 0.1953
REMARK 3 8 3.4768 - 3.3255 1.00 5585 297 0.1857 0.2249
REMARK 3 9 3.3255 - 3.1975 1.00 5602 294 0.2012 0.2307
REMARK 3 10 3.1975 - 3.0872 1.00 5600 297 0.2082 0.2657
REMARK 3 11 3.0872 - 2.9907 1.00 5564 294 0.2119 0.2478
REMARK 3 12 2.9907 - 2.9052 1.00 5612 291 0.2055 0.2330
REMARK 3 13 2.9052 - 2.8287 1.00 5561 294 0.2114 0.2369
REMARK 3 14 2.8287 - 2.7597 1.00 5596 294 0.2031 0.2179
REMARK 3 15 2.7597 - 2.6970 1.00 5565 290 0.1893 0.2529
REMARK 3 16 2.6970 - 2.6396 1.00 5580 296 0.2017 0.2355
REMARK 3 17 2.6396 - 2.5868 1.00 5625 292 0.2028 0.2613
REMARK 3 18 2.5868 - 2.5380 1.00 5583 296 0.2054 0.2237
REMARK 3 19 2.5380 - 2.4927 1.00 5603 287 0.2205 0.2345
REMARK 3 20 2.4927 - 2.4504 1.00 5598 288 0.2217 0.2558
REMARK 3 21 2.4504 - 2.4109 1.00 5543 292 0.2038 0.2539
REMARK 3 22 2.4109 - 2.3738 1.00 5613 302 0.2172 0.2641
REMARK 3 23 2.3738 - 2.3389 1.00 5613 292 0.2170 0.2282
REMARK 3 24 2.3389 - 2.3060 1.00 5551 296 0.2205 0.2809
REMARK 3 25 2.3060 - 2.2748 1.00 5585 292 0.2281 0.2536
REMARK 3 26 2.2748 - 2.2453 1.00 5617 296 0.2309 0.2899
REMARK 3 27 2.2453 - 2.2172 1.00 5571 292 0.2420 0.2895
REMARK 3 28 2.2172 - 2.1905 1.00 5608 297 0.2431 0.2710
REMARK 3 29 2.1905 - 2.1650 1.00 5596 291 0.2517 0.2783
REMARK 3 30 2.1650 - 2.1407 0.94 5289 285 0.2635 0.3022
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.950
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) : 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 : 0.008 9505
REMARK 3 ANGLE : 1.159 12929
REMARK 3 CHIRALITY : 0.049 1454
REMARK 3 PLANARITY : 0.007 1672
REMARK 3 DIHEDRAL : 13.007 3497
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5MIF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1200002500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93001
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 47.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 71.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : 0.71100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: IN HOUSE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 MG/ML IN 25 MM TRIS-HCL PH 8.0,
REMARK 280 0.1M NACL, 2% V/V TRITON X-100) AND 20% POLYETHYLENE GLYCOL 3350
REMARK 280 IN 0.2 M KNO3 (PH 6.0), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 151.20600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 75.60300
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 113.40450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.80150
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 189.00750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 151.20600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 75.60300
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.80150
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 113.40450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 189.00750
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 504 LIES ON A SPECIAL POSITION.
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 ARG A 2
REMARK 465 PHE A 3
REMARK 465 THR A 4
REMARK 465 ILE A 5
REMARK 465 LEU A 6
REMARK 465 SER A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 PHE A 11
REMARK 465 SER A 12
REMARK 465 LEU A 13
REMARK 465 PRO A 14
REMARK 465 LEU A 15
REMARK 465 VAL A 16
REMARK 465 LEU A 17
REMARK 465 ALA A 18
REMARK 465 GLU A 19
REMARK 465 THR A 20
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 PRO A 23
REMARK 465 SER A 24
REMARK 465 CYS A 25
REMARK 465 PRO A 26
REMARK 465 VAL A 27
REMARK 465 THR A 28
REMARK 465 ASN A 29
REMARK 465 VAL A 30
REMARK 465 THR A 31
REMARK 465 THR A 32
REMARK 465 PRO A 33
REMARK 465 ASN A 67
REMARK 465 VAL A 68
REMARK 465 SER A 69
REMARK 465 ASP A 70
REMARK 465 PRO A 71
REMARK 465 GLY A 100
REMARK 465 GLU A 101
REMARK 465 ARG A 102
REMARK 465 GLU A 103
REMARK 465 LYS A 104
REMARK 465 GLY A 105
REMARK 465 LYS A 106
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 PHE B 3
REMARK 465 THR B 4
REMARK 465 ILE B 5
REMARK 465 LEU B 6
REMARK 465 SER B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 PHE B 11
REMARK 465 SER B 12
REMARK 465 LEU B 13
REMARK 465 PRO B 14
REMARK 465 LEU B 15
REMARK 465 VAL B 16
REMARK 465 LEU B 17
REMARK 465 ALA B 18
REMARK 465 GLU B 19
REMARK 465 THR B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 PRO B 23
REMARK 465 SER B 24
REMARK 465 CYS B 25
REMARK 465 PRO B 26
REMARK 465 VAL B 27
REMARK 465 THR B 28
REMARK 465 ASN B 29
REMARK 465 VAL B 30
REMARK 465 THR B 31
REMARK 465 THR B 32
REMARK 465 PRO B 33
REMARK 465 ASN B 67
REMARK 465 VAL B 68
REMARK 465 SER B 69
REMARK 465 ASP B 70
REMARK 465 PRO B 71
REMARK 465 GLY B 100
REMARK 465 GLU B 101
REMARK 465 ARG B 102
REMARK 465 GLU B 103
REMARK 465 LYS B 104
REMARK 465 GLY B 105
REMARK 465 LYS B 106
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 PHE C 3
REMARK 465 THR C 4
REMARK 465 ILE C 5
REMARK 465 LEU C 6
REMARK 465 SER C 7
REMARK 465 VAL C 8
REMARK 465 LEU C 9
REMARK 465 ALA C 10
REMARK 465 PHE C 11
REMARK 465 SER C 12
REMARK 465 LEU C 13
REMARK 465 PRO C 14
REMARK 465 LEU C 15
REMARK 465 VAL C 16
REMARK 465 LEU C 17
REMARK 465 ALA C 18
REMARK 465 GLU C 19
REMARK 465 THR C 20
REMARK 465 PRO C 21
REMARK 465 ALA C 22
REMARK 465 PRO C 23
REMARK 465 SER C 24
REMARK 465 CYS C 25
REMARK 465 PRO C 26
REMARK 465 VAL C 27
REMARK 465 THR C 28
REMARK 465 ASN C 29
REMARK 465 VAL C 30
REMARK 465 THR C 31
REMARK 465 THR C 32
REMARK 465 PRO C 33
REMARK 465 ASN C 67
REMARK 465 VAL C 68
REMARK 465 SER C 69
REMARK 465 ASP C 70
REMARK 465 PRO C 71
REMARK 465 SER C 99
REMARK 465 GLY C 100
REMARK 465 GLU C 101
REMARK 465 ARG C 102
REMARK 465 GLU C 103
REMARK 465 LYS C 104
REMARK 465 GLY C 105
REMARK 465 LYS C 106
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 PHE D 3
REMARK 465 THR D 4
REMARK 465 ILE D 5
REMARK 465 LEU D 6
REMARK 465 SER D 7
REMARK 465 VAL D 8
REMARK 465 LEU D 9
REMARK 465 ALA D 10
REMARK 465 PHE D 11
REMARK 465 SER D 12
REMARK 465 LEU D 13
REMARK 465 PRO D 14
REMARK 465 LEU D 15
REMARK 465 VAL D 16
REMARK 465 LEU D 17
REMARK 465 ALA D 18
REMARK 465 GLU D 19
REMARK 465 THR D 20
REMARK 465 PRO D 21
REMARK 465 ALA D 22
REMARK 465 PRO D 23
REMARK 465 SER D 24
REMARK 465 CYS D 25
REMARK 465 PRO D 26
REMARK 465 VAL D 27
REMARK 465 THR D 28
REMARK 465 ASN D 29
REMARK 465 VAL D 30
REMARK 465 THR D 31
REMARK 465 THR D 32
REMARK 465 PRO D 33
REMARK 465 ASN D 67
REMARK 465 VAL D 68
REMARK 465 SER D 69
REMARK 465 ASP D 70
REMARK 465 PRO D 71
REMARK 465 SER D 72
REMARK 465 GLY D 100
REMARK 465 GLU D 101
REMARK 465 ARG D 102
REMARK 465 GLU D 103
REMARK 465 LYS D 104
REMARK 465 GLY D 105
REMARK 465 LYS D 106
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 SER C 72 OG
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 O HOH C 665 O HOH C 670 1.43
REMARK 500 O HOH A 520 O HOH A 523 1.81
REMARK 500 OE1 GLN B 34 O HOH B 401 1.86
REMARK 500 O HOH C 569 O HOH C 631 1.89
REMARK 500 O HOH B 473 O HOH B 523 1.89
REMARK 500 O HOH D 661 O HOH D 693 1.90
REMARK 500 O HOH A 512 O HOH A 514 1.90
REMARK 500 O HOH C 667 O HOH C 674 1.90
REMARK 500 O HOH D 681 O HOH D 706 1.94
REMARK 500 O HOH C 614 O HOH C 659 1.96
REMARK 500 O HOH A 496 O HOH A 507 1.97
REMARK 500 O HOH D 623 O HOH D 646 2.00
REMARK 500 O SER B 66 O HOH B 402 2.02
REMARK 500 O SER B 66 O HOH B 403 2.02
REMARK 500 OE1 GLN A 291 O HOH A 401 2.03
REMARK 500 OE2 GLU D 74 O HOH D 501 2.03
REMARK 500 O HOH B 549 O HOH B 557 2.07
REMARK 500 N GLY C 236 O HOH C 501 2.08
REMARK 500 O ALA B 43 O HOH B 404 2.08
REMARK 500 OE1 GLU D 175 O HOH D 502 2.09
REMARK 500 OD2 ASP B 147 O HOH B 405 2.11
REMARK 500 O HOH A 514 O HOH A 519 2.12
REMARK 500 OH TYR A 340 OE1 GLU C 138 2.12
REMARK 500 OH TYR A 42 O HOH A 402 2.12
REMARK 500 O HOH D 701 O HOH D 705 2.13
REMARK 500 O LEU D 57 O HOH D 503 2.13
REMARK 500 O HOH B 557 O HOH B 562 2.13
REMARK 500 OE1 GLU C 232 O HOH C 502 2.14
REMARK 500 O HOH B 519 O HOH B 542 2.14
REMARK 500 O HOH D 658 O HOH D 704 2.14
REMARK 500 OH TYR B 340 OE1 GLU D 138 2.15
REMARK 500 O HOH A 438 O HOH A 476 2.15
REMARK 500 OH TYR A 42 O HOH A 403 2.15
REMARK 500 OE1 GLN C 40 O HOH C 503 2.15
REMARK 500 NZ LYS A 341 OE2 GLU C 336 2.16
REMARK 500 O HOH D 688 O HOH D 709 2.17
REMARK 500 NE ARG D 298 O HOH D 504 2.18
REMARK 500 OE1 GLU B 138 OH TYR D 340 2.18
REMARK 500 O HOH C 602 O HOH C 662 2.18
REMARK 500 OG SER D 227 O HOH D 505 2.19
REMARK 500 O HOH B 498 O HOH B 561 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 608 O HOH D 679 2454 1.69
REMARK 500 O HOH C 652 O HOH C 654 10445 1.83
REMARK 500 O HOH B 481 O HOH D 686 6564 2.03
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO D 86 C - N - CA ANGL. DEV. = 9.8 DEGREES
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 TRP A 120 -6.98 67.49
REMARK 500 ASN A 183 66.72 -117.20
REMARK 500 SER A 190 -116.48 57.91
REMARK 500 TYR A 218 58.91 31.85
REMARK 500 TRP B 120 -5.53 68.40
REMARK 500 ASN B 183 64.55 -112.89
REMARK 500 SER B 190 -117.33 58.03
REMARK 500 TYR B 218 60.66 30.06
REMARK 500 LEU B 303 -8.58 82.32
REMARK 500 TRP C 120 -9.55 66.06
REMARK 500 ASN C 183 69.03 -119.04
REMARK 500 SER C 190 -116.42 57.75
REMARK 500 TYR C 218 59.06 31.78
REMARK 500 TRP D 120 -7.01 67.71
REMARK 500 ASN D 183 67.77 -118.15
REMARK 500 SER D 190 -116.13 58.06
REMARK 500 TYR D 218 60.44 29.87
REMARK 500 ASP D 287 120.35 -170.19
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 TRT C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRT D 401
DBREF 5MIF A 1 347 UNP D5GA36 D5GA36_TUBMM 1 347
DBREF 5MIF B 1 347 UNP D5GA36 D5GA36_TUBMM 1 347
DBREF 5MIF C 1 347 UNP D5GA36 D5GA36_TUBMM 1 347
DBREF 5MIF D 1 347 UNP D5GA36 D5GA36_TUBMM 1 347
SEQRES 1 A 347 MET ARG PHE THR ILE LEU SER VAL LEU ALA PHE SER LEU
SEQRES 2 A 347 PRO LEU VAL LEU ALA GLU THR PRO ALA PRO SER CYS PRO
SEQRES 3 A 347 VAL THR ASN VAL THR THR PRO GLN LEU ASP PRO ILE THR
SEQRES 4 A 347 GLN ALA TYR ALA ASP ALA ILE SER SER ARG PRO SER LEU
SEQRES 5 A 347 PHE ALA PHE PRO LEU PRO GLU ILE ARG ASP GLY TYR GLN
SEQRES 6 A 347 SER ASN VAL SER ASP PRO SER THR GLU PHE THR THR LYS
SEQRES 7 A 347 ILE LEU SER LEU PRO VAL GLY PRO THR GLY ASN VAL THR
SEQRES 8 A 347 ALA TYR LEU TYR LYS PRO VAL SER GLY GLU ARG GLU LYS
SEQRES 9 A 347 GLY LYS ASP LEU LEU PRO VAL ILE ALA TYR PHE HIS GLY
SEQRES 10 A 347 GLY GLY TRP VAL PHE GLY GLY PRO LYS SER TYR ARG GLY
SEQRES 11 A 347 LEU ILE THR ASN LEU ILE ARG GLU SER GLY ALA ALA VAL
SEQRES 12 A 347 PHE PHE VAL ASP TYR THR LEU THR PRO LYS VAL ALA TYR
SEQRES 13 A 347 PRO VAL PRO ASN GLU GLN CYS TYR ALA ALA VAL GLN TRP
SEQRES 14 A 347 LEU LEU GLU HIS GLY GLU LYS LEU GLY VAL ASP PRO THR
SEQRES 15 A 347 ASN MET GLY PHE GLY GLY ASP SER ALA GLY GLY GLU LEU
SEQRES 16 A 347 SER SER SER VAL SER LEU LEU SER ILE LYS ARG LYS THR
SEQRES 17 A 347 PRO LEU PRO LYS PHE GLN VAL LEU ILE TYR PRO ALA THR
SEQRES 18 A 347 ASP LEU ALA CYS GLU SER ALA THR PHE LYS GLU PHE PRO
SEQRES 19 A 347 ASN GLY PRO GLY LEU THR THR ASP GLU ILE ARG PHE ALA
SEQRES 20 A 347 ALA SER LEU PHE THR PRO ASP PRO LYS SER ARG LEU GLU
SEQRES 21 A 347 ASP VAL ALA SER PRO GLY ARG ALA SER ASP GLU ASP LEU
SEQRES 22 A 347 ALA LYS PHE PRO GLU THR LEU ILE VAL VAL ALA GLU VAL
SEQRES 23 A 347 ASP PRO ILE ARG GLN GLN GLY GLU ASP PHE GLY ARG ARG
SEQRES 24 A 347 LEU GLN LYS LEU GLY VAL ARG ALA ALA ILE ILE ARG VAL
SEQRES 25 A 347 LEU GLY THR ILE HIS GLY PHE ALA SER ILE ASP VAL LEU
SEQRES 26 A 347 SER GLU ALA PRO GLY ALA LYS ALA THR ILE GLU LEU ILE
SEQRES 27 A 347 GLY TYR LYS PHE LYS LYS ALA LEU HIS
SEQRES 1 B 347 MET ARG PHE THR ILE LEU SER VAL LEU ALA PHE SER LEU
SEQRES 2 B 347 PRO LEU VAL LEU ALA GLU THR PRO ALA PRO SER CYS PRO
SEQRES 3 B 347 VAL THR ASN VAL THR THR PRO GLN LEU ASP PRO ILE THR
SEQRES 4 B 347 GLN ALA TYR ALA ASP ALA ILE SER SER ARG PRO SER LEU
SEQRES 5 B 347 PHE ALA PHE PRO LEU PRO GLU ILE ARG ASP GLY TYR GLN
SEQRES 6 B 347 SER ASN VAL SER ASP PRO SER THR GLU PHE THR THR LYS
SEQRES 7 B 347 ILE LEU SER LEU PRO VAL GLY PRO THR GLY ASN VAL THR
SEQRES 8 B 347 ALA TYR LEU TYR LYS PRO VAL SER GLY GLU ARG GLU LYS
SEQRES 9 B 347 GLY LYS ASP LEU LEU PRO VAL ILE ALA TYR PHE HIS GLY
SEQRES 10 B 347 GLY GLY TRP VAL PHE GLY GLY PRO LYS SER TYR ARG GLY
SEQRES 11 B 347 LEU ILE THR ASN LEU ILE ARG GLU SER GLY ALA ALA VAL
SEQRES 12 B 347 PHE PHE VAL ASP TYR THR LEU THR PRO LYS VAL ALA TYR
SEQRES 13 B 347 PRO VAL PRO ASN GLU GLN CYS TYR ALA ALA VAL GLN TRP
SEQRES 14 B 347 LEU LEU GLU HIS GLY GLU LYS LEU GLY VAL ASP PRO THR
SEQRES 15 B 347 ASN MET GLY PHE GLY GLY ASP SER ALA GLY GLY GLU LEU
SEQRES 16 B 347 SER SER SER VAL SER LEU LEU SER ILE LYS ARG LYS THR
SEQRES 17 B 347 PRO LEU PRO LYS PHE GLN VAL LEU ILE TYR PRO ALA THR
SEQRES 18 B 347 ASP LEU ALA CYS GLU SER ALA THR PHE LYS GLU PHE PRO
SEQRES 19 B 347 ASN GLY PRO GLY LEU THR THR ASP GLU ILE ARG PHE ALA
SEQRES 20 B 347 ALA SER LEU PHE THR PRO ASP PRO LYS SER ARG LEU GLU
SEQRES 21 B 347 ASP VAL ALA SER PRO GLY ARG ALA SER ASP GLU ASP LEU
SEQRES 22 B 347 ALA LYS PHE PRO GLU THR LEU ILE VAL VAL ALA GLU VAL
SEQRES 23 B 347 ASP PRO ILE ARG GLN GLN GLY GLU ASP PHE GLY ARG ARG
SEQRES 24 B 347 LEU GLN LYS LEU GLY VAL ARG ALA ALA ILE ILE ARG VAL
SEQRES 25 B 347 LEU GLY THR ILE HIS GLY PHE ALA SER ILE ASP VAL LEU
SEQRES 26 B 347 SER GLU ALA PRO GLY ALA LYS ALA THR ILE GLU LEU ILE
SEQRES 27 B 347 GLY TYR LYS PHE LYS LYS ALA LEU HIS
SEQRES 1 C 347 MET ARG PHE THR ILE LEU SER VAL LEU ALA PHE SER LEU
SEQRES 2 C 347 PRO LEU VAL LEU ALA GLU THR PRO ALA PRO SER CYS PRO
SEQRES 3 C 347 VAL THR ASN VAL THR THR PRO GLN LEU ASP PRO ILE THR
SEQRES 4 C 347 GLN ALA TYR ALA ASP ALA ILE SER SER ARG PRO SER LEU
SEQRES 5 C 347 PHE ALA PHE PRO LEU PRO GLU ILE ARG ASP GLY TYR GLN
SEQRES 6 C 347 SER ASN VAL SER ASP PRO SER THR GLU PHE THR THR LYS
SEQRES 7 C 347 ILE LEU SER LEU PRO VAL GLY PRO THR GLY ASN VAL THR
SEQRES 8 C 347 ALA TYR LEU TYR LYS PRO VAL SER GLY GLU ARG GLU LYS
SEQRES 9 C 347 GLY LYS ASP LEU LEU PRO VAL ILE ALA TYR PHE HIS GLY
SEQRES 10 C 347 GLY GLY TRP VAL PHE GLY GLY PRO LYS SER TYR ARG GLY
SEQRES 11 C 347 LEU ILE THR ASN LEU ILE ARG GLU SER GLY ALA ALA VAL
SEQRES 12 C 347 PHE PHE VAL ASP TYR THR LEU THR PRO LYS VAL ALA TYR
SEQRES 13 C 347 PRO VAL PRO ASN GLU GLN CYS TYR ALA ALA VAL GLN TRP
SEQRES 14 C 347 LEU LEU GLU HIS GLY GLU LYS LEU GLY VAL ASP PRO THR
SEQRES 15 C 347 ASN MET GLY PHE GLY GLY ASP SER ALA GLY GLY GLU LEU
SEQRES 16 C 347 SER SER SER VAL SER LEU LEU SER ILE LYS ARG LYS THR
SEQRES 17 C 347 PRO LEU PRO LYS PHE GLN VAL LEU ILE TYR PRO ALA THR
SEQRES 18 C 347 ASP LEU ALA CYS GLU SER ALA THR PHE LYS GLU PHE PRO
SEQRES 19 C 347 ASN GLY PRO GLY LEU THR THR ASP GLU ILE ARG PHE ALA
SEQRES 20 C 347 ALA SER LEU PHE THR PRO ASP PRO LYS SER ARG LEU GLU
SEQRES 21 C 347 ASP VAL ALA SER PRO GLY ARG ALA SER ASP GLU ASP LEU
SEQRES 22 C 347 ALA LYS PHE PRO GLU THR LEU ILE VAL VAL ALA GLU VAL
SEQRES 23 C 347 ASP PRO ILE ARG GLN GLN GLY GLU ASP PHE GLY ARG ARG
SEQRES 24 C 347 LEU GLN LYS LEU GLY VAL ARG ALA ALA ILE ILE ARG VAL
SEQRES 25 C 347 LEU GLY THR ILE HIS GLY PHE ALA SER ILE ASP VAL LEU
SEQRES 26 C 347 SER GLU ALA PRO GLY ALA LYS ALA THR ILE GLU LEU ILE
SEQRES 27 C 347 GLY TYR LYS PHE LYS LYS ALA LEU HIS
SEQRES 1 D 347 MET ARG PHE THR ILE LEU SER VAL LEU ALA PHE SER LEU
SEQRES 2 D 347 PRO LEU VAL LEU ALA GLU THR PRO ALA PRO SER CYS PRO
SEQRES 3 D 347 VAL THR ASN VAL THR THR PRO GLN LEU ASP PRO ILE THR
SEQRES 4 D 347 GLN ALA TYR ALA ASP ALA ILE SER SER ARG PRO SER LEU
SEQRES 5 D 347 PHE ALA PHE PRO LEU PRO GLU ILE ARG ASP GLY TYR GLN
SEQRES 6 D 347 SER ASN VAL SER ASP PRO SER THR GLU PHE THR THR LYS
SEQRES 7 D 347 ILE LEU SER LEU PRO VAL GLY PRO THR GLY ASN VAL THR
SEQRES 8 D 347 ALA TYR LEU TYR LYS PRO VAL SER GLY GLU ARG GLU LYS
SEQRES 9 D 347 GLY LYS ASP LEU LEU PRO VAL ILE ALA TYR PHE HIS GLY
SEQRES 10 D 347 GLY GLY TRP VAL PHE GLY GLY PRO LYS SER TYR ARG GLY
SEQRES 11 D 347 LEU ILE THR ASN LEU ILE ARG GLU SER GLY ALA ALA VAL
SEQRES 12 D 347 PHE PHE VAL ASP TYR THR LEU THR PRO LYS VAL ALA TYR
SEQRES 13 D 347 PRO VAL PRO ASN GLU GLN CYS TYR ALA ALA VAL GLN TRP
SEQRES 14 D 347 LEU LEU GLU HIS GLY GLU LYS LEU GLY VAL ASP PRO THR
SEQRES 15 D 347 ASN MET GLY PHE GLY GLY ASP SER ALA GLY GLY GLU LEU
SEQRES 16 D 347 SER SER SER VAL SER LEU LEU SER ILE LYS ARG LYS THR
SEQRES 17 D 347 PRO LEU PRO LYS PHE GLN VAL LEU ILE TYR PRO ALA THR
SEQRES 18 D 347 ASP LEU ALA CYS GLU SER ALA THR PHE LYS GLU PHE PRO
SEQRES 19 D 347 ASN GLY PRO GLY LEU THR THR ASP GLU ILE ARG PHE ALA
SEQRES 20 D 347 ALA SER LEU PHE THR PRO ASP PRO LYS SER ARG LEU GLU
SEQRES 21 D 347 ASP VAL ALA SER PRO GLY ARG ALA SER ASP GLU ASP LEU
SEQRES 22 D 347 ALA LYS PHE PRO GLU THR LEU ILE VAL VAL ALA GLU VAL
SEQRES 23 D 347 ASP PRO ILE ARG GLN GLN GLY GLU ASP PHE GLY ARG ARG
SEQRES 24 D 347 LEU GLN LYS LEU GLY VAL ARG ALA ALA ILE ILE ARG VAL
SEQRES 25 D 347 LEU GLY THR ILE HIS GLY PHE ALA SER ILE ASP VAL LEU
SEQRES 26 D 347 SER GLU ALA PRO GLY ALA LYS ALA THR ILE GLU LEU ILE
SEQRES 27 D 347 GLY TYR LYS PHE LYS LYS ALA LEU HIS
HET TRT C 401 25
HET TRT D 401 25
HETNAM TRT FRAGMENT OF TRITON X-100
HETSYN TRT 1-{2-[2-(2-METHOXYETHOXY)ETHOXY]ETHOXY}-4-(1,1,3,3-
HETSYN 2 TRT TETRAMETHYLBUTYL)BENZENE
FORMUL 5 TRT 2(C21 H36 O4)
FORMUL 7 HOH *692(H2 O)
HELIX 1 AA1 ASP A 36 SER A 48 1 13
HELIX 2 AA2 TYR A 128 GLY A 140 1 13
HELIX 3 AA3 PRO A 157 GLY A 174 1 18
HELIX 4 AA4 GLU A 175 LEU A 177 5 3
HELIX 5 AA5 SER A 190 LYS A 207 1 18
HELIX 6 AA6 SER A 227 PHE A 233 1 7
HELIX 7 AA7 THR A 240 THR A 252 1 13
HELIX 8 AA8 ASP A 254 GLU A 260 5 7
HELIX 9 AA9 SER A 264 ALA A 268 5 5
HELIX 10 AB1 SER A 269 ALA A 274 1 6
HELIX 11 AB2 ILE A 289 LEU A 303 1 15
HELIX 12 AB3 ILE A 322 GLU A 327 1 6
HELIX 13 AB4 ALA A 328 LEU A 346 1 19
HELIX 14 AB5 ASP B 36 SER B 47 1 12
HELIX 15 AB6 TYR B 128 GLY B 140 1 13
HELIX 16 AB7 PRO B 157 GLY B 174 1 18
HELIX 17 AB8 GLU B 175 LEU B 177 5 3
HELIX 18 AB9 SER B 190 ARG B 206 1 17
HELIX 19 AC1 SER B 227 PHE B 233 1 7
HELIX 20 AC2 THR B 240 THR B 252 1 13
HELIX 21 AC3 ASP B 254 GLU B 260 5 7
HELIX 22 AC4 SER B 264 ALA B 268 5 5
HELIX 23 AC5 SER B 269 ALA B 274 1 6
HELIX 24 AC6 ILE B 289 LYS B 302 1 14
HELIX 25 AC7 ILE B 322 GLU B 327 1 6
HELIX 26 AC8 ALA B 328 LEU B 346 1 19
HELIX 27 AC9 ASP C 36 SER C 47 1 12
HELIX 28 AD1 TYR C 128 GLY C 140 1 13
HELIX 29 AD2 PRO C 157 GLY C 174 1 18
HELIX 30 AD3 GLU C 175 LEU C 177 5 3
HELIX 31 AD4 SER C 190 ARG C 206 1 17
HELIX 32 AD5 SER C 227 PHE C 233 1 7
HELIX 33 AD6 THR C 240 THR C 252 1 13
HELIX 34 AD7 LYS C 256 GLU C 260 5 5
HELIX 35 AD8 SER C 264 ALA C 268 5 5
HELIX 36 AD9 SER C 269 ALA C 274 1 6
HELIX 37 AE1 ILE C 289 LEU C 303 1 15
HELIX 38 AE2 VAL C 324 GLU C 327 5 4
HELIX 39 AE3 ALA C 328 LEU C 346 1 19
HELIX 40 AE4 ASP D 36 ILE D 46 1 11
HELIX 41 AE5 TYR D 128 GLY D 140 1 13
HELIX 42 AE6 PRO D 157 GLY D 174 1 18
HELIX 43 AE7 GLU D 175 LEU D 177 5 3
HELIX 44 AE8 SER D 190 LYS D 207 1 18
HELIX 45 AE9 SER D 227 PHE D 233 1 7
HELIX 46 AF1 THR D 240 THR D 252 1 13
HELIX 47 AF2 ASP D 254 GLU D 260 5 7
HELIX 48 AF3 SER D 264 ALA D 268 5 5
HELIX 49 AF4 SER D 269 ALA D 274 1 6
HELIX 50 AF5 ILE D 289 LEU D 303 1 15
HELIX 51 AF6 ILE D 322 GLU D 327 1 6
HELIX 52 AF7 ALA D 328 LEU D 346 1 19
SHEET 1 AA116 PHE A 75 LEU A 82 0
SHEET 2 AA116 VAL A 90 PRO A 97 -1 O ALA A 92 N LEU A 80
SHEET 3 AA116 ALA A 142 ASP A 147 -1 O VAL A 143 N TYR A 95
SHEET 4 AA116 LEU A 109 PHE A 115 1 N ILE A 112 O PHE A 144
SHEET 5 AA116 VAL A 179 ASP A 189 1 O GLY A 185 N ALA A 113
SHEET 6 AA116 PHE A 213 ILE A 217 1 O VAL A 215 N PHE A 186
SHEET 7 AA116 THR A 279 VAL A 286 1 O LEU A 280 N GLN A 214
SHEET 8 AA116 ALA A 307 ILE A 316 1 O ALA A 308 N ILE A 281
SHEET 9 AA116 ALA C 307 ILE C 316 -1 O ILE C 309 N LEU A 313
SHEET 10 AA116 GLU C 278 VAL C 286 1 N ILE C 281 O ALA C 308
SHEET 11 AA116 PHE C 213 ILE C 217 1 N GLN C 214 O LEU C 280
SHEET 12 AA116 VAL C 179 ASP C 189 1 N PHE C 186 O VAL C 215
SHEET 13 AA116 LEU C 109 PHE C 115 1 N LEU C 109 O ASP C 180
SHEET 14 AA116 ALA C 142 ASP C 147 1 O PHE C 144 N ILE C 112
SHEET 15 AA116 VAL C 90 PRO C 97 -1 N TYR C 93 O PHE C 145
SHEET 16 AA116 PHE C 75 LEU C 82 -1 N LEU C 80 O ALA C 92
SHEET 1 AA216 PHE B 75 LEU B 82 0
SHEET 2 AA216 VAL B 90 PRO B 97 -1 O ALA B 92 N LEU B 80
SHEET 3 AA216 ALA B 142 ASP B 147 -1 O VAL B 143 N TYR B 95
SHEET 4 AA216 LEU B 109 PHE B 115 1 N PRO B 110 O ALA B 142
SHEET 5 AA216 VAL B 179 ASP B 189 1 O GLY B 185 N ALA B 113
SHEET 6 AA216 PHE B 213 ILE B 217 1 O ILE B 217 N GLY B 188
SHEET 7 AA216 GLU B 278 VAL B 286 1 O LEU B 280 N GLN B 214
SHEET 8 AA216 ALA B 307 ILE B 316 1 O ALA B 308 N ILE B 281
SHEET 9 AA216 ALA D 307 ILE D 316 -1 O ARG D 311 N ARG B 311
SHEET 10 AA216 THR D 279 VAL D 286 1 N ILE D 281 O ALA D 308
SHEET 11 AA216 PHE D 213 ILE D 217 1 N GLN D 214 O LEU D 280
SHEET 12 AA216 VAL D 179 ASP D 189 1 N PHE D 186 O VAL D 215
SHEET 13 AA216 LEU D 109 PHE D 115 1 N ALA D 113 O GLY D 185
SHEET 14 AA216 ALA D 142 ASP D 147 1 O ALA D 142 N ILE D 112
SHEET 15 AA216 VAL D 90 PRO D 97 -1 N TYR D 93 O PHE D 145
SHEET 16 AA216 PHE D 75 LEU D 82 -1 N LEU D 80 O ALA D 92
CISPEP 1 PHE A 55 PRO A 56 0 -2.70
CISPEP 2 THR A 151 PRO A 152 0 -0.76
CISPEP 3 TYR A 156 PRO A 157 0 1.16
CISPEP 4 PHE B 55 PRO B 56 0 -2.84
CISPEP 5 THR B 151 PRO B 152 0 -0.37
CISPEP 6 TYR B 156 PRO B 157 0 1.35
CISPEP 7 PHE C 55 PRO C 56 0 -2.97
CISPEP 8 THR C 151 PRO C 152 0 -2.36
CISPEP 9 TYR C 156 PRO C 157 0 0.70
CISPEP 10 PHE D 55 PRO D 56 0 -1.16
CISPEP 11 THR D 151 PRO D 152 0 -1.44
CISPEP 12 TYR D 156 PRO D 157 0 1.45
SITE 1 AC1 13 GLY C 118 GLY C 119 TRP C 120 PHE C 122
SITE 2 AC1 13 TYR C 128 SER C 190 ALA C 191 ALA C 220
SITE 3 AC1 13 LEU C 239 ILE C 244 ALA C 247 ILE C 289
SITE 4 AC1 13 SER C 321
SITE 1 AC2 14 LEU D 52 PHE D 53 GLY D 118 GLY D 119
SITE 2 AC2 14 TRP D 120 SER D 127 TYR D 128 SER D 190
SITE 3 AC2 14 ALA D 191 LEU D 239 GLU D 243 ALA D 247
SITE 4 AC2 14 HOH D 512 HOH D 594
CRYST1 158.898 158.898 226.809 90.00 90.00 120.00 P 65 2 2 48
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 0.006293 0.003633 0.000000 0.00000
SCALE2 0.000000 0.007267 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004409 0.00000
TER 2311 HIS A 347
TER 4622 HIS B 347
TER 6926 HIS C 347
TER 9231 HIS D 347
MASTER 599 0 2 52 32 0 8 6 9969 4 50 108
END |