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HEADER HYDROLASE 07-AUG-18 6ECC
TITLE VLM2 THIOESTERASE DOMAIN WILD TYPE STRUCTURE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VLM2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN (UNP RESIDUES 2368-2655);
COMPND 5 EC: 3.1.2.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES TSUSIMAENSIS;
SOURCE 3 ORGANISM_TAXID: 285482;
SOURCE 4 ATCC: 15141;
SOURCE 5 GENE: VLM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS THIOESTERASE, THIOESTERASE DOMAIN, NRPS, NON-RIBOSOMAL PEPTIDE
KEYWDS 2 SYNTHETASE, NONRIBOSOMAL PEPTIDE SYNTHETASE, VALINOMYCIN, HYDROLASE,
KEYWDS 3 DEPSIPEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.ALONZO,T.M.SCHMEING
REVDAT 1 12-DEC-18 6ECC 0
JRNL AUTH N.HUGUENIN-DEZOT,D.A.ALONZO,G.W.HEBERLIG,M.MAHESH,
JRNL AUTH 2 D.P.NGUYEN,M.H.DORNAN,C.N.BODDY,T.M.SCHMEING,J.W.CHIN
JRNL TITL TRAPPING BIOSYNTHETIC ACYL-ENZYME INTERMEDIATES WITH ENCODED
JRNL TITL 2 2,3--DIAMINOPROPIONIC ACID.
JRNL REF NATURE 2018
JRNL REFN ESSN 1476-4687
JRNL DOI 10.1038/S41586-018-0781-Z
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 55838
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.540
REMARK 3 FREE R VALUE TEST SET COUNT : 3093
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 87.9800 - 5.0400 1.00 2689 157 0.2218 0.2142
REMARK 3 2 5.0400 - 4.0000 1.00 2501 146 0.1441 0.1673
REMARK 3 3 4.0000 - 3.5000 1.00 2487 146 0.1479 0.1566
REMARK 3 4 3.5000 - 3.1800 1.00 2438 143 0.1612 0.1866
REMARK 3 5 3.1800 - 2.9500 1.00 2430 143 0.1679 0.1966
REMARK 3 6 2.9500 - 2.7800 1.00 2428 141 0.1890 0.1844
REMARK 3 7 2.7800 - 2.6400 1.00 2407 141 0.1828 0.2065
REMARK 3 8 2.6400 - 2.5200 1.00 2411 141 0.1734 0.1939
REMARK 3 9 2.5200 - 2.4200 1.00 2390 140 0.1674 0.1694
REMARK 3 10 2.4200 - 2.3400 1.00 2398 140 0.1574 0.2010
REMARK 3 11 2.3400 - 2.2700 1.00 2387 140 0.1567 0.1493
REMARK 3 12 2.2700 - 2.2000 1.00 2396 141 0.1514 0.1845
REMARK 3 13 2.2000 - 2.1500 1.00 2390 139 0.1595 0.1747
REMARK 3 14 2.1500 - 2.0900 1.00 2367 139 0.1665 0.1716
REMARK 3 15 2.0900 - 2.0500 1.00 2389 139 0.1671 0.1830
REMARK 3 16 2.0500 - 2.0000 1.00 2375 139 0.1737 0.2027
REMARK 3 17 2.0000 - 1.9600 1.00 2373 139 0.1847 0.2096
REMARK 3 18 1.9600 - 1.9200 1.00 2336 136 0.2142 0.2171
REMARK 3 19 1.9200 - 1.8900 0.99 2364 139 0.2304 0.2544
REMARK 3 20 1.8900 - 1.8600 0.98 2310 136 0.2496 0.2590
REMARK 3 21 1.8600 - 1.8300 0.95 2280 136 0.2815 0.2727
REMARK 3 22 1.8300 - 1.8000 0.93 2199 132 0.3290 0.3374
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) : 0.197
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.31
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.37
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 : 0.019 1791
REMARK 3 ANGLE : 1.476 2438
REMARK 3 CHIRALITY : 0.095 271
REMARK 3 PLANARITY : 0.012 322
REMARK 3 DIHEDRAL : 13.338 1060
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 352.4867 131.9267 382.0087
REMARK 3 T TENSOR
REMARK 3 T11: 0.1688 T22: 0.1877
REMARK 3 T33: 0.2397 T12: -0.0438
REMARK 3 T13: 0.0088 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.2662 L22: 1.1111
REMARK 3 L33: 1.3076 L12: 0.1956
REMARK 3 L13: 0.0928 L23: -0.0736
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: -0.0004 S13: -0.0492
REMARK 3 S21: 0.0806 S22: 0.0245 S23: 0.1650
REMARK 3 S31: 0.0049 S32: -0.0437 S33: 0.0000
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 6ECC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1000236060.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55855
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 152.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 6ECB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.65 M DL-MALIC ACID, PH 8.1, 25 MM
REMARK 280 HEPES, PH 8.0, 100 MM SODIUM CHLORIDE, 0.2 MM TCEP, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-X
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 2353
REMARK 465 HIS A 2354
REMARK 465 HIS A 2355
REMARK 465 HIS A 2356
REMARK 465 HIS A 2357
REMARK 465 HIS A 2358
REMARK 465 HIS A 2359
REMARK 465 HIS A 2360
REMARK 465 HIS A 2361
REMARK 465 GLU A 2362
REMARK 465 ASN A 2363
REMARK 465 LEU A 2364
REMARK 465 TYR A 2365
REMARK 465 PHE A 2366
REMARK 465 GLN A 2367
REMARK 465 GLY A 2368
REMARK 465 GLY A 2369
REMARK 465 SER A 2370
REMARK 465 SER A 2371
REMARK 465 THR A 2372
REMARK 465 ALA A 2373
REMARK 465 GLY A 2374
REMARK 465 ALA A 2429
REMARK 465 GLY A 2430
REMARK 465 VAL A 2500
REMARK 465 ALA A 2501
REMARK 465 ASP A 2502
REMARK 465 ALA A 2503
REMARK 465 ASP A 2504
REMARK 465 LEU A 2505
REMARK 465 THR A 2506
REMARK 465 GLU A 2507
REMARK 465 GLU A 2508
REMARK 465 GLU A 2509
REMARK 465 THR A 2510
REMARK 465 LYS A 2511
REMARK 465 VAL A 2512
REMARK 465 PHE A 2513
REMARK 465 ILE A 2514
REMARK 465 LEU A 2515
REMARK 465 ALA A 2516
REMARK 465 MET A 2517
REMARK 465 GLY A 2518
REMARK 465 ILE A 2519
REMARK 465 GLY A 2520
REMARK 465 GLY A 2521
REMARK 465 MET A 2522
REMARK 465 LEU A 2523
REMARK 465 ASP A 2524
REMARK 465 GLN A 2525
REMARK 465 ASP A 2526
REMARK 465 ARG A 2527
REMARK 465 ASP A 2528
REMARK 465 ALA A 2529
REMARK 465 LEU A 2530
REMARK 465 LYS A 2531
REMARK 465 ASP A 2532
REMARK 465 LEU A 2533
REMARK 465 PRO A 2534
REMARK 465 TYR A 2535
REMARK 465 GLU A 2536
REMARK 465 GLU A 2537
REMARK 465 ALA A 2538
REMARK 465 LYS A 2539
REMARK 465 PRO A 2648
REMARK 465 SER A 2649
REMARK 465 ASP A 2650
REMARK 465 ASP A 2651
REMARK 465 GLY A 2652
REMARK 465 PRO A 2653
REMARK 465 ARG A 2654
REMARK 465 GLY A 2655
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 ASP A2375 CG OD1 OD2
REMARK 470 ARG A2386 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2439 CG CD OE1 OE2
REMARK 470 LEU A2541 CG CD1 CD2
REMARK 470 LYS A2547 CG CD CE NZ
REMARK 470 LEU A2556 CG CD1 CD2
REMARK 470 GLU A2558 CD OE1 OE2
REMARK 470 ARG A2576 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2615 CG CD OE1 OE2
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 ARG A2494 NE - CZ - NH1 ANGL. DEV. = 3.3 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 SER A2463 -132.88 53.41
REMARK 500 ASP A2549 89.45 -152.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ECB RELATED DB: PDB
REMARK 900 RELATED ID: 6ECD RELATED DB: PDB
REMARK 900 RELATED ID: 6ECE RELATED DB: PDB
REMARK 900 RELATED ID: 6ECF RELATED DB: PDB
DBREF 6ECC A 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
SEQADV 6ECC MET A 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC HIS A 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC GLU A 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC ASN A 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC LEU A 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC TYR A 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC PHE A 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECC GLN A 2367 UNP Q1PSF3 EXPRESSION TAG
SEQRES 1 A 303 MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR
SEQRES 2 A 303 PHE GLN GLY GLY SER SER THR ALA GLY ASP PRO THR ALA
SEQRES 3 A 303 LYS LEU VAL ARG LEU ASN PRO ARG GLY GLY ASP GLY PRO
SEQRES 4 A 303 GLY ILE VAL PHE ALA PRO PRO ALA GLY GLY THR VAL LEU
SEQRES 5 A 303 GLY TYR ILE GLU LEU ALA ARG HIS LEU LYS GLY PHE GLY
SEQRES 6 A 303 GLU ILE HIS GLY VAL GLU ALA PRO GLY LEU GLY ALA GLY
SEQRES 7 A 303 GLU THR PRO VAL TYR PRO SER PHE GLU GLU MET VAL GLN
SEQRES 8 A 303 PHE CYS SER ASP SER ALA ALA GLY VAL ALA GLY ASP GLY
SEQRES 9 A 303 VAL TYR ILE GLY GLY HIS SER LEU GLY GLY HIS ILE ALA
SEQRES 10 A 303 PHE TYR LEU ALA THR MET LEU LEU ASP ARG GLY ILE ARG
SEQRES 11 A 303 PRO LYS GLY LEU ILE ILE LEU ASP THR PRO PRO ARG LEU
SEQRES 12 A 303 GLY ASP ILE PRO VAL ALA ASP ALA ASP LEU THR GLU GLU
SEQRES 13 A 303 GLU THR LYS VAL PHE ILE LEU ALA MET GLY ILE GLY GLY
SEQRES 14 A 303 MET LEU ASP GLN ASP ARG ASP ALA LEU LYS ASP LEU PRO
SEQRES 15 A 303 TYR GLU GLU ALA LYS GLN LEU LEU LEU ASP ARG ALA LYS
SEQRES 16 A 303 ASN ASP PRO ARG VAL SER ALA PHE LEU SER GLU ASP TYR
SEQRES 17 A 303 LEU ASP ARG PHE LEU ARG LEU GLN MET HIS GLN LEU MET
SEQRES 18 A 303 TYR SER ARG ASP VAL VAL LEU PRO GLN ARG LYS LEU ASP
SEQRES 19 A 303 ILE PRO ILE HIS VAL PHE ARG THR LYS ASN HIS ALA PRO
SEQRES 20 A 303 GLU VAL ALA ARG LEU PHE SER ALA TRP GLU ASN TYR ALA
SEQRES 21 A 303 ALA GLY GLU VAL THR PHE VAL ASP ILE PRO GLY ASP HIS
SEQRES 22 A 303 ALA THR MET LEU ARG ALA PRO HIS VAL SER GLU VAL ALA
SEQRES 23 A 303 GLN LEU LEU ASP ARG HIS CYS GLY LEU PRO SER ASP ASP
SEQRES 24 A 303 GLY PRO ARG GLY
FORMUL 2 HOH *171(H2 O)
HELIX 1 AA1 VAL A 2403 GLY A 2405 5 3
HELIX 2 AA2 TYR A 2406 LEU A 2413 1 8
HELIX 3 AA3 SER A 2437 ALA A 2450 1 14
HELIX 4 AA4 SER A 2463 ARG A 2479 1 17
HELIX 5 AA5 ARG A 2494 ILE A 2498 5 5
HELIX 6 AA6 LEU A 2541 ASP A 2549 1 9
HELIX 7 AA7 ASP A 2549 ALA A 2554 1 6
HELIX 8 AA8 SER A 2557 MET A 2573 1 17
HELIX 9 AA9 SER A 2575 LEU A 2580 1 6
HELIX 10 AB1 ALA A 2598 ARG A 2603 1 6
HELIX 11 AB2 LEU A 2604 ALA A 2612 5 9
HELIX 12 AB3 ALA A 2626 ARG A 2630 5 5
HELIX 13 AB4 PRO A 2632 GLY A 2646 1 15
SHEET 1 AA1 7 LYS A2379 ARG A2382 0
SHEET 2 AA1 7 ILE A2419 GLU A2423 -1 O GLU A2423 N LYS A2379
SHEET 3 AA1 7 GLY A2392 PHE A2395 1 N ILE A2393 O HIS A2420
SHEET 4 AA1 7 VAL A2457 HIS A2462 1 O TYR A2458 N GLY A2392
SHEET 5 AA1 7 GLY A2485 LEU A2489 1 O ILE A2487 N ILE A2459
SHEET 6 AA1 7 ILE A2589 ARG A2593 1 O HIS A2590 N LEU A2486
SHEET 7 AA1 7 VAL A2616 ASP A2620 1 O THR A2617 N VAL A2591
CISPEP 1 ALA A 2631 PRO A 2632 0 1.94
CRYST1 152.202 152.202 152.202 90.00 90.00 90.00 P 4 3 2 24
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 0.006570 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006570 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006570 0.00000
TER 3461 LEU A2647
MASTER 447 0 0 13 7 0 0 6 1913 1 0 24
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