| content |
HEADER HYDROLASE 07-AUG-18 6ECD
TITLE VLM2 THIOESTERASE DOMAIN WITH GENETICALLY ENCODED 2,3-DIAMINOPROPIONIC
TITLE 2 ACID BOUND WITH A TETRADEPSIPEPTIDE
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;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TETRADEPSIPEPTIDE;
COMPND 9 CHAIN: B;
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 6ECD 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. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 107.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 48054
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.530
REMARK 3 FREE R VALUE TEST SET COUNT : 2658
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1107.8600 - 5.0700 1.00 2660 156 0.2116 0.2229
REMARK 3 2 5.0700 - 4.0200 1.00 2472 145 0.1488 0.1901
REMARK 3 3 4.0200 - 3.5200 1.00 2433 142 0.1587 0.2057
REMARK 3 4 3.5200 - 3.1900 1.00 2416 142 0.1813 0.1875
REMARK 3 5 3.1900 - 2.9600 1.00 2408 141 0.1943 0.2233
REMARK 3 6 2.9600 - 2.7900 1.00 2385 139 0.2224 0.2197
REMARK 3 7 2.7900 - 2.6500 1.00 2385 140 0.2151 0.2614
REMARK 3 8 2.6500 - 2.5400 1.00 2370 139 0.2033 0.2309
REMARK 3 9 2.5400 - 2.4400 1.00 2369 138 0.1930 0.1904
REMARK 3 10 2.4400 - 2.3500 1.00 2367 138 0.1863 0.2369
REMARK 3 11 2.3500 - 2.2800 1.00 2361 139 0.1850 0.1999
REMARK 3 12 2.2800 - 2.2100 1.00 2346 137 0.1826 0.1959
REMARK 3 13 2.2100 - 2.1600 1.00 2338 138 0.1819 0.2374
REMARK 3 14 2.1600 - 2.1000 1.00 2365 137 0.1818 0.2199
REMARK 3 15 2.1000 - 2.0600 1.00 2342 137 0.2040 0.2300
REMARK 3 16 2.0600 - 2.0100 1.00 2344 138 0.2155 0.2193
REMARK 3 17 2.0100 - 1.9700 1.00 2338 137 0.2221 0.2365
REMARK 3 18 1.9700 - 1.9300 1.00 2341 137 0.2452 0.2608
REMARK 3 19 1.9300 - 1.9000 1.00 2356 138 0.2817 0.3126
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) : 19.797
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.42
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 : 0.017 1856
REMARK 3 ANGLE : 1.402 2529
REMARK 3 CHIRALITY : 0.092 285
REMARK 3 PLANARITY : 0.010 335
REMARK 3 DIHEDRAL : 11.340 1092
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): 351.7085 132.4787 381.9896
REMARK 3 T TENSOR
REMARK 3 T11: 0.2644 T22: 0.2835
REMARK 3 T33: 0.3718 T12: -0.0852
REMARK 3 T13: 0.0033 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 1.4065 L22: 1.1213
REMARK 3 L33: 1.6292 L12: 0.4460
REMARK 3 L13: 0.1113 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0384 S12: -0.0154 S13: -0.1050
REMARK 3 S21: 0.0670 S22: 0.0303 S23: 0.1926
REMARK 3 S31: 0.0292 S32: -0.0703 S33: -0.0002
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 6ECD 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_1000236064.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-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 : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48063
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 107.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 37.20
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
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 (%): 72.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.65 M DL-MALIC ACID, PH 8.0, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 A2759 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 ALA A 2429
REMARK 465 GLY A 2430
REMARK 465 GLY A 2496
REMARK 465 ASP A 2497
REMARK 465 ILE A 2498
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 GLU A 2508
REMARK 465 GLU A 2509
REMARK 465 THR A 2510
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 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 VAD B 3009
REMARK 465 DVA B 3010
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 LYS A2511 CG CD CE NZ
REMARK 470 VAL A2512 CG1 CG2
REMARK 470 PHE A2513 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A2514 CG1 CG2 CD1
REMARK 470 LEU A2515 CG CD1 CD2
REMARK 470 MET A2517 CG SD CE
REMARK 470 ILE A2519 CG1 CG2 CD1
REMARK 470 LEU A2523 CG CD1 CD2
REMARK 470 ASP A2524 CG OD1 OD2
REMARK 470 GLN A2525 CG CD OE1 NE2
REMARK 470 GLU A2536 CG CD OE1 OE2
REMARK 470 GLU A2537 CG CD OE1 OE2
REMARK 470 LYS A2539 CG CD CE NZ
REMARK 470 LEU A2541 CG CD1 CD2
REMARK 470 LEU A2542 CG CD1 CD2
REMARK 470 LEU A2543 CG CD1 CD2
REMARK 470 ASP A2544 CG OD1 OD2
REMARK 470 ARG A2545 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2547 CG CD CE NZ
REMARK 470 ASN A2548 CG OD1 ND2
REMARK 470 ARG A2551 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2558 CG CD OE1 OE2
REMARK 470 ARG A2576 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2595 CG CD CE NZ
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 DPP A2463 -134.01 57.70
REMARK 500
REMARK 500 REMARK: NULL
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: 6ECE RELATED DB: PDB
REMARK 900 RELATED ID: 6ECF RELATED DB: PDB
DBREF 6ECD A 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECD B 3009 3012 PDB 6ECD 6ECD 3009 3012
SEQADV 6ECD MET A 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD HIS A 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD GLU A 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD ASN A 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD LEU A 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD TYR A 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD PHE A 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECD 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 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 4 VAD DVA 2OP VAL
MODRES 6ECD DPP A 2463 SER MODIFIED RESIDUE
HET DPP A2463 10
HET 2OP B3011 9
HETNAM DPP DIAMINOPROPANOIC ACID
HETNAM 2OP (2S)-2-HYDROXYPROPANOIC ACID
FORMUL 1 DPP C3 H8 N2 O2
FORMUL 2 2OP C3 H6 O3
FORMUL 3 HOH *106(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 DPP A 2463 ARG A 2479 1 17
HELIX 5 AA5 VAL A 2512 GLY A 2518 1 7
HELIX 6 AA6 GLY A 2518 LEU A 2523 1 6
HELIX 7 AA7 GLU A 2537 ASN A 2548 1 12
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 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 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 GLY A2485 LEU A2489 1 O ILE A2487 N ILE A2459
SHEET 6 AA1 7 ILE A2589 ARG A2593 1 O HIS A2590 N ILE A2488
SHEET 7 AA1 7 VAL A2616 ASP A2620 1 O THR A2617 N VAL A2591
LINK C HIS A2462 N DPP A2463 1555 1555 1.32
LINK C DPP A2463 N LEU A2464 1555 1555 1.32
LINK NG DPP A2463 C VAL B3012 1555 1555 1.34
LINK C 2OP B3011 N VAL B3012 1555 1555 1.33
CISPEP 1 ALA A 2631 PRO A 2632 0 -1.13
CRYST1 152.298 152.298 152.298 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 0.006566 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006566 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006566 0.00000
TER 3511 PRO A2648
TER 3537 VAL B3012
MASTER 437 0 2 12 7 0 0 6 1904 2 23 25
END |