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HEADER HYDROLASE 07-AUG-18 6ECF
TITLE VLM2 THIOESTERASE DOMAIN WITH GENETICALLY ENCODED 2,3-DIAMINOPROPIONIC
TITLE 2 ACID BOUND WITH A DODECADEPSIPEPTIDE, SPACE GROUP P1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VLM2;
COMPND 3 CHAIN: A, B, C, D, E, F;
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: G, I, H, K, J, L;
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 6ECF 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. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.080
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 53933
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2683
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 78.5900 - 6.6700 0.99 2726 158 0.1973 0.2635
REMARK 3 2 6.6700 - 5.2900 0.98 2657 174 0.2100 0.2673
REMARK 3 3 5.2900 - 4.6300 0.98 2724 152 0.1545 0.1973
REMARK 3 4 4.6300 - 4.2000 0.98 2675 183 0.1583 0.1937
REMARK 3 5 4.2000 - 3.9000 0.98 2698 119 0.1702 0.2437
REMARK 3 6 3.9000 - 3.6700 0.98 2675 155 0.1724 0.1859
REMARK 3 7 3.6700 - 3.4900 0.98 2731 114 0.1808 0.2172
REMARK 3 8 3.4900 - 3.3400 0.98 2732 130 0.1942 0.2898
REMARK 3 9 3.3400 - 3.2100 0.98 2687 126 0.2228 0.2660
REMARK 3 10 3.2100 - 3.1000 0.97 2748 106 0.2181 0.2770
REMARK 3 11 3.1000 - 3.0000 0.98 2706 121 0.2218 0.3061
REMARK 3 12 3.0000 - 2.9100 0.97 2692 169 0.2205 0.2845
REMARK 3 13 2.9100 - 2.8400 0.97 2611 166 0.2362 0.3061
REMARK 3 14 2.8400 - 2.7700 0.97 2754 120 0.2404 0.2983
REMARK 3 15 2.7700 - 2.7100 0.97 2739 126 0.2497 0.3445
REMARK 3 16 2.7100 - 2.6500 0.97 2588 135 0.2345 0.2903
REMARK 3 17 2.6500 - 2.5900 0.97 2735 143 0.2390 0.2635
REMARK 3 18 2.5900 - 2.5500 0.97 2711 127 0.2418 0.3044
REMARK 3 19 2.5500 - 2.5000 0.97 2661 159 0.2423 0.2992
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) : 0.329
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.508
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.32
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 : 0.002 11837
REMARK 3 ANGLE : 0.558 16106
REMARK 3 CHIRALITY : 0.040 1817
REMARK 3 PLANARITY : 0.003 2110
REMARK 3 DIHEDRAL : 11.355 6960
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 6ECF 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_1000236075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-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 : 53945
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 78.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
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 (%): 40.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M DL-MALIC ACID, 25 MM HEPES, PH
REMARK 280 8.0, 100 MM SODIUM CHLORIDE, 0.2 MM TCEP, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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, G
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, I
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, K
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L
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 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 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 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 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 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 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 MET C 2353
REMARK 465 HIS C 2354
REMARK 465 HIS C 2355
REMARK 465 HIS C 2356
REMARK 465 HIS C 2357
REMARK 465 HIS C 2358
REMARK 465 HIS C 2359
REMARK 465 HIS C 2360
REMARK 465 HIS C 2361
REMARK 465 GLU C 2362
REMARK 465 ASN C 2363
REMARK 465 LEU C 2364
REMARK 465 TYR C 2365
REMARK 465 PHE C 2366
REMARK 465 GLN C 2367
REMARK 465 GLY C 2368
REMARK 465 GLY C 2369
REMARK 465 SER C 2370
REMARK 465 SER C 2371
REMARK 465 THR C 2372
REMARK 465 ALA C 2373
REMARK 465 GLY C 2374
REMARK 465 ASP C 2375
REMARK 465 ILE C 2498
REMARK 465 PRO C 2499
REMARK 465 VAL C 2500
REMARK 465 ALA C 2501
REMARK 465 ASP C 2502
REMARK 465 ALA C 2503
REMARK 465 ASP C 2504
REMARK 465 LEU C 2505
REMARK 465 THR C 2506
REMARK 465 ILE C 2519
REMARK 465 GLY C 2520
REMARK 465 GLY C 2521
REMARK 465 MET C 2522
REMARK 465 LEU C 2523
REMARK 465 ASP C 2524
REMARK 465 GLN C 2525
REMARK 465 ASP C 2526
REMARK 465 ARG C 2527
REMARK 465 ASP C 2528
REMARK 465 ALA C 2529
REMARK 465 LEU C 2530
REMARK 465 SER C 2649
REMARK 465 ASP C 2650
REMARK 465 ASP C 2651
REMARK 465 GLY C 2652
REMARK 465 PRO C 2653
REMARK 465 ARG C 2654
REMARK 465 GLY C 2655
REMARK 465 MET D 2353
REMARK 465 HIS D 2354
REMARK 465 HIS D 2355
REMARK 465 HIS D 2356
REMARK 465 HIS D 2357
REMARK 465 HIS D 2358
REMARK 465 HIS D 2359
REMARK 465 HIS D 2360
REMARK 465 HIS D 2361
REMARK 465 GLU D 2362
REMARK 465 ASN D 2363
REMARK 465 LEU D 2364
REMARK 465 TYR D 2365
REMARK 465 PHE D 2366
REMARK 465 GLN D 2367
REMARK 465 GLY D 2368
REMARK 465 GLY D 2369
REMARK 465 SER D 2370
REMARK 465 SER D 2371
REMARK 465 THR D 2372
REMARK 465 ALA D 2373
REMARK 465 GLY D 2374
REMARK 465 ASP D 2375
REMARK 465 PRO D 2376
REMARK 465 VAL D 2500
REMARK 465 ALA D 2501
REMARK 465 ASP D 2502
REMARK 465 ALA D 2503
REMARK 465 ASP D 2504
REMARK 465 LEU D 2505
REMARK 465 PRO D 2648
REMARK 465 SER D 2649
REMARK 465 ASP D 2650
REMARK 465 ASP D 2651
REMARK 465 GLY D 2652
REMARK 465 PRO D 2653
REMARK 465 ARG D 2654
REMARK 465 GLY D 2655
REMARK 465 MET E 2353
REMARK 465 HIS E 2354
REMARK 465 HIS E 2355
REMARK 465 HIS E 2356
REMARK 465 HIS E 2357
REMARK 465 HIS E 2358
REMARK 465 HIS E 2359
REMARK 465 HIS E 2360
REMARK 465 HIS E 2361
REMARK 465 GLU E 2362
REMARK 465 ASN E 2363
REMARK 465 LEU E 2364
REMARK 465 TYR E 2365
REMARK 465 PHE E 2366
REMARK 465 GLN E 2367
REMARK 465 GLY E 2368
REMARK 465 GLY E 2369
REMARK 465 SER E 2370
REMARK 465 SER E 2371
REMARK 465 THR E 2372
REMARK 465 ALA E 2373
REMARK 465 GLY E 2374
REMARK 465 ASP E 2375
REMARK 465 PRO E 2376
REMARK 465 THR E 2377
REMARK 465 ALA E 2378
REMARK 465 PRO E 2499
REMARK 465 VAL E 2500
REMARK 465 ALA E 2501
REMARK 465 ASP E 2502
REMARK 465 ALA E 2503
REMARK 465 ASP E 2504
REMARK 465 LEU E 2505
REMARK 465 THR E 2506
REMARK 465 ALA E 2598
REMARK 465 ASP E 2650
REMARK 465 ASP E 2651
REMARK 465 GLY E 2652
REMARK 465 PRO E 2653
REMARK 465 ARG E 2654
REMARK 465 GLY E 2655
REMARK 465 MET F 2353
REMARK 465 HIS F 2354
REMARK 465 HIS F 2355
REMARK 465 HIS F 2356
REMARK 465 HIS F 2357
REMARK 465 HIS F 2358
REMARK 465 HIS F 2359
REMARK 465 HIS F 2360
REMARK 465 HIS F 2361
REMARK 465 GLU F 2362
REMARK 465 ASN F 2363
REMARK 465 LEU F 2364
REMARK 465 TYR F 2365
REMARK 465 PHE F 2366
REMARK 465 GLN F 2367
REMARK 465 GLY F 2368
REMARK 465 GLY F 2369
REMARK 465 SER F 2370
REMARK 465 SER F 2371
REMARK 465 THR F 2372
REMARK 465 ALA F 2373
REMARK 465 GLY F 2374
REMARK 465 ASP F 2375
REMARK 465 ASP F 2389
REMARK 465 GLY F 2390
REMARK 465 GLY F 2496
REMARK 465 ASP F 2497
REMARK 465 ILE F 2498
REMARK 465 PRO F 2499
REMARK 465 VAL F 2500
REMARK 465 ALA F 2501
REMARK 465 ASP F 2502
REMARK 465 ALA F 2503
REMARK 465 ASP F 2504
REMARK 465 LEU F 2505
REMARK 465 THR F 2506
REMARK 465 GLU F 2507
REMARK 465 PRO F 2648
REMARK 465 SER F 2649
REMARK 465 ASP F 2650
REMARK 465 ASP F 2651
REMARK 465 GLY F 2652
REMARK 465 PRO F 2653
REMARK 465 ARG F 2654
REMARK 465 GLY F 2655
REMARK 465 VAD G 3013
REMARK 465 DVA G 3014
REMARK 465 2OP G 3015
REMARK 465 VAL G 3016
REMARK 465 VAD G 3017
REMARK 465 DVA G 3018
REMARK 465 2OP G 3019
REMARK 465 VAL G 3020
REMARK 465 VAD I 3009
REMARK 465 VAD I 3013
REMARK 465 DVA I 3014
REMARK 465 2OP I 3015
REMARK 465 VAL I 3016
REMARK 465 VAD I 3017
REMARK 465 DVA I 3018
REMARK 465 2OP I 3019
REMARK 465 VAL I 3020
REMARK 465 VAD H 3009
REMARK 465 DVA H 3010
REMARK 465 VAD H 3013
REMARK 465 DVA H 3014
REMARK 465 2OP H 3015
REMARK 465 VAL H 3016
REMARK 465 VAD H 3017
REMARK 465 DVA H 3018
REMARK 465 2OP H 3019
REMARK 465 VAL H 3020
REMARK 465 VAD K 3009
REMARK 465 DVA K 3010
REMARK 465 VAD K 3013
REMARK 465 DVA K 3014
REMARK 465 2OP K 3015
REMARK 465 VAL K 3016
REMARK 465 VAD K 3017
REMARK 465 DVA K 3018
REMARK 465 2OP K 3019
REMARK 465 VAL K 3020
REMARK 465 VAD J 3009
REMARK 465 DVA J 3010
REMARK 465 VAD J 3013
REMARK 465 DVA J 3014
REMARK 465 2OP J 3015
REMARK 465 VAL J 3016
REMARK 465 VAD J 3017
REMARK 465 DVA J 3018
REMARK 465 2OP J 3019
REMARK 465 VAL J 3020
REMARK 465 VAD L 3009
REMARK 465 DVA L 3010
REMARK 465 VAD L 3013
REMARK 465 DVA L 3014
REMARK 465 2OP L 3015
REMARK 465 VAL L 3016
REMARK 465 VAD L 3017
REMARK 465 DVA L 3018
REMARK 465 2OP L 3019
REMARK 465 VAL L 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 LEU A2495 CG CD1 CD2
REMARK 470 THR A2506 OG1 CG2
REMARK 470 GLU A2507 CG CD OE1 OE2
REMARK 470 GLU A2508 CG CD OE1 OE2
REMARK 470 GLU A2509 CG CD OE1 OE2
REMARK 470 LYS A2511 CG CD CE NZ
REMARK 470 LYS A2531 CG CD CE NZ
REMARK 470 ASP A2532 CG OD1 OD2
REMARK 470 LEU A2533 CG CD1 CD2
REMARK 470 LYS A2539 CG CD CE NZ
REMARK 470 ARG A2545 CG CD NE CZ NH1 NH2
REMARK 470 ARG A2576 CG CD NE CZ NH1 NH2
REMARK 470 GLN A2582 CG CD OE1 NE2
REMARK 470 ARG A2583 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2600 CG CD OE1 OE2
REMARK 470 ARG A2603 CG CD NE CZ NH1 NH2
REMARK 470 ARG B2494 CG CD NE CZ NH1 NH2
REMARK 470 GLU B2507 CG CD OE1 OE2
REMARK 470 GLU B2508 CG CD OE1 OE2
REMARK 470 LYS B2511 CG CD CE NZ
REMARK 470 ASP B2532 CG OD1 OD2
REMARK 470 LEU B2533 CG CD1 CD2
REMARK 470 ARG B2576 CG CD NE CZ NH1 NH2
REMARK 470 VAL B2579 CG1 CG2
REMARK 470 GLU B2600 CG CD OE1 OE2
REMARK 470 GLU B2615 CG CD OE1 OE2
REMARK 470 ARG B2630 CG CD NE CZ NH1 NH2
REMARK 470 ASP C2389 CG OD1 OD2
REMARK 470 ASP C2455 CG OD1 OD2
REMARK 470 ARG C2494 CG CD NE CZ NH1 NH2
REMARK 470 LEU C2495 CG CD1 CD2
REMARK 470 ASP C2497 CG OD1 OD2
REMARK 470 GLU C2507 CG CD OE1 OE2
REMARK 470 GLU C2508 CG CD OE1 OE2
REMARK 470 LYS C2511 CG CD CE NZ
REMARK 470 LYS C2531 CG CD CE NZ
REMARK 470 ASP C2532 CG OD1 OD2
REMARK 470 ARG C2576 CG CD NE CZ NH1 NH2
REMARK 470 ASP C2577 CG OD1 OD2
REMARK 470 GLN C2582 CG CD OE1 NE2
REMARK 470 ARG D2386 CG CD NE CZ NH1 NH2
REMARK 470 GLU D2439 CG CD OE1 OE2
REMARK 470 ARG D2494 CG CD NE CZ NH1 NH2
REMARK 470 ASP D2497 CG OD1 OD2
REMARK 470 GLU D2507 CG CD OE1 OE2
REMARK 470 GLU D2508 CG CD OE1 OE2
REMARK 470 GLU D2509 CG CD OE1 OE2
REMARK 470 LYS D2511 CG CD CE NZ
REMARK 470 ILE D2519 CG1 CG2 CD1
REMARK 470 ASP D2524 CG OD1 OD2
REMARK 470 GLN D2525 CG CD OE1 NE2
REMARK 470 ASP D2526 CG OD1 OD2
REMARK 470 ARG D2527 CG CD NE CZ NH1 NH2
REMARK 470 ASP D2532 CG OD1 OD2
REMARK 470 LEU D2533 CG CD1 CD2
REMARK 470 ARG D2545 CG CD NE CZ NH1 NH2
REMARK 470 GLN D2582 CG CD OE1 NE2
REMARK 470 GLU D2600 CG CD OE1 OE2
REMARK 470 ARG D2630 CG CD NE CZ NH1 NH2
REMARK 470 LYS E2379 CG CD CE NZ
REMARK 470 ARG E2386 CG CD NE CZ NH1 NH2
REMARK 470 ARG E2411 CG CD NE CZ NH1 NH2
REMARK 470 ARG E2494 CG CD NE CZ NH1 NH2
REMARK 470 ASP E2497 CG OD1 OD2
REMARK 470 ILE E2498 CG1 CG2 CD1
REMARK 470 GLU E2507 CG CD OE1 OE2
REMARK 470 GLU E2508 CG CD OE1 OE2
REMARK 470 GLU E2509 CG CD OE1 OE2
REMARK 470 THR E2510 OG1 CG2
REMARK 470 LYS E2511 CG CD CE NZ
REMARK 470 ASP E2524 CG OD1 OD2
REMARK 470 GLN E2525 CG CD OE1 NE2
REMARK 470 ASP E2526 CG OD1 OD2
REMARK 470 ARG E2527 CG CD NE CZ NH1 NH2
REMARK 470 LYS E2531 CG CD CE NZ
REMARK 470 ASP E2532 CG OD1 OD2
REMARK 470 ARG E2545 CG CD NE CZ NH1 NH2
REMARK 470 ARG E2576 CG CD NE CZ NH1 NH2
REMARK 470 GLN E2582 CG CD OE1 NE2
REMARK 470 ARG E2583 CG CD NE CZ NH1 NH2
REMARK 470 GLU E2600 CG CD OE1 OE2
REMARK 470 ARG E2603 CG CD NE CZ NH1 NH2
REMARK 470 ARG F2386 CG CD NE CZ NH1 NH2
REMARK 470 ARG F2411 CG CD NE CZ NH1 NH2
REMARK 470 GLU F2508 CG CD OE1 OE2
REMARK 470 GLU F2509 CG CD OE1 OE2
REMARK 470 LYS F2511 CG CD CE NZ
REMARK 470 VAL F2512 CG1 CG2
REMARK 470 ASP F2524 CG OD1 OD2
REMARK 470 GLN F2525 CG CD OE1 NE2
REMARK 470 ASP F2526 CG OD1 OD2
REMARK 470 ARG F2527 CG CD NE CZ NH1 NH2
REMARK 470 ASP F2528 CG OD1 OD2
REMARK 470 ASP F2532 CG OD1 OD2
REMARK 470 LYS F2539 CG CD CE NZ
REMARK 470 ARG F2545 CG CD NE CZ NH1 NH2
REMARK 470 ARG F2576 CG CD NE CZ NH1 NH2
REMARK 470 GLN F2582 CG CD OE1 NE2
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 -134.00 63.82
REMARK 500 GLN A2582 34.95 -77.25
REMARK 500 ASP A2586 31.63 -86.69
REMARK 500 LEU A2647 80.02 -170.77
REMARK 500 DPP B2463 -137.77 60.54
REMARK 500 ASP B2478 1.88 -68.17
REMARK 500 GLN B2582 81.77 -67.05
REMARK 500 ASN C2384 119.61 -172.07
REMARK 500 DPP C2463 -126.74 61.03
REMARK 500 PHE C2555 -30.02 -131.08
REMARK 500 GLN C2582 88.67 -67.05
REMARK 500 LEU C2647 80.67 -165.39
REMARK 500 VAL D2452 -30.53 -134.33
REMARK 500 DPP D2463 -125.65 57.17
REMARK 500 ASP D2526 53.89 -119.72
REMARK 500 GLN D2582 77.12 -67.92
REMARK 500 DPP E2463 -137.57 64.39
REMARK 500 ASN E2596 62.03 -108.31
REMARK 500 ALA E2626 -60.75 -95.04
REMARK 500 LEU F2383 -38.05 -139.02
REMARK 500 DPP F2463 -136.95 64.08
REMARK 500 MET F2517 5.82 -69.53
REMARK 500 ASP F2526 32.49 -87.24
REMARK 500 CYS F2645 -37.70 -132.38
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 C2735 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH D2730 DISTANCE = 6.84 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: 6ECE RELATED DB: PDB
DBREF 6ECF A 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECF B 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECF C 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECF D 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECF E 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECF F 2368 2655 UNP Q1PSF3 Q1PSF3_9ACTN 2368 2655
DBREF 6ECF G 3009 3020 PDB 6ECF 6ECF 3009 3020
DBREF 6ECF I 3009 3020 PDB 6ECF 6ECF 3009 3020
DBREF 6ECF H 3009 3020 PDB 6ECF 6ECF 3009 3020
DBREF 6ECF K 3009 3020 PDB 6ECF 6ECF 3009 3020
DBREF 6ECF J 3009 3020 PDB 6ECF 6ECF 3009 3020
DBREF 6ECF L 3009 3020 PDB 6ECF 6ECF 3009 3020
SEQADV 6ECF MET A 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS A 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLU A 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF ASN A 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF LEU A 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF TYR A 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF PHE A 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLN A 2367 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF MET B 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS B 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLU B 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF ASN B 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF LEU B 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF TYR B 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF PHE B 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLN B 2367 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF MET C 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS C 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLU C 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF ASN C 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF LEU C 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF TYR C 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF PHE C 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLN C 2367 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF MET D 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS D 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLU D 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF ASN D 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF LEU D 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF TYR D 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF PHE D 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLN D 2367 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF MET E 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS E 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLU E 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF ASN E 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF LEU E 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF TYR E 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF PHE E 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLN E 2367 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF MET F 2353 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2354 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2355 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2356 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2357 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2358 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2359 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2360 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF HIS F 2361 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLU F 2362 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF ASN F 2363 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF LEU F 2364 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF TYR F 2365 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF PHE F 2366 UNP Q1PSF3 EXPRESSION TAG
SEQADV 6ECF GLN F 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 303 MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR
SEQRES 2 C 303 PHE GLN GLY GLY SER SER THR ALA GLY ASP PRO THR ALA
SEQRES 3 C 303 LYS LEU VAL ARG LEU ASN PRO ARG GLY GLY ASP GLY PRO
SEQRES 4 C 303 GLY ILE VAL PHE ALA PRO PRO ALA GLY GLY THR VAL LEU
SEQRES 5 C 303 GLY TYR ILE GLU LEU ALA ARG HIS LEU LYS GLY PHE GLY
SEQRES 6 C 303 GLU ILE HIS GLY VAL GLU ALA PRO GLY LEU GLY ALA GLY
SEQRES 7 C 303 GLU THR PRO VAL TYR PRO SER PHE GLU GLU MET VAL GLN
SEQRES 8 C 303 PHE CYS SER ASP SER ALA ALA GLY VAL ALA GLY ASP GLY
SEQRES 9 C 303 VAL TYR ILE GLY GLY HIS DPP LEU GLY GLY HIS ILE ALA
SEQRES 10 C 303 PHE TYR LEU ALA THR MET LEU LEU ASP ARG GLY ILE ARG
SEQRES 11 C 303 PRO LYS GLY LEU ILE ILE LEU ASP THR PRO PRO ARG LEU
SEQRES 12 C 303 GLY ASP ILE PRO VAL ALA ASP ALA ASP LEU THR GLU GLU
SEQRES 13 C 303 GLU THR LYS VAL PHE ILE LEU ALA MET GLY ILE GLY GLY
SEQRES 14 C 303 MET LEU ASP GLN ASP ARG ASP ALA LEU LYS ASP LEU PRO
SEQRES 15 C 303 TYR GLU GLU ALA LYS GLN LEU LEU LEU ASP ARG ALA LYS
SEQRES 16 C 303 ASN ASP PRO ARG VAL SER ALA PHE LEU SER GLU ASP TYR
SEQRES 17 C 303 LEU ASP ARG PHE LEU ARG LEU GLN MET HIS GLN LEU MET
SEQRES 18 C 303 TYR SER ARG ASP VAL VAL LEU PRO GLN ARG LYS LEU ASP
SEQRES 19 C 303 ILE PRO ILE HIS VAL PHE ARG THR LYS ASN HIS ALA PRO
SEQRES 20 C 303 GLU VAL ALA ARG LEU PHE SER ALA TRP GLU ASN TYR ALA
SEQRES 21 C 303 ALA GLY GLU VAL THR PHE VAL ASP ILE PRO GLY ASP HIS
SEQRES 22 C 303 ALA THR MET LEU ARG ALA PRO HIS VAL SER GLU VAL ALA
SEQRES 23 C 303 GLN LEU LEU ASP ARG HIS CYS GLY LEU PRO SER ASP ASP
SEQRES 24 C 303 GLY PRO ARG GLY
SEQRES 1 D 303 MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR
SEQRES 2 D 303 PHE GLN GLY GLY SER SER THR ALA GLY ASP PRO THR ALA
SEQRES 3 D 303 LYS LEU VAL ARG LEU ASN PRO ARG GLY GLY ASP GLY PRO
SEQRES 4 D 303 GLY ILE VAL PHE ALA PRO PRO ALA GLY GLY THR VAL LEU
SEQRES 5 D 303 GLY TYR ILE GLU LEU ALA ARG HIS LEU LYS GLY PHE GLY
SEQRES 6 D 303 GLU ILE HIS GLY VAL GLU ALA PRO GLY LEU GLY ALA GLY
SEQRES 7 D 303 GLU THR PRO VAL TYR PRO SER PHE GLU GLU MET VAL GLN
SEQRES 8 D 303 PHE CYS SER ASP SER ALA ALA GLY VAL ALA GLY ASP GLY
SEQRES 9 D 303 VAL TYR ILE GLY GLY HIS DPP LEU GLY GLY HIS ILE ALA
SEQRES 10 D 303 PHE TYR LEU ALA THR MET LEU LEU ASP ARG GLY ILE ARG
SEQRES 11 D 303 PRO LYS GLY LEU ILE ILE LEU ASP THR PRO PRO ARG LEU
SEQRES 12 D 303 GLY ASP ILE PRO VAL ALA ASP ALA ASP LEU THR GLU GLU
SEQRES 13 D 303 GLU THR LYS VAL PHE ILE LEU ALA MET GLY ILE GLY GLY
SEQRES 14 D 303 MET LEU ASP GLN ASP ARG ASP ALA LEU LYS ASP LEU PRO
SEQRES 15 D 303 TYR GLU GLU ALA LYS GLN LEU LEU LEU ASP ARG ALA LYS
SEQRES 16 D 303 ASN ASP PRO ARG VAL SER ALA PHE LEU SER GLU ASP TYR
SEQRES 17 D 303 LEU ASP ARG PHE LEU ARG LEU GLN MET HIS GLN LEU MET
SEQRES 18 D 303 TYR SER ARG ASP VAL VAL LEU PRO GLN ARG LYS LEU ASP
SEQRES 19 D 303 ILE PRO ILE HIS VAL PHE ARG THR LYS ASN HIS ALA PRO
SEQRES 20 D 303 GLU VAL ALA ARG LEU PHE SER ALA TRP GLU ASN TYR ALA
SEQRES 21 D 303 ALA GLY GLU VAL THR PHE VAL ASP ILE PRO GLY ASP HIS
SEQRES 22 D 303 ALA THR MET LEU ARG ALA PRO HIS VAL SER GLU VAL ALA
SEQRES 23 D 303 GLN LEU LEU ASP ARG HIS CYS GLY LEU PRO SER ASP ASP
SEQRES 24 D 303 GLY PRO ARG GLY
SEQRES 1 E 303 MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR
SEQRES 2 E 303 PHE GLN GLY GLY SER SER THR ALA GLY ASP PRO THR ALA
SEQRES 3 E 303 LYS LEU VAL ARG LEU ASN PRO ARG GLY GLY ASP GLY PRO
SEQRES 4 E 303 GLY ILE VAL PHE ALA PRO PRO ALA GLY GLY THR VAL LEU
SEQRES 5 E 303 GLY TYR ILE GLU LEU ALA ARG HIS LEU LYS GLY PHE GLY
SEQRES 6 E 303 GLU ILE HIS GLY VAL GLU ALA PRO GLY LEU GLY ALA GLY
SEQRES 7 E 303 GLU THR PRO VAL TYR PRO SER PHE GLU GLU MET VAL GLN
SEQRES 8 E 303 PHE CYS SER ASP SER ALA ALA GLY VAL ALA GLY ASP GLY
SEQRES 9 E 303 VAL TYR ILE GLY GLY HIS DPP LEU GLY GLY HIS ILE ALA
SEQRES 10 E 303 PHE TYR LEU ALA THR MET LEU LEU ASP ARG GLY ILE ARG
SEQRES 11 E 303 PRO LYS GLY LEU ILE ILE LEU ASP THR PRO PRO ARG LEU
SEQRES 12 E 303 GLY ASP ILE PRO VAL ALA ASP ALA ASP LEU THR GLU GLU
SEQRES 13 E 303 GLU THR LYS VAL PHE ILE LEU ALA MET GLY ILE GLY GLY
SEQRES 14 E 303 MET LEU ASP GLN ASP ARG ASP ALA LEU LYS ASP LEU PRO
SEQRES 15 E 303 TYR GLU GLU ALA LYS GLN LEU LEU LEU ASP ARG ALA LYS
SEQRES 16 E 303 ASN ASP PRO ARG VAL SER ALA PHE LEU SER GLU ASP TYR
SEQRES 17 E 303 LEU ASP ARG PHE LEU ARG LEU GLN MET HIS GLN LEU MET
SEQRES 18 E 303 TYR SER ARG ASP VAL VAL LEU PRO GLN ARG LYS LEU ASP
SEQRES 19 E 303 ILE PRO ILE HIS VAL PHE ARG THR LYS ASN HIS ALA PRO
SEQRES 20 E 303 GLU VAL ALA ARG LEU PHE SER ALA TRP GLU ASN TYR ALA
SEQRES 21 E 303 ALA GLY GLU VAL THR PHE VAL ASP ILE PRO GLY ASP HIS
SEQRES 22 E 303 ALA THR MET LEU ARG ALA PRO HIS VAL SER GLU VAL ALA
SEQRES 23 E 303 GLN LEU LEU ASP ARG HIS CYS GLY LEU PRO SER ASP ASP
SEQRES 24 E 303 GLY PRO ARG GLY
SEQRES 1 F 303 MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR
SEQRES 2 F 303 PHE GLN GLY GLY SER SER THR ALA GLY ASP PRO THR ALA
SEQRES 3 F 303 LYS LEU VAL ARG LEU ASN PRO ARG GLY GLY ASP GLY PRO
SEQRES 4 F 303 GLY ILE VAL PHE ALA PRO PRO ALA GLY GLY THR VAL LEU
SEQRES 5 F 303 GLY TYR ILE GLU LEU ALA ARG HIS LEU LYS GLY PHE GLY
SEQRES 6 F 303 GLU ILE HIS GLY VAL GLU ALA PRO GLY LEU GLY ALA GLY
SEQRES 7 F 303 GLU THR PRO VAL TYR PRO SER PHE GLU GLU MET VAL GLN
SEQRES 8 F 303 PHE CYS SER ASP SER ALA ALA GLY VAL ALA GLY ASP GLY
SEQRES 9 F 303 VAL TYR ILE GLY GLY HIS DPP LEU GLY GLY HIS ILE ALA
SEQRES 10 F 303 PHE TYR LEU ALA THR MET LEU LEU ASP ARG GLY ILE ARG
SEQRES 11 F 303 PRO LYS GLY LEU ILE ILE LEU ASP THR PRO PRO ARG LEU
SEQRES 12 F 303 GLY ASP ILE PRO VAL ALA ASP ALA ASP LEU THR GLU GLU
SEQRES 13 F 303 GLU THR LYS VAL PHE ILE LEU ALA MET GLY ILE GLY GLY
SEQRES 14 F 303 MET LEU ASP GLN ASP ARG ASP ALA LEU LYS ASP LEU PRO
SEQRES 15 F 303 TYR GLU GLU ALA LYS GLN LEU LEU LEU ASP ARG ALA LYS
SEQRES 16 F 303 ASN ASP PRO ARG VAL SER ALA PHE LEU SER GLU ASP TYR
SEQRES 17 F 303 LEU ASP ARG PHE LEU ARG LEU GLN MET HIS GLN LEU MET
SEQRES 18 F 303 TYR SER ARG ASP VAL VAL LEU PRO GLN ARG LYS LEU ASP
SEQRES 19 F 303 ILE PRO ILE HIS VAL PHE ARG THR LYS ASN HIS ALA PRO
SEQRES 20 F 303 GLU VAL ALA ARG LEU PHE SER ALA TRP GLU ASN TYR ALA
SEQRES 21 F 303 ALA GLY GLU VAL THR PHE VAL ASP ILE PRO GLY ASP HIS
SEQRES 22 F 303 ALA THR MET LEU ARG ALA PRO HIS VAL SER GLU VAL ALA
SEQRES 23 F 303 GLN LEU LEU ASP ARG HIS CYS GLY LEU PRO SER ASP ASP
SEQRES 24 F 303 GLY PRO ARG GLY
SEQRES 1 G 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
SEQRES 1 I 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
SEQRES 1 H 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
SEQRES 1 K 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
SEQRES 1 J 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
SEQRES 1 L 12 VAD DVA 2OP VAL VAD DVA 2OP VAL VAD DVA 2OP VAL
MODRES 6ECF DPP A 2463 SER MODIFIED RESIDUE
MODRES 6ECF DPP B 2463 SER MODIFIED RESIDUE
MODRES 6ECF DPP C 2463 SER MODIFIED RESIDUE
MODRES 6ECF DPP D 2463 SER MODIFIED RESIDUE
MODRES 6ECF DPP E 2463 SER MODIFIED RESIDUE
MODRES 6ECF DPP F 2463 SER MODIFIED RESIDUE
HET DPP A2463 10
HET DPP B2463 10
HET DPP C2463 10
HET DPP D2463 10
HET DPP E2463 10
HET DPP F2463 10
HET VAD G3009 16
HET DVA G3010 15
HET 2OP G3011 9
HET DVA I3010 16
HET 2OP I3011 9
HET 2OP H3011 9
HET 2OP K3011 9
HET 2OP J3011 9
HET 2OP L3011 9
HETNAM DPP DIAMINOPROPANOIC ACID
HETNAM VAD DEAMINOHYDROXYVALINE
HETNAM DVA D-VALINE
HETNAM 2OP (2S)-2-HYDROXYPROPANOIC ACID
FORMUL 1 DPP 6(C3 H8 N2 O2)
FORMUL 7 VAD C5 H10 O3
FORMUL 7 DVA 2(C5 H11 N O2)
FORMUL 7 2OP 6(C3 H6 O3)
FORMUL 13 HOH *206(H2 O)
HELIX 1 AA1 ASP A 2375 ALA A 2378 5 4
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 ALA A 2450 1 14
HELIX 5 AA5 GLY A 2451 VAL A 2452 5 2
HELIX 6 AA6 ALA A 2453 ASP A 2455 5 3
HELIX 7 AA7 DPP A 2463 ARG A 2479 1 17
HELIX 8 AA8 GLU A 2507 MET A 2517 1 11
HELIX 9 AA9 PRO A 2534 ASP A 2549 1 16
HELIX 10 AB1 ASP A 2549 LEU A 2556 1 8
HELIX 11 AB2 SER A 2557 SER A 2575 1 19
HELIX 12 AB3 ARG A 2576 VAL A 2578 5 3
HELIX 13 AB4 ALA A 2598 ARG A 2603 1 6
HELIX 14 AB5 LEU A 2604 ALA A 2612 5 9
HELIX 15 AB6 ALA A 2626 ARG A 2630 5 5
HELIX 16 AB7 PRO A 2632 CYS A 2645 1 14
HELIX 17 AB8 PRO B 2376 ALA B 2378 5 3
HELIX 18 AB9 VAL B 2403 GLY B 2405 5 3
HELIX 19 AC1 TYR B 2406 LEU B 2413 1 8
HELIX 20 AC2 SER B 2437 GLY B 2454 1 18
HELIX 21 AC3 DPP B 2463 ASP B 2478 1 16
HELIX 22 AC4 GLU B 2507 GLY B 2518 1 12
HELIX 23 AC5 PRO B 2534 ASP B 2549 1 16
HELIX 24 AC6 ASP B 2549 LEU B 2556 1 8
HELIX 25 AC7 SER B 2557 TYR B 2574 1 18
HELIX 26 AC8 SER B 2575 VAL B 2578 5 4
HELIX 27 AC9 ALA B 2598 ARG B 2603 1 6
HELIX 28 AD1 LEU B 2604 ALA B 2612 5 9
HELIX 29 AD2 ALA B 2626 ARG B 2630 5 5
HELIX 30 AD3 HIS B 2633 CYS B 2645 1 13
HELIX 31 AD4 PRO C 2376 ALA C 2378 5 3
HELIX 32 AD5 VAL C 2403 GLY C 2405 5 3
HELIX 33 AD6 TYR C 2406 LEU C 2413 1 8
HELIX 34 AD7 SER C 2437 ALA C 2450 1 14
HELIX 35 AD8 GLY C 2451 ASP C 2455 5 5
HELIX 36 AD9 DPP C 2463 ARG C 2479 1 17
HELIX 37 AE1 GLU C 2508 MET C 2517 1 10
HELIX 38 AE2 PRO C 2534 ASP C 2549 1 16
HELIX 39 AE3 ASP C 2549 LEU C 2556 1 8
HELIX 40 AE4 SER C 2557 TYR C 2574 1 18
HELIX 41 AE5 ALA C 2598 ARG C 2603 1 6
HELIX 42 AE6 LEU C 2604 ALA C 2612 5 9
HELIX 43 AE7 ALA C 2626 ARG C 2630 5 5
HELIX 44 AE8 HIS C 2633 GLY C 2646 1 14
HELIX 45 AE9 VAL D 2403 GLY D 2405 5 3
HELIX 46 AF1 TYR D 2406 HIS D 2412 1 7
HELIX 47 AF2 SER D 2437 ALA D 2450 1 14
HELIX 48 AF3 DPP D 2463 ARG D 2479 1 17
HELIX 49 AF4 GLU D 2507 MET D 2517 1 11
HELIX 50 AF5 ASP D 2526 LYS D 2531 1 6
HELIX 51 AF6 PRO D 2534 ASN D 2548 1 15
HELIX 52 AF7 ASP D 2549 LEU D 2556 1 8
HELIX 53 AF8 SER D 2557 ARG D 2576 1 20
HELIX 54 AF9 ALA D 2598 SER D 2606 1 9
HELIX 55 AG1 ALA D 2607 ALA D 2612 5 6
HELIX 56 AG2 ALA D 2626 ARG D 2630 5 5
HELIX 57 AG3 PRO D 2632 GLY D 2646 1 15
HELIX 58 AG4 VAL E 2403 GLY E 2405 5 3
HELIX 59 AG5 TYR E 2406 LEU E 2413 1 8
HELIX 60 AG6 SER E 2437 ALA E 2450 1 14
HELIX 61 AG7 DPP E 2463 ARG E 2479 1 17
HELIX 62 AG8 ARG E 2494 ILE E 2498 5 5
HELIX 63 AG9 GLU E 2508 MET E 2517 1 10
HELIX 64 AH1 ASP E 2526 LEU E 2533 1 8
HELIX 65 AH2 PRO E 2534 ASN E 2548 1 15
HELIX 66 AH3 ASP E 2549 LEU E 2556 1 8
HELIX 67 AH4 SER E 2557 TYR E 2574 1 18
HELIX 68 AH5 SER E 2575 VAL E 2578 5 4
HELIX 69 AH6 GLU E 2600 LEU E 2604 1 5
HELIX 70 AH7 PHE E 2605 ALA E 2612 5 8
HELIX 71 AH8 ALA E 2626 ARG E 2630 5 5
HELIX 72 AH9 HIS E 2633 GLY E 2646 1 14
HELIX 73 AI1 PRO F 2376 ALA F 2378 5 3
HELIX 74 AI2 VAL F 2403 GLY F 2405 5 3
HELIX 75 AI3 TYR F 2406 LEU F 2413 1 8
HELIX 76 AI4 SER F 2437 ALA F 2450 1 14
HELIX 77 AI5 DPP F 2463 ASP F 2478 1 16
HELIX 78 AI6 GLU F 2509 MET F 2517 1 9
HELIX 79 AI7 ASP F 2526 LEU F 2533 1 8
HELIX 80 AI8 PRO F 2534 ASN F 2548 1 15
HELIX 81 AI9 ASP F 2549 LEU F 2556 1 8
HELIX 82 AJ1 SER F 2557 TYR F 2574 1 18
HELIX 83 AJ2 ALA F 2598 ARG F 2603 1 6
HELIX 84 AJ3 LEU F 2604 ALA F 2612 5 9
HELIX 85 AJ4 ALA F 2626 ARG F 2630 5 5
HELIX 86 AJ5 PRO F 2632 CYS F 2645 1 14
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 GLY A2485 N ILE A2459
SHEET 6 AA114 ILE A2589 THR A2594 1 O HIS A2590 N LEU A2486
SHEET 7 AA114 GLU A2615 ILE A2621 1 O THR A2617 N VAL A2591
SHEET 8 AA114 VAL E2616 ILE E2621 1 O PHE E2618 N VAL A2616
SHEET 9 AA114 ILE E2589 THR E2594 1 N VAL E2591 O THR E2617
SHEET 10 AA114 GLY E2485 LEU E2489 1 N ILE E2488 O HIS E2590
SHEET 11 AA114 TYR E2458 HIS E2462 1 N ILE E2459 O ILE E2487
SHEET 12 AA114 ILE E2393 ALA E2396 1 N ALA E2396 O GLY E2460
SHEET 13 AA114 ILE E2419 VAL E2422 1 O HIS E2420 N ILE E2393
SHEET 14 AA114 LEU E2380 ARG E2382 -1 N VAL E2381 O GLY E2421
SHEET 1 AA214 LEU B2380 ASN B2384 0
SHEET 2 AA214 ILE B2419 VAL B2422 -1 O GLY B2421 N VAL B2381
SHEET 3 AA214 GLY B2392 ALA B2396 1 N ILE B2393 O HIS B2420
SHEET 4 AA214 VAL B2457 HIS B2462 1 O GLY B2460 N VAL B2394
SHEET 5 AA214 GLY B2485 LEU B2489 1 O ILE B2487 N ILE B2459
SHEET 6 AA214 ILE B2589 ARG B2593 1 O HIS B2590 N ILE B2488
SHEET 7 AA214 GLU B2615 ASP B2620 1 O THR B2617 N VAL B2591
SHEET 8 AA214 VAL F2616 ILE F2621 1 O PHE F2618 N PHE B2618
SHEET 9 AA214 ILE F2589 THR F2594 1 N VAL F2591 O THR F2617
SHEET 10 AA214 GLY F2485 LEU F2489 1 N ILE F2488 O PHE F2592
SHEET 11 AA214 TYR F2458 HIS F2462 1 N ILE F2459 O ILE F2487
SHEET 12 AA214 ILE F2393 ALA F2396 1 N VAL F2394 O GLY F2460
SHEET 13 AA214 ILE F2419 VAL F2422 1 O HIS F2420 N ILE F2393
SHEET 14 AA214 LEU F2380 ARG F2382 -1 N VAL F2381 O GLY F2421
SHEET 1 AA314 LEU C2380 ASN C2384 0
SHEET 2 AA314 ILE C2419 VAL C2422 -1 O GLY C2421 N VAL C2381
SHEET 3 AA314 GLY C2392 ALA C2396 1 N ILE C2393 O HIS C2420
SHEET 4 AA314 VAL C2457 HIS C2462 1 O TYR C2458 N VAL C2394
SHEET 5 AA314 GLY C2485 LEU C2489 1 O ILE C2487 N ILE C2459
SHEET 6 AA314 ILE C2589 THR C2594 1 O HIS C2590 N LEU C2486
SHEET 7 AA314 GLU C2615 ILE C2621 1 O THR C2617 N VAL C2591
SHEET 8 AA314 VAL D2616 ILE D2621 1 O PHE D2618 N PHE C2618
SHEET 9 AA314 ILE D2589 THR D2594 1 N VAL D2591 O THR D2617
SHEET 10 AA314 GLY D2485 LEU D2489 1 N ILE D2488 O HIS D2590
SHEET 11 AA314 VAL D2457 HIS D2462 1 N ILE D2459 O ILE D2487
SHEET 12 AA314 GLY D2392 ALA D2396 1 N GLY D2392 O TYR D2458
SHEET 13 AA314 ILE D2419 VAL D2422 1 O HIS D2420 N ILE D2393
SHEET 14 AA314 LEU D2380 ARG D2382 -1 N VAL D2381 O GLY D2421
LINK C HIS A2462 N DPP A2463 1555 1555 1.33
LINK C DPP A2463 N LEU A2464 1555 1555 1.33
LINK NG DPP A2463 C VAL G3012 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 I3012 1555 1555 1.34
LINK C HIS C2462 N DPP C2463 1555 1555 1.33
LINK C DPP C2463 N LEU C2464 1555 1555 1.33
LINK NG DPP C2463 C VAL H3012 1555 1555 1.33
LINK C HIS D2462 N DPP D2463 1555 1555 1.33
LINK C DPP D2463 N LEU D2464 1555 1555 1.33
LINK NG DPP D2463 C VAL K3012 1555 1555 1.34
LINK C HIS E2462 N DPP E2463 1555 1555 1.33
LINK C DPP E2463 N LEU E2464 1555 1555 1.33
LINK NG DPP E2463 C VAL J3012 1555 1555 1.34
LINK C HIS F2462 N DPP F2463 1555 1555 1.33
LINK C DPP F2463 N LEU F2464 1555 1555 1.33
LINK NG DPP F2463 C VAL L3012 1555 1555 1.33
LINK C VAD G3009 N DVA G3010 1555 1555 1.34
LINK C DVA G3010 OHN 2OP G3011 1555 1555 1.33
LINK C 2OP G3011 N VAL G3012 1555 1555 1.33
LINK C DVA I3010 OHN 2OP I3011 1555 1555 1.34
LINK C 2OP I3011 N VAL I3012 1555 1555 1.34
LINK C 2OP H3011 N VAL H3012 1555 1555 1.34
LINK C 2OP K3011 N VAL K3012 1555 1555 1.33
LINK C 2OP J3011 N VAL J3012 1555 1555 1.33
LINK C 2OP L3011 N VAL L3012 1555 1555 1.34
CISPEP 1 ALA A 2631 PRO A 2632 0 3.25
CISPEP 2 ALA B 2631 PRO B 2632 0 1.64
CISPEP 3 ALA C 2631 PRO C 2632 0 3.39
CISPEP 4 LEU D 2533 PRO D 2534 0 -5.60
CISPEP 5 ALA D 2631 PRO D 2632 0 2.07
CISPEP 6 LEU E 2533 PRO E 2534 0 -1.09
CISPEP 7 ALA E 2631 PRO E 2632 0 -0.71
CISPEP 8 LEU F 2533 PRO F 2534 0 -5.23
CISPEP 9 ALA F 2631 PRO F 2632 0 2.42
CRYST1 76.996 77.129 90.329 91.77 114.89 117.94 P 1 6
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 0.012988 0.006888 0.008329 0.00000
SCALE2 0.000000 0.014676 0.004355 0.00000
SCALE3 0.000000 0.000000 0.012730 0.00000
TER 3676 PRO A2648
TER 7415 SER B2649
TER 11161 PRO C2648
TER 15025 LEU D2647
TER 18784 SER E2649
TER 22606 LEU F2647
TER 22663 VAL G3012
TER 22705 VAL I3012
TER 22731 VAL H3012
TER 22757 VAL K3012
TER 22783 VAL J3012
TER 22809 VAL L3012
MASTER 737 0 15 86 42 0 0 611750 12 185 150
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