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HEADER HYDROLASE 07-AUG-18 6ECB
TITLE VLM2 THIOESTERASE DOMAIN WILD TYPE STRUCTURE 1
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 6ECB 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. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 64287
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.540
REMARK 3 FREE R VALUE TEST SET COUNT : 3561
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 87.5300 - 4.9700 1.00 2761 161 0.2098 0.2160
REMARK 3 2 4.9700 - 3.9500 1.00 2578 151 0.1395 0.1547
REMARK 3 3 3.9500 - 3.4500 1.00 2536 148 0.1485 0.1698
REMARK 3 4 3.4500 - 3.1300 1.00 2521 148 0.1614 0.1759
REMARK 3 5 3.1300 - 2.9100 1.00 2495 146 0.1761 0.2022
REMARK 3 6 2.9100 - 2.7400 1.00 2492 146 0.1777 0.1960
REMARK 3 7 2.7400 - 2.6000 1.00 2478 145 0.1766 0.2024
REMARK 3 8 2.6000 - 2.4900 1.00 2474 144 0.1700 0.1752
REMARK 3 9 2.4900 - 2.3900 1.00 2464 145 0.1624 0.1644
REMARK 3 10 2.3900 - 2.3100 1.00 2467 144 0.1559 0.1805
REMARK 3 11 2.3100 - 2.2400 1.00 2450 143 0.1488 0.1635
REMARK 3 12 2.2400 - 2.1700 1.00 2460 144 0.1494 0.1628
REMARK 3 13 2.1700 - 2.1100 1.00 2437 143 0.1574 0.1646
REMARK 3 14 2.1100 - 2.0600 1.00 2449 144 0.1604 0.1728
REMARK 3 15 2.0600 - 2.0200 1.00 2427 143 0.1615 0.1683
REMARK 3 16 2.0200 - 1.9700 1.00 2459 143 0.1633 0.1839
REMARK 3 17 1.9700 - 1.9300 1.00 2440 143 0.1679 0.1810
REMARK 3 18 1.9300 - 1.9000 1.00 2429 141 0.1869 0.2021
REMARK 3 19 1.9000 - 1.8600 1.00 2418 142 0.1953 0.2091
REMARK 3 20 1.8600 - 1.8300 1.00 2427 143 0.2062 0.2070
REMARK 3 21 1.8300 - 1.8000 0.97 2348 138 0.2243 0.2646
REMARK 3 22 1.8000 - 1.7700 0.92 2252 132 0.2610 0.2539
REMARK 3 23 1.7700 - 1.7500 0.90 2204 130 0.2575 0.2941
REMARK 3 24 1.7500 - 1.7200 0.89 2146 129 0.2936 0.3331
REMARK 3 25 1.7200 - 1.7000 0.88 2114 125 0.3265 0.3568
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.483
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.31
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 : 0.009 2032
REMARK 3 ANGLE : 1.011 2761
REMARK 3 CHIRALITY : 0.059 307
REMARK 3 PLANARITY : 0.007 364
REMARK 3 DIHEDRAL : 11.863 1210
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): 347.8551 132.1259 378.9590
REMARK 3 T TENSOR
REMARK 3 T11: 0.1502 T22: 0.1585
REMARK 3 T33: 0.2124 T12: -0.0385
REMARK 3 T13: -0.0070 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.7821 L22: 1.4231
REMARK 3 L33: 1.3289 L12: 0.1806
REMARK 3 L13: -0.0739 L23: -0.0351
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: 0.0681 S13: 0.0339
REMARK 3 S21: -0.0236 S22: 0.0057 S23: 0.2542
REMARK 3 S31: -0.0135 S32: -0.0533 S33: -0.0153
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 6ECB 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_1000236029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
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) : 0.9794
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 : 64289
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 151.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
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 2VSQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.65 M DL-MALIC ACID, PH 9.5, 25 MM
REMARK 280 HEPES, PH 8.0, 100 MM SODIUM CHLORIDE, 0.2 MM TCEP, VAPOR
REMARK 280 DIFFUSION, SITTING 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: 11650 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 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 A2838 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 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 ARG A 2386
REMARK 465 GLY A 2387
REMARK 465 PRO A 2499
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 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 GLU A2439 CG CD OE1 OE2
REMARK 470 ILE A2498 CG1 CG2 CD1
REMARK 470 GLU A2508 CG CD OE1 OE2
REMARK 470 GLU A2509 CG CD OE1 OE2
REMARK 470 THR A2510 OG1 CG2
REMARK 470 LYS A2511 CG CD CE NZ
REMARK 470 ASP A2532 CG OD1 OD2
REMARK 470 GLU A2536 CG 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: 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 PRO A2398 -169.85 -78.10
REMARK 500 SER A2463 -134.98 55.79
REMARK 500 ASP A2532 21.47 -76.37
REMARK 500 ASP A2586 32.98 -95.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2904 DISTANCE = 6.16 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ECC 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 6ECB A 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
SEQADV 6ECB MET A 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB HIS A 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB GLU A 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB ASN A 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB LEU A 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB TYR A 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB PHE A 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECB 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 *204(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 GLU A 2509 GLY A 2518 1 10
HELIX 6 AA6 GLY A 2518 LEU A 2523 1 6
HELIX 7 AA7 ASP A 2526 ASP A 2532 1 7
HELIX 8 AA8 PRO A 2534 LYS A 2547 1 14
HELIX 9 AA9 SER A 2557 MET A 2573 1 17
HELIX 10 AB1 SER A 2575 LEU A 2580 1 6
HELIX 11 AB2 ALA A 2598 ARG A 2603 1 6
HELIX 12 AB3 LEU A 2604 ALA A 2612 5 9
HELIX 13 AB4 ALA A 2626 ARG A 2630 5 5
HELIX 14 AB5 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 GLY A2421 N VAL A2381
SHEET 3 AA1 7 GLY A2392 ALA A2396 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 LEU A2486 LEU A2489 1 O ILE A2487 N ILE A2459
SHEET 6 AA1 7 ILE A2589 ARG A2593 1 O PHE A2592 N ILE A2488
SHEET 7 AA1 7 VAL A2616 ASP A2620 1 O THR A2617 N VAL A2591
CISPEP 1 ALA A 2631 PRO A 2632 0 2.06
CRYST1 151.399 151.399 151.399 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 0.006605 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006605 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006605 0.00000
TER 3939 PRO A2648
MASTER 424 0 0 14 7 0 0 6 2185 1 0 24
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