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HEADER HYDROLASE 07-AUG-18 6ECE
TITLE VLM2 THIOESTERASE DOMAIN WITH GENETICALLY ENCODED 2,3-DIAMINOPROPIONIC
TITLE 2 ACID BOUND WITH A DODECADEPSIPEPTIDE, SPACE GROUP H3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VLM2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN (UNP RESIDUES 2368-2655);
COMPND 5 EC: 3.1.2.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DODECADEPSIPEPTIDE;
COMPND 9 CHAIN: C, D;
COMPND 10 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;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS THIOESTERASE, THIOESTERASE DOMAIN, NRPS, NON-RIBOSOMAL PEPTIDE
KEYWDS 2 SYNTHETASE, NONRIBOSOMAL PEPTIDE SYNTHETASE, VALINOMYCIN, HYDROLASE,
KEYWDS 3 DEPSIPEPTIDE, UNNATURAL AMINO ACID, 2, 3-DIAMINOPROPIONIC ACID
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.ALONZO,N.HUGUENIN-DEZOT,G.W.HEBERLIG,M.MAHESH,D.P.NGUYEN,
AUTHOR 2 M.H.DORNAN,C.N.BODDY,J.W.CHIN,T.M.SCHMEING
REVDAT 1 12-DEC-18 6ECE 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.090
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1784
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 64.6300 - 4.7000 1.00 2617 139 0.1924 0.2431
REMARK 3 2 4.7000 - 3.7300 1.00 2594 137 0.1703 0.1902
REMARK 3 3 3.7300 - 3.2600 1.00 2605 137 0.1870 0.2265
REMARK 3 4 3.2600 - 2.9600 1.00 2605 137 0.2130 0.2399
REMARK 3 5 2.9600 - 2.7500 1.00 2612 137 0.2297 0.2565
REMARK 3 6 2.7500 - 2.5900 1.00 2580 136 0.2302 0.2718
REMARK 3 7 2.5900 - 2.4600 1.00 2639 139 0.2330 0.2789
REMARK 3 8 2.4600 - 2.3500 1.00 2610 137 0.2409 0.2647
REMARK 3 9 2.3500 - 2.2600 1.00 2587 136 0.2383 0.2866
REMARK 3 10 2.2600 - 2.1800 1.00 2620 141 0.2659 0.2855
REMARK 3 11 2.1800 - 2.1100 1.00 2610 135 0.2866 0.3149
REMARK 3 12 2.1100 - 2.0500 1.00 2588 136 0.3009 0.3314
REMARK 3 13 2.0500 - 2.0000 1.00 2627 137 0.3361 0.3341
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) : 0.272
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.854
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.50
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 3741
REMARK 3 ANGLE : 0.527 5097
REMARK 3 CHIRALITY : 0.040 581
REMARK 3 PLANARITY : 0.003 664
REMARK 3 DIHEDRAL : 10.007 2192
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): 15.5882 -22.9007 -2.6963
REMARK 3 T TENSOR
REMARK 3 T11: 0.1840 T22: 0.2595
REMARK 3 T33: 0.2233 T12: 0.0188
REMARK 3 T13: 0.0167 T23: 0.0594
REMARK 3 L TENSOR
REMARK 3 L11: -0.0874 L22: 0.2111
REMARK 3 L33: 0.0606 L12: -0.0063
REMARK 3 L13: 0.1294 L23: -0.1749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: -0.0027 S13: -0.0094
REMARK 3 S21: -0.0105 S22: -0.0833 S23: -0.0665
REMARK 3 S31: -0.0174 S32: -0.0273 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 6ECE 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_1000236069.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-18
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 : 35685
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 64.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
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 (%): 39.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 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: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.78550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.39282
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 78.38367
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 38.78550
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 22.39282
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 78.38367
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 38.78550
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 22.39282
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.38367
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.78564
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 156.76733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 44.78564
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 156.76733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 44.78564
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 156.76733
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 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 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 A2702 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2749 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2705 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 ASP A 2375
REMARK 465 GLY A 2496
REMARK 465 ASP A 2497
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 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 465 MET B 2353
REMARK 465 HIS B 2354
REMARK 465 HIS B 2355
REMARK 465 HIS B 2356
REMARK 465 HIS B 2357
REMARK 465 HIS B 2358
REMARK 465 HIS B 2359
REMARK 465 HIS B 2360
REMARK 465 HIS B 2361
REMARK 465 GLU B 2362
REMARK 465 ASN B 2363
REMARK 465 LEU B 2364
REMARK 465 TYR B 2365
REMARK 465 PHE B 2366
REMARK 465 GLN B 2367
REMARK 465 GLY B 2368
REMARK 465 GLY B 2369
REMARK 465 SER B 2370
REMARK 465 SER B 2371
REMARK 465 THR B 2372
REMARK 465 ALA B 2373
REMARK 465 GLY B 2374
REMARK 465 ASP B 2375
REMARK 465 PRO B 2376
REMARK 465 THR B 2377
REMARK 465 ALA B 2378
REMARK 465 PRO B 2385
REMARK 465 ARG B 2386
REMARK 465 GLY B 2387
REMARK 465 GLY B 2388
REMARK 465 ASP B 2389
REMARK 465 GLY B 2496
REMARK 465 ASP B 2497
REMARK 465 ILE B 2498
REMARK 465 PRO B 2499
REMARK 465 VAL B 2500
REMARK 465 ALA B 2501
REMARK 465 ASP B 2502
REMARK 465 ALA B 2503
REMARK 465 ASP B 2504
REMARK 465 LEU B 2505
REMARK 465 GLY B 2518
REMARK 465 ILE B 2519
REMARK 465 GLY B 2520
REMARK 465 GLY B 2521
REMARK 465 MET B 2522
REMARK 465 LEU B 2523
REMARK 465 ASP B 2524
REMARK 465 GLN B 2525
REMARK 465 ASP B 2526
REMARK 465 ARG B 2527
REMARK 465 ASP B 2528
REMARK 465 ALA B 2529
REMARK 465 LEU B 2530
REMARK 465 LYS B 2531
REMARK 465 ASP B 2532
REMARK 465 LEU B 2533
REMARK 465 LEU B 2647
REMARK 465 PRO B 2648
REMARK 465 SER B 2649
REMARK 465 ASP B 2650
REMARK 465 ASP B 2651
REMARK 465 GLY B 2652
REMARK 465 PRO B 2653
REMARK 465 ARG B 2654
REMARK 465 GLY B 2655
REMARK 465 VAD C 3009
REMARK 465 VAD C 3013
REMARK 465 DVA C 3014
REMARK 465 2OP C 3015
REMARK 465 VAL C 3016
REMARK 465 VAD C 3017
REMARK 465 DVA C 3018
REMARK 465 2OP C 3019
REMARK 465 VAL C 3020
REMARK 465 VAD D 3009
REMARK 465 DVA D 3010
REMARK 465 2OP D 3011
REMARK 465 VAD D 3013
REMARK 465 DVA D 3014
REMARK 465 2OP D 3015
REMARK 465 VAL D 3016
REMARK 465 VAD D 3017
REMARK 465 DVA D 3018
REMARK 465 2OP D 3019
REMARK 465 VAL D 3020
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 A2389 CG OD1 OD2
REMARK 470 ILE A2498 CG1 CG2 CD1
REMARK 470 VAL A2500 CG1 CG2
REMARK 470 ASP A2502 CG OD1 OD2
REMARK 470 ASP A2504 CG OD1 OD2
REMARK 470 LEU A2505 CG CD1 CD2
REMARK 470 GLU A2507 CG CD OE1 OE2
REMARK 470 GLU A2508 CG CD OE1 OE2
REMARK 470 LYS A2511 CG CD CE NZ
REMARK 470 LYS A2539 CG CD CE NZ
REMARK 470 ARG A2545 CG CD NE CZ NH1 NH2
REMARK 470 LEU A2565 CG CD1 CD2
REMARK 470 ARG A2576 CG CD NE CZ NH1 NH2
REMARK 470 ASP A2577 CG OD1 OD2
REMARK 470 LYS A2595 CG CD CE NZ
REMARK 470 GLU A2600 CG CD OE1 OE2
REMARK 470 ARG A2603 CG CD NE CZ NH1 NH2
REMARK 470 LEU A2647 CG CD1 CD2
REMARK 470 ARG B2382 CG CD NE CZ NH1 NH2
REMARK 470 ASN B2384 CG OD1 ND2
REMARK 470 GLU B2408 CG CD OE1 OE2
REMARK 470 ARG B2411 CG CD NE CZ NH1 NH2
REMARK 470 ARG B2494 CG CD NE CZ NH1 NH2
REMARK 470 LEU B2495 CG CD1 CD2
REMARK 470 THR B2506 OG1 CG2
REMARK 470 GLU B2507 CG CD OE1 OE2
REMARK 470 GLU B2508 CG CD OE1 OE2
REMARK 470 GLU B2509 CG CD OE1 OE2
REMARK 470 THR B2510 OG1 CG2
REMARK 470 LYS B2511 CG CD CE NZ
REMARK 470 LEU B2515 CG CD1 CD2
REMARK 470 ARG B2545 CG CD NE CZ NH1 NH2
REMARK 470 GLU B2558 CG CD OE1 OE2
REMARK 470 ASP B2559 CG OD1 OD2
REMARK 470 ARG B2576 CG CD NE CZ NH1 NH2
REMARK 470 GLN B2582 CG CD OE1 NE2
REMARK 470 ARG B2583 CG CD NE CZ NH1 NH2
REMARK 470 GLU B2600 CG CD OE1 OE2
REMARK 470 ARG B2603 CG CD NE CZ NH1 NH2
REMARK 470 ARG B2630 CG CD NE CZ NH1 NH2
REMARK 470 GLU B2636 CG CD OE1 OE2
REMARK 470 GLN B2639 CG CD OE1 NE2
REMARK 470 ARG B2643 CG CD NE CZ NH1 NH2
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 DPP A2463 -138.16 62.68
REMARK 500 ALA A2501 -70.19 -49.29
REMARK 500 ASP A2502 -5.41 70.71
REMARK 500 ASP A2504 44.87 -100.09
REMARK 500 GLN A2582 57.69 -144.17
REMARK 500 LEU A2647 77.25 -155.16
REMARK 500 LEU B2383 -166.35 -104.11
REMARK 500 DPP B2463 -139.17 62.87
REMARK 500 ASP B2586 30.74 -91.14
REMARK 500 ALA B2626 -63.81 -98.41
REMARK 500 ASP B2642 -48.04 -141.17
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 B2738 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH B2739 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH B2740 DISTANCE = 7.10 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ECB RELATED DB: PDB
REMARK 900 RELATED ID: 6ECC RELATED DB: PDB
REMARK 900 RELATED ID: 6ECD RELATED DB: PDB
REMARK 900 RELATED ID: 6ECF RELATED DB: PDB
DBREF 6ECE A 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECE B 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECE C 3009 3020 PDB 6ECE 6ECE 3009 3020
DBREF 6ECE D 3009 3020 PDB 6ECE 6ECE 3009 3020
SEQADV 6ECE MET A 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS A 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE GLU A 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE ASN A 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE LEU A 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE TYR A 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE PHE A 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE GLN A 2367 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE MET B 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE HIS B 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE GLU B 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE ASN B 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE LEU B 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE TYR B 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE PHE B 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECE GLN B 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 DPP 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
SEQRES 1 B 303 MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR
SEQRES 2 B 303 PHE GLN GLY GLY SER SER THR ALA GLY ASP PRO THR ALA
SEQRES 3 B 303 LYS LEU VAL ARG LEU ASN PRO ARG GLY GLY ASP GLY PRO
SEQRES 4 B 303 GLY ILE VAL PHE ALA PRO PRO ALA GLY GLY THR VAL LEU
SEQRES 5 B 303 GLY TYR ILE GLU LEU ALA ARG HIS LEU LYS GLY PHE GLY
SEQRES 6 B 303 GLU ILE HIS GLY VAL GLU ALA PRO GLY LEU GLY ALA GLY
SEQRES 7 B 303 GLU THR PRO VAL TYR PRO SER PHE GLU GLU MET VAL GLN
SEQRES 8 B 303 PHE CYS SER ASP SER ALA ALA GLY VAL ALA GLY ASP GLY
SEQRES 9 B 303 VAL TYR ILE GLY GLY HIS DPP LEU GLY GLY HIS ILE ALA
SEQRES 10 B 303 PHE TYR LEU ALA THR MET LEU LEU ASP ARG GLY ILE ARG
SEQRES 11 B 303 PRO LYS GLY LEU ILE ILE LEU ASP THR PRO PRO ARG LEU
SEQRES 12 B 303 GLY ASP ILE PRO VAL ALA ASP ALA ASP LEU THR GLU GLU
SEQRES 13 B 303 GLU THR LYS VAL PHE ILE LEU ALA MET GLY ILE GLY GLY
SEQRES 14 B 303 MET LEU ASP GLN ASP ARG ASP ALA LEU LYS ASP LEU PRO
SEQRES 15 B 303 TYR GLU GLU ALA LYS GLN LEU LEU LEU ASP ARG ALA LYS
SEQRES 16 B 303 ASN ASP PRO ARG VAL SER ALA PHE LEU SER GLU ASP TYR
SEQRES 17 B 303 LEU ASP ARG PHE LEU ARG LEU GLN MET HIS GLN LEU MET
SEQRES 18 B 303 TYR SER ARG ASP VAL VAL LEU PRO GLN ARG LYS LEU ASP
SEQRES 19 B 303 ILE PRO ILE HIS VAL PHE ARG THR LYS ASN HIS ALA PRO
SEQRES 20 B 303 GLU VAL ALA ARG LEU PHE SER ALA TRP GLU ASN TYR ALA
SEQRES 21 B 303 ALA GLY GLU VAL THR PHE VAL ASP ILE PRO GLY ASP HIS
SEQRES 22 B 303 ALA THR MET LEU ARG ALA PRO HIS VAL SER GLU VAL ALA
SEQRES 23 B 303 GLN LEU LEU ASP ARG HIS CYS GLY LEU PRO SER ASP ASP
SEQRES 24 B 303 GLY PRO ARG GLY
SEQRES 1 C 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
SEQRES 1 D 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
MODRES 6ECE DPP A 2463 SER MODIFIED RESIDUE
MODRES 6ECE DPP B 2463 SER MODIFIED RESIDUE
HET DPP A2463 10
HET DPP B2463 10
HET DVA C3010 16
HET 2OP C3011 9
HETNAM DPP DIAMINOPROPANOIC ACID
HETNAM DVA D-VALINE
HETNAM 2OP (2S)-2-HYDROXYPROPANOIC ACID
FORMUL 1 DPP 2(C3 H8 N2 O2)
FORMUL 3 DVA C5 H11 N O2
FORMUL 3 2OP C3 H6 O3
FORMUL 5 HOH *89(H2 O)
HELIX 1 AA1 PRO A 2376 ALA A 2378 5 3
HELIX 2 AA2 VAL A 2403 GLY A 2405 5 3
HELIX 3 AA3 TYR A 2406 LEU A 2413 1 8
HELIX 4 AA4 SER A 2437 GLY A 2454 1 18
HELIX 5 AA5 DPP A 2463 ARG A 2479 1 17
HELIX 6 AA6 THR A 2506 MET A 2517 1 12
HELIX 7 AA7 TYR A 2535 ASP A 2549 1 15
HELIX 8 AA8 ASP A 2549 LEU A 2556 1 8
HELIX 9 AA9 SER A 2557 MET A 2573 1 17
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
HELIX 14 AB5 VAL B 2403 GLY B 2405 5 3
HELIX 15 AB6 TYR B 2406 LEU B 2413 1 8
HELIX 16 AB7 SER B 2437 ALA B 2450 1 14
HELIX 17 AB8 DPP B 2463 ARG B 2479 1 17
HELIX 18 AB9 GLU B 2507 MET B 2517 1 11
HELIX 19 AC1 TYR B 2535 ASN B 2548 1 14
HELIX 20 AC2 ASP B 2549 LEU B 2556 1 8
HELIX 21 AC3 SER B 2557 ARG B 2576 1 20
HELIX 22 AC4 ALA B 2598 SER B 2606 1 9
HELIX 23 AC5 ALA B 2607 ALA B 2612 5 6
HELIX 24 AC6 ALA B 2626 ARG B 2630 5 5
HELIX 25 AC7 PRO B 2632 HIS B 2644 1 13
SHEET 1 AA114 LEU A2380 ASN A2384 0
SHEET 2 AA114 ILE A2419 VAL A2422 -1 O GLY A2421 N VAL A2381
SHEET 3 AA114 GLY A2392 ALA A2396 1 N ILE A2393 O HIS A2420
SHEET 4 AA114 VAL A2457 HIS A2462 1 O TYR A2458 N GLY A2392
SHEET 5 AA114 GLY A2485 LEU A2489 1 O ILE A2487 N ILE A2459
SHEET 6 AA114 ILE A2589 THR A2594 1 O HIS A2590 N ILE A2488
SHEET 7 AA114 GLU A2615 ILE A2621 1 O THR A2617 N VAL A2591
SHEET 8 AA114 VAL B2616 ILE B2621 1 O PHE B2618 N VAL A2616
SHEET 9 AA114 ILE B2589 THR B2594 1 N VAL B2591 O THR B2617
SHEET 10 AA114 GLY B2485 LEU B2489 1 N ILE B2488 O HIS B2590
SHEET 11 AA114 TYR B2458 HIS B2462 1 N ILE B2459 O ILE B2487
SHEET 12 AA114 ILE B2393 ALA B2396 1 N VAL B2394 O GLY B2460
SHEET 13 AA114 ILE B2419 VAL B2422 1 O HIS B2420 N PHE B2395
SHEET 14 AA114 LEU B2380 ARG B2382 -1 N VAL B2381 O GLY B2421
LINK C HIS A2462 N DPP A2463 1555 1555 1.34
LINK C DPP A2463 N LEU A2464 1555 1555 1.33
LINK NG DPP A2463 C VAL C3012 1555 1555 1.34
LINK C HIS B2462 N DPP B2463 1555 1555 1.33
LINK C DPP B2463 N LEU B2464 1555 1555 1.33
LINK NG DPP B2463 C VAL D3012 1555 1555 1.33
LINK C DVA C3010 OHN 2OP C3011 1555 1555 1.33
LINK C 2OP C3011 N VAL C3012 1555 1555 1.34
CISPEP 1 ALA A 2631 PRO A 2632 0 0.62
CISPEP 2 ALA B 2631 PRO B 2632 0 -2.76
CRYST1 77.571 77.571 235.151 90.00 90.00 120.00 H 3 18
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 0.012891 0.007443 0.000000 0.00000
SCALE2 0.000000 0.014886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004253 0.00000
TER 3724 PRO A2648
TER 7103 GLY B2646
TER 7145 VAL C3012
TER 7161 VAL D3012
MASTER 491 0 4 25 14 0 0 6 3739 4 52 50
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