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HEADER BIOSYNTHETIC PROTEIN 14-FEB-23 8G5U
TITLE CRYSTAL STRUCTURE OF TNMK2 COMPLEXED WITH TNM B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TNMK2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. CB03234;
SOURCE 3 ORGANISM_TAXID: 1703937;
SOURCE 4 GENE: TNMK2, AMK26_32040;
SOURCE 5 EXPRESSION_SYSTEM: STREPTOMYCES LIVIDANS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1916
KEYWDS BIOSYNTHESIS, NATURAL PRODUCT, TIANCIMYCIN, ENEDIYNE, BIOSYNTHETIC
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-C.LIU,C.GUI,B.SHEN
REVDAT 1 18-OCT-23 8G5U 0
JRNL AUTH C.GUI,E.KALKREUTER,Y.-C.LIU,G.LI,B.SHEN
JRNL TITL CONSECUTIVELY-ACTING COFACTORLESS OXYGENASES GUIDE
JRNL TITL 2 ANTHRAQUINONE-FUSED ENEDIYNE BIOSYNTHESIS
JRNL REF NAT.CHEM.BIOL. 2023
JRNL REFN ESSN 1552-4469
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2689: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 217453
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) : 0.189
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.210
REMARK 3 FREE R VALUE TEST SET COUNT : 11332
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 29.6460 - 5.5933 1.00 6943 343 0.1834 0.1827
REMARK 3 2 5.5933 - 4.4444 1.00 6900 422 0.1553 0.1593
REMARK 3 3 4.4444 - 3.8840 1.00 6955 357 0.1497 0.1960
REMARK 3 4 3.8840 - 3.5295 1.00 6830 445 0.1665 0.1867
REMARK 3 5 3.5295 - 3.2768 1.00 6974 382 0.1779 0.2037
REMARK 3 6 3.2768 - 3.0839 1.00 6916 390 0.1754 0.2199
REMARK 3 7 3.0839 - 2.9296 1.00 6924 392 0.1829 0.2020
REMARK 3 8 2.9296 - 2.8021 1.00 6958 361 0.1782 0.2035
REMARK 3 9 2.8021 - 2.6943 1.00 6976 339 0.1755 0.1878
REMARK 3 10 2.6943 - 2.6014 1.00 7012 294 0.1814 0.2158
REMARK 3 11 2.6014 - 2.5201 1.00 6915 379 0.1864 0.2231
REMARK 3 12 2.5201 - 2.4481 1.00 6980 325 0.1790 0.2001
REMARK 3 13 2.4481 - 2.3837 1.00 6949 393 0.1919 0.2203
REMARK 3 14 2.3837 - 2.3256 1.00 6948 388 0.1907 0.2036
REMARK 3 15 2.3256 - 2.2727 1.00 6886 376 0.1996 0.2324
REMARK 3 16 2.2727 - 2.2244 1.00 6975 386 0.1962 0.2226
REMARK 3 17 2.2244 - 2.1799 1.00 6845 439 0.2048 0.2565
REMARK 3 18 2.1799 - 2.1388 1.00 6881 407 0.2115 0.2435
REMARK 3 19 2.1388 - 2.1006 1.00 6920 408 0.2151 0.2570
REMARK 3 20 2.1006 - 2.0650 1.00 6980 363 0.2133 0.2526
REMARK 3 21 2.0650 - 2.0317 1.00 6888 384 0.2229 0.2683
REMARK 3 22 2.0317 - 2.0004 1.00 6931 396 0.2285 0.2785
REMARK 3 23 2.0004 - 1.9710 1.00 6918 372 0.2278 0.2431
REMARK 3 24 1.9710 - 1.9433 1.00 6941 383 0.2334 0.2754
REMARK 3 25 1.9433 - 1.9170 1.00 6932 390 0.2395 0.2676
REMARK 3 26 1.9170 - 1.8921 1.00 6883 417 0.2441 0.2912
REMARK 3 27 1.8921 - 1.8685 0.97 6747 387 0.2444 0.2608
REMARK 3 28 1.8685 - 1.8460 0.96 6700 345 0.2580 0.2825
REMARK 3 29 1.8460 - 1.8245 0.95 6540 346 0.2736 0.3116
REMARK 3 30 1.8245 - 1.8040 0.86 5974 323 0.2741 0.3121
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.005 15511
REMARK 3 ANGLE : 0.823 21240
REMARK 3 CHIRALITY : 0.047 2307
REMARK 3 PLANARITY : 0.005 2820
REMARK 3 DIHEDRAL : 16.328 9222
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 8G5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1000271013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 217453
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 0.1 M
REMARK 280 IMIDAZOLE/HCL, PH 8.0, 20% W/V PEG 1000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
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 67.05500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.71422
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 118.58567
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 67.05500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 38.71422
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 118.58567
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 67.05500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 38.71422
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 118.58567
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.42844
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 237.17133
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 77.42844
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 237.17133
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 77.42844
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 237.17133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 A1194 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1196 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1197 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1186 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1189 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1191 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 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ARG A 5
REMARK 465 HIS A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 489
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ARG B 5
REMARK 465 HIS B 6
REMARK 465 GLU B 7
REMARK 465 VAL B 489
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ALA C 3
REMARK 465 ALA C 4
REMARK 465 ARG C 5
REMARK 465 HIS C 6
REMARK 465 GLU C 7
REMARK 465 VAL C 489
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 ARG D 5
REMARK 465 HIS D 6
REMARK 465 GLU D 7
REMARK 465 VAL D 489
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H ALA C 104 O HOH C 602 1.16
REMARK 500 H GLY A 36 O HOH A 604 1.35
REMARK 500 HH21 ARG D 186 O HOH D 608 1.44
REMARK 500 HE ARG B 400 O HOH B 606 1.46
REMARK 500 HH22 ARG D 479 O HOH D 605 1.46
REMARK 500 HH22 ARG C 72 O HOH C 604 1.49
REMARK 500 HH22 ARG C 479 O HOH C 613 1.51
REMARK 500 H GLY B 36 O HOH B 616 1.51
REMARK 500 O PHE A 334 H GLN A 336 1.52
REMARK 500 O PHE B 334 H GLN B 336 1.56
REMARK 500 OE2 GLU B 237 H PHE B 376 1.57
REMARK 500 HE2 HIS A 318 O HOH A 605 1.57
REMARK 500 HE2 HIS B 318 O HOH B 612 1.58
REMARK 500 HH11 ARG C 427 O HOH C 618 1.59
REMARK 500 O HOH A 823 O HOH A 952 1.76
REMARK 500 O HOH B 856 O HOH B 997 1.77
REMARK 500 O HOH A 620 O HOH A 1058 1.80
REMARK 500 O HOH C 954 O HOH C 1008 1.81
REMARK 500 O HOH D 857 O HOH D 871 1.82
REMARK 500 O HOH A 847 O HOH A 1093 1.82
REMARK 500 OG1 THR B 488 O HOH B 601 1.82
REMARK 500 O HOH C 936 O HOH C 960 1.83
REMARK 500 O HOH C 765 O HOH C 905 1.86
REMARK 500 NH1 ARG B 16 O HOH B 602 1.86
REMARK 500 O HOH A 776 O HOH A 984 1.86
REMARK 500 O HOH B 623 O HOH B 940 1.87
REMARK 500 O HOH B 1080 O HOH B 1177 1.87
REMARK 500 O HOH D 952 O HOH D 962 1.87
REMARK 500 O HOH A 998 O HOH A 1056 1.87
REMARK 500 O HOH C 937 O HOH C 943 1.89
REMARK 500 O ARG A 35 O HOH A 601 1.89
REMARK 500 O HOH A 984 O HOH A 1124 1.89
REMARK 500 O HOH D 636 O HOH D 906 1.89
REMARK 500 OE1 GLU C 279 O HOH C 601 1.90
REMARK 500 O HOH A 906 O HOH A 1053 1.91
REMARK 500 O HOH A 953 O HOH A 1095 1.92
REMARK 500 OD1 ASP D 222 O HOH D 601 1.93
REMARK 500 O HOH A 1037 O HOH A 1084 1.95
REMARK 500 O HOH A 619 O HOH A 1001 1.96
REMARK 500 O HOH B 1056 O HOH B 1171 1.96
REMARK 500 O HOH A 951 O HOH A 978 1.97
REMARK 500 NH2 ARG B 16 O HOH B 603 1.97
REMARK 500 OE1 GLU D 101 O HOH D 602 1.97
REMARK 500 O HOH D 929 O HOH D 1013 1.97
REMARK 500 N ALA C 104 O HOH C 602 1.98
REMARK 500 O HOH A 886 O HOH A 1034 1.99
REMARK 500 O HOH B 611 O HOH B 639 2.00
REMARK 500 O HOH A 1005 O HOH A 1148 2.00
REMARK 500 O HOH B 634 O HOH B 1082 2.00
REMARK 500 O HOH C 611 O HOH C 833 2.01
REMARK 500
REMARK 500 THIS ENTRY HAS 126 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 957 O HOH D 938 3565 1.67
REMARK 500 O HOH B 928 O HOH C 919 3565 1.67
REMARK 500 O HOH A 645 O HOH C 849 5555 2.00
REMARK 500 O HOH B 824 O HOH C 645 3565 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 81 -92.03 -85.22
REMARK 500 PHE A 115 10.48 88.54
REMARK 500 PHE A 132 33.29 -96.34
REMARK 500 SER A 193 -117.87 54.97
REMARK 500 ASP A 211 -86.22 -95.84
REMARK 500 SER A 217 89.93 69.42
REMARK 500 ALA A 283 -124.06 55.02
REMARK 500 HIS A 318 -78.89 -113.03
REMARK 500 PHE A 334 -103.62 -108.14
REMARK 500 ARG A 449 82.00 78.16
REMARK 500 ASP B 81 -91.27 -86.04
REMARK 500 PHE B 115 10.63 89.61
REMARK 500 PHE B 132 32.24 -94.85
REMARK 500 ALA B 159 13.65 -140.87
REMARK 500 SER B 193 -119.62 55.19
REMARK 500 ASP B 211 -85.28 -95.58
REMARK 500 SER B 217 90.19 68.51
REMARK 500 ASP B 288 -169.49 -115.91
REMARK 500 VAL B 317 -70.39 -71.53
REMARK 500 HIS B 318 -91.40 -98.97
REMARK 500 PHE B 334 -114.71 -112.65
REMARK 500 ARG B 449 81.52 77.85
REMARK 500 ASP C 81 -90.12 -83.89
REMARK 500 PHE C 115 13.13 88.68
REMARK 500 PHE C 132 32.45 -91.87
REMARK 500 ALA C 159 11.60 -142.49
REMARK 500 SER C 193 -118.63 56.73
REMARK 500 ASP C 211 -89.06 -89.10
REMARK 500 SER C 217 91.46 70.36
REMARK 500 HIS C 318 -76.53 -124.31
REMARK 500 MET C 419 -63.90 -93.54
REMARK 500 ARG C 449 80.36 80.81
REMARK 500 ALA C 483 73.76 -111.10
REMARK 500 ASP D 81 -89.97 -83.93
REMARK 500 PHE D 115 12.63 90.26
REMARK 500 PHE D 132 31.70 -93.43
REMARK 500 ALA D 159 10.97 -141.15
REMARK 500 SER D 193 -117.71 57.32
REMARK 500 ASP D 211 -89.06 -89.22
REMARK 500 SER D 217 91.39 68.79
REMARK 500 HIS D 318 -126.97 -116.81
REMARK 500 MET D 419 -64.88 -90.81
REMARK 500 ARG D 449 83.38 79.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 217 ILE A 218 -149.58
REMARK 500 GLY B 319 GLY B 320 -145.16
REMARK 500 HIS C 318 GLY C 319 -141.28
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 A1192 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A1193 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A1194 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1195 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A1196 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A1197 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A1198 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A1200 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH B1186 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B1187 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B1188 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B1189 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B1190 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B1191 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B1192 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH C1011 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH C1012 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH D1019 DISTANCE = 6.20 ANGSTROMS
DBREF1 8G5U A 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5U A A0A125SA15 1 489
DBREF1 8G5U B 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5U B A0A125SA15 1 489
DBREF1 8G5U C 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5U C A0A125SA15 1 489
DBREF1 8G5U D 1 489 UNP A0A125SA15_9ACTN
DBREF2 8G5U D A0A125SA15 1 489
SEQRES 1 A 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 A 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 A 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 A 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 A 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 A 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 A 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 A 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 A 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 A 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 A 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 A 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 A 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 A 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 A 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 A 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 A 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 A 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 A 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 A 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 A 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 A 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 A 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 A 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 A 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 A 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 A 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 A 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 A 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 A 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 A 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 A 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 A 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 A 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 A 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 A 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 A 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 A 489 PRO ALA PRO MET VAL PRO THR VAL
SEQRES 1 B 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 B 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 B 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 B 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 B 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 B 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 B 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 B 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 B 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 B 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 B 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 B 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 B 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 B 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 B 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 B 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 B 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 B 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 B 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 B 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 B 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 B 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 B 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 B 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 B 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 B 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 B 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 B 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 B 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 B 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 B 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 B 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 B 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 B 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 B 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 B 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 B 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 B 489 PRO ALA PRO MET VAL PRO THR VAL
SEQRES 1 C 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 C 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 C 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 C 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 C 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 C 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 C 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 C 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 C 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 C 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 C 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 C 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 C 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 C 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 C 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 C 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 C 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 C 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 C 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 C 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 C 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 C 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 C 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 C 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 C 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 C 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 C 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 C 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 C 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 C 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 C 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 C 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 C 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 C 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 C 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 C 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 C 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 C 489 PRO ALA PRO MET VAL PRO THR VAL
SEQRES 1 D 489 MET THR ALA ALA ARG HIS GLU PRO HIS LEU LEU THR ASP
SEQRES 2 D 489 ALA VAL ARG ALA PHE GLN ALA GLN SER PRO VAL TRP ARG
SEQRES 3 D 489 PRO ALA ASP ASP GLU GLU ALA LEU ARG GLY LEU GLU ALA
SEQRES 4 D 489 ALA GLU LEU THR VAL PRO LEU ASP TYR ARG ALA PRO ALA
SEQRES 5 D 489 GLY ARG THR LEU THR LEU GLY LEU VAL ARG HIS ARG ALA
SEQRES 6 D 489 THR ALA PRO GLU ARG ARG ARG GLY VAL LEU LEU VAL GLY
SEQRES 7 D 489 PRO GLY ASP ASP LEU GLY ASN ARG GLY THR LEU LEU GLY
SEQRES 8 D 489 ALA GLN LEU VAL GLY GLN LEU PRO LYS GLU VAL LEU ALA
SEQRES 9 D 489 GLN TYR ASP VAL VAL ALA PHE ASP HIS ARG PHE MET GLY
SEQRES 10 D 489 ARG SER SER PRO VAL VAL CYS GLY LEU GLU PRO GLU GLU
SEQRES 11 D 489 ARG PHE TRP VAL PHE HIS HIS PRO ARG ASP PHE ASP HIS
SEQRES 12 D 489 GLU VAL ARG PHE GLN ALA ASN VAL ALA ALA LYS VAL ALA
SEQRES 13 D 489 GLU HIS ALA LEU ASP ILE LEU PRO TYR ALA SER SER ARG
SEQRES 14 D 489 ASN ILE ALA ARG ASP ILE GLU VAL ILE ARG GLY ALA LEU
SEQRES 15 D 489 GLY GLU ASP ARG ILE SER TYR LEU GLY TYR SER TYR GLY
SEQRES 16 D 489 THR TYR LEU GLY ALA VAL TRP THR GLN MET PHE GLY GLU
SEQRES 17 D 489 HIS ALA ASP ARG VAL VAL LEU ASP SER ILE CYS SER PRO
SEQRES 18 D 489 ASP TRP VAL TRP ARG GLY LEU PHE THR ASP PHE PRO PRO
SEQRES 19 D 489 ASN GLY GLU ARG ALA LEU THR ARG TRP ALA ARG TRP ALA
SEQRES 20 D 489 ALA ALA ARG ASP ALA ASP LEU GLY LEU GLY ALA THR ASP
SEQRES 21 D 489 GLY ALA VAL ARG ALA ALA TYR ASP GLY VAL LEU ALA ARG
SEQRES 22 D 489 VAL ASP THR ASP ARG GLU VAL THR VAL ALA GLY PHE PRO
SEQRES 23 D 489 LEU ASP ARG THR LEU ALA ARG LEU ILE VAL VAL GLY MET
SEQRES 24 D 489 LEU ASN SER ASP ARG ASN TYR PRO PHE LEU GLY ASP ILE
SEQRES 25 D 489 VAL ARG SER ALA VAL HIS GLY GLY GLN LEU GLU PRO ALA
SEQRES 26 D 489 THR MET GLY PHE LEU GLY GLN MET PHE GLY GLN PRO LYS
SEQRES 27 D 489 GLU GLU SER GLY THR VAL ALA GLN LEU ALA ILE LEU ALA
SEQRES 28 D 489 GLY ASP TRP ALA TRP PRO ARG ASN VAL ASP LEU TYR GLU
SEQRES 29 D 489 ARG ASP MET GLU ARG ALA SER ARG THR HIS PRO PHE THR
SEQRES 30 D 489 GLY ALA ALA MET ALA GLY ILE LYS ALA PRO ALA PHE TRP
SEQRES 31 D 489 PRO VAL PRO PRO SER GLU PRO VAL THR ARG LEU GLY PRO
SEQRES 32 D 489 ASP ASN PRO ALA ASP SER ILE LEU LEU VAL GLN ALA ALA
SEQRES 33 D 489 ASP ASP MET SER THR PRO LEU ALA ALA ALA ARG ARG MET
SEQRES 34 D 489 ARG GLU VAL LEU GLY ASP THR SER ARG LEU LEU THR VAL
SEQRES 35 D 489 ALA ASP THR ALA HIS HIS ARG VAL PHE PRO PHE TYR GLY
SEQRES 36 D 489 ASN PRO GLY ALA ASP GLU LEU VAL THR ALA TYR LEU VAL
SEQRES 37 D 489 ASP GLY GLU LEU PRO ALA ALA ASP VAL THR ARG PRO ASN
SEQRES 38 D 489 PRO ALA PRO MET VAL PRO THR VAL
HET 9VG A 501 56
HET 9VG B 501 56
HET 9VG C 501 56
HET 9VG D 501 56
HETNAM 9VG METHYL (2E)-3-[(1AS,11S,11AS,14Z,18R)-3,18-DIHYDROXY-4,
HETNAM 2 9VG 9-DIOXO-4,9,10,11-TETRAHYDRO-11AH-11,1A-HEPT[3]ENE[1,
HETNAM 3 9VG 5]DIYNONAPHTHO[2,3-H]OXIRENO[C]QUINOLIN-11A-YL]BUT-2-
HETNAM 4 9VG ENOATE
FORMUL 5 9VG 4(C29 H19 N O7)
FORMUL 9 HOH *2023(H2 O)
HELIX 1 AA1 LEU A 11 GLN A 19 1 9
HELIX 2 AA2 GLU A 31 ARG A 35 5 5
HELIX 3 AA3 ALA A 67 ARG A 71 5 5
HELIX 4 AA4 ARG A 86 LEU A 98 1 13
HELIX 5 AA5 PRO A 99 GLN A 105 1 7
HELIX 6 AA6 GLU A 127 TRP A 133 5 7
HELIX 7 AA7 ASP A 140 LEU A 160 1 21
HELIX 8 AA8 ILE A 162 ALA A 166 5 5
HELIX 9 AA9 SER A 167 GLY A 183 1 17
HELIX 10 AB1 SER A 193 GLY A 207 1 15
HELIX 11 AB2 TRP A 225 ASP A 231 1 7
HELIX 12 AB3 ASP A 231 ALA A 249 1 19
HELIX 13 AB4 ARG A 250 GLY A 255 1 6
HELIX 14 AB5 THR A 259 ASP A 275 1 17
HELIX 15 AB6 THR A 290 ASN A 301 1 12
HELIX 16 AB7 SER A 302 ARG A 304 5 3
HELIX 17 AB8 ASN A 305 HIS A 318 1 14
HELIX 18 AB9 GLU A 323 PHE A 334 1 12
HELIX 19 AC1 GLU A 339 ASP A 353 1 15
HELIX 20 AC2 ASN A 359 HIS A 374 1 16
HELIX 21 AC3 THR A 377 GLY A 383 1 7
HELIX 22 AC4 LYS A 385 TRP A 390 5 6
HELIX 23 AC5 PRO A 422 GLY A 434 1 13
HELIX 24 AC6 ASN A 456 GLY A 470 1 15
HELIX 25 AC7 LEU B 11 GLN B 19 1 9
HELIX 26 AC8 GLU B 31 ARG B 35 5 5
HELIX 27 AC9 ALA B 67 ARG B 71 5 5
HELIX 28 AD1 ARG B 86 LEU B 98 1 13
HELIX 29 AD2 PRO B 99 GLN B 105 1 7
HELIX 30 AD3 PRO B 128 TRP B 133 5 6
HELIX 31 AD4 ASP B 140 LEU B 160 1 21
HELIX 32 AD5 ILE B 162 ALA B 166 5 5
HELIX 33 AD6 SER B 167 LEU B 182 1 16
HELIX 34 AD7 SER B 193 GLY B 207 1 15
HELIX 35 AD8 ARG B 226 ASP B 231 1 6
HELIX 36 AD9 ASP B 231 ALA B 249 1 19
HELIX 37 AE1 ARG B 250 GLY B 255 1 6
HELIX 38 AE2 THR B 259 ASP B 275 1 17
HELIX 39 AE3 THR B 290 LEU B 300 1 11
HELIX 40 AE4 ASN B 301 ARG B 304 5 4
HELIX 41 AE5 ASN B 305 HIS B 318 1 14
HELIX 42 AE6 GLU B 323 PHE B 334 1 12
HELIX 43 AE7 GLU B 339 ASP B 353 1 15
HELIX 44 AE8 ASN B 359 HIS B 374 1 16
HELIX 45 AE9 THR B 377 GLY B 383 1 7
HELIX 46 AF1 LYS B 385 TRP B 390 5 6
HELIX 47 AF2 PRO B 422 GLY B 434 1 13
HELIX 48 AF3 ASN B 456 GLY B 470 1 15
HELIX 49 AF4 LEU C 11 ALA C 20 1 10
HELIX 50 AF5 GLU C 31 ARG C 35 5 5
HELIX 51 AF6 ARG C 86 LEU C 98 1 13
HELIX 52 AF7 PRO C 99 GLN C 105 1 7
HELIX 53 AF8 GLU C 127 PHE C 132 1 6
HELIX 54 AF9 ASP C 140 LEU C 160 1 21
HELIX 55 AG1 ILE C 162 ALA C 166 5 5
HELIX 56 AG2 SER C 167 LEU C 182 1 16
HELIX 57 AG3 SER C 193 GLY C 207 1 15
HELIX 58 AG4 SER C 220 VAL C 224 5 5
HELIX 59 AG5 ARG C 226 ASP C 231 1 6
HELIX 60 AG6 ASP C 231 ALA C 249 1 19
HELIX 61 AG7 ARG C 250 GLY C 255 1 6
HELIX 62 AG8 THR C 259 ASP C 275 1 17
HELIX 63 AG9 THR C 290 LEU C 300 1 11
HELIX 64 AH1 ASN C 301 ARG C 304 5 4
HELIX 65 AH2 ASN C 305 HIS C 318 1 14
HELIX 66 AH3 GLU C 323 GLY C 335 1 13
HELIX 67 AH4 GLU C 339 ASP C 353 1 15
HELIX 68 AH5 ASN C 359 HIS C 374 1 16
HELIX 69 AH6 THR C 377 GLY C 383 1 7
HELIX 70 AH7 LYS C 385 TRP C 390 5 6
HELIX 71 AH8 PRO C 422 GLY C 434 1 13
HELIX 72 AH9 ASN C 456 GLY C 470 1 15
HELIX 73 AI1 LEU D 11 ALA D 20 1 10
HELIX 74 AI2 GLU D 31 ARG D 35 5 5
HELIX 75 AI3 ARG D 86 LEU D 98 1 13
HELIX 76 AI4 PRO D 99 GLN D 105 1 7
HELIX 77 AI5 GLU D 127 PHE D 132 1 6
HELIX 78 AI6 ASP D 140 LEU D 160 1 21
HELIX 79 AI7 ILE D 162 ALA D 166 5 5
HELIX 80 AI8 SER D 167 LEU D 182 1 16
HELIX 81 AI9 SER D 193 GLY D 207 1 15
HELIX 82 AJ1 SER D 220 VAL D 224 5 5
HELIX 83 AJ2 ARG D 226 ASP D 231 1 6
HELIX 84 AJ3 ASP D 231 ALA D 249 1 19
HELIX 85 AJ4 ARG D 250 GLY D 255 1 6
HELIX 86 AJ5 THR D 259 ASP D 275 1 17
HELIX 87 AJ6 THR D 290 LEU D 300 1 11
HELIX 88 AJ7 ASN D 301 ARG D 304 5 4
HELIX 89 AJ8 ASN D 305 HIS D 318 1 14
HELIX 90 AJ9 GLU D 323 GLY D 335 1 13
HELIX 91 AK1 GLU D 339 ASP D 353 1 15
HELIX 92 AK2 ASN D 359 HIS D 374 1 16
HELIX 93 AK3 THR D 377 GLY D 383 1 7
HELIX 94 AK4 LYS D 385 TRP D 390 5 6
HELIX 95 AK5 PRO D 422 GLY D 434 1 13
HELIX 96 AK6 ASN D 456 GLY D 470 1 15
SHEET 1 AA110 ARG A 26 PRO A 27 0
SHEET 2 AA110 GLU A 38 PRO A 45 -1 O ALA A 39 N ARG A 26
SHEET 3 AA110 THR A 55 HIS A 63 -1 O LEU A 60 N ALA A 40
SHEET 4 AA110 TYR A 106 PHE A 111 -1 O VAL A 108 N HIS A 63
SHEET 5 AA110 GLY A 73 VAL A 77 1 N VAL A 77 O VAL A 109
SHEET 6 AA110 ILE A 187 TYR A 192 1 O SER A 188 N LEU A 76
SHEET 7 AA110 ALA A 210 ASP A 216 1 O VAL A 214 N TYR A 189
SHEET 8 AA110 ILE A 410 ALA A 415 1 O LEU A 411 N VAL A 213
SHEET 9 AA110 SER A 437 VAL A 442 1 O ARG A 438 N LEU A 412
SHEET 10 AA110 VAL A 477 ARG A 479 1 O VAL A 477 N THR A 441
SHEET 1 AA2 2 THR A 281 VAL A 282 0
SHEET 2 AA2 2 PHE A 285 PRO A 286 -1 O PHE A 285 N VAL A 282
SHEET 1 AA310 ARG B 26 PRO B 27 0
SHEET 2 AA310 GLU B 38 PRO B 45 -1 O ALA B 39 N ARG B 26
SHEET 3 AA310 THR B 55 HIS B 63 -1 O LEU B 60 N ALA B 40
SHEET 4 AA310 TYR B 106 PHE B 111 -1 O VAL B 108 N HIS B 63
SHEET 5 AA310 GLY B 73 VAL B 77 1 N LEU B 75 O ASP B 107
SHEET 6 AA310 ILE B 187 TYR B 192 1 O SER B 188 N LEU B 76
SHEET 7 AA310 ALA B 210 ASP B 216 1 O VAL B 214 N TYR B 189
SHEET 8 AA310 ILE B 410 ALA B 415 1 O LEU B 411 N VAL B 213
SHEET 9 AA310 SER B 437 VAL B 442 1 O ARG B 438 N LEU B 412
SHEET 10 AA310 VAL B 477 ARG B 479 1 O VAL B 477 N THR B 441
SHEET 1 AA4 2 THR B 281 VAL B 282 0
SHEET 2 AA4 2 PHE B 285 PRO B 286 -1 O PHE B 285 N VAL B 282
SHEET 1 AA510 ARG C 26 PRO C 27 0
SHEET 2 AA510 GLU C 38 PRO C 45 -1 O ALA C 39 N ARG C 26
SHEET 3 AA510 THR C 55 HIS C 63 -1 O LEU C 60 N ALA C 40
SHEET 4 AA510 TYR C 106 PHE C 111 -1 O VAL C 108 N HIS C 63
SHEET 5 AA510 GLY C 73 VAL C 77 1 N LEU C 75 O ASP C 107
SHEET 6 AA510 ILE C 187 TYR C 192 1 O SER C 188 N LEU C 76
SHEET 7 AA510 ALA C 210 ASP C 216 1 O VAL C 214 N TYR C 189
SHEET 8 AA510 ILE C 410 ALA C 415 1 O LEU C 411 N VAL C 213
SHEET 9 AA510 SER C 437 VAL C 442 1 O ARG C 438 N LEU C 412
SHEET 10 AA510 VAL C 477 ARG C 479 1 O VAL C 477 N THR C 441
SHEET 1 AA6 2 THR C 281 VAL C 282 0
SHEET 2 AA6 2 PHE C 285 PRO C 286 -1 O PHE C 285 N VAL C 282
SHEET 1 AA710 ARG D 26 PRO D 27 0
SHEET 2 AA710 GLU D 38 PRO D 45 -1 O ALA D 39 N ARG D 26
SHEET 3 AA710 THR D 55 HIS D 63 -1 O LEU D 60 N ALA D 40
SHEET 4 AA710 TYR D 106 PHE D 111 -1 O VAL D 108 N HIS D 63
SHEET 5 AA710 GLY D 73 VAL D 77 1 N LEU D 75 O ASP D 107
SHEET 6 AA710 ILE D 187 TYR D 192 1 O SER D 188 N LEU D 76
SHEET 7 AA710 ALA D 210 ASP D 216 1 O VAL D 214 N TYR D 189
SHEET 8 AA710 ILE D 410 ALA D 415 1 O LEU D 411 N VAL D 213
SHEET 9 AA710 SER D 437 VAL D 442 1 O ARG D 438 N LEU D 412
SHEET 10 AA710 VAL D 477 ARG D 479 1 O VAL D 477 N THR D 441
CISPEP 1 VAL A 224 TRP A 225 0 -19.79
CISPEP 2 PHE A 451 PRO A 452 0 -4.28
CISPEP 3 VAL B 224 TRP B 225 0 -20.15
CISPEP 4 PHE B 451 PRO B 452 0 -5.64
CISPEP 5 VAL C 224 TRP C 225 0 -15.88
CISPEP 6 PHE C 451 PRO C 452 0 -4.60
CISPEP 7 VAL D 224 TRP D 225 0 -15.78
CISPEP 8 PHE D 451 PRO D 452 0 -4.98
CRYST1 134.110 134.110 355.757 90.00 90.00 120.00 H 3 36
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 0.007457 0.004305 0.000000 0.00000
SCALE2 0.000000 0.008610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002811 0.00000
TER 7402 THR A 488
TER 14804 THR B 488
TER 22197 THR C 488
TER 29589 THR D 488
MASTER 505 0 4 96 46 0 0 617031 4 224 152
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