6t70-pdb | HEADER HYDROLASE 20-OCT-19 6T70
TITLE STRUCTURE OF THE BOTTROMYCIN EPIMERASE BOTH IN COMPLEX WITH
TITLE 2 BOTTROMYCIN A2 DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOTH;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. BC16019;
SOURCE 3 ORGANISM_TAXID: 1109705;
SOURCE 4 GENE: BOTH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2
KEYWDS BOTTROMYCIN, RIPP, EPIMERASE, ABH, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KOEHNKE,A.SIKANDAR
REVDAT 1 15-JUL-20 6T70 0
JRNL AUTH A.SIKANDAR,L.FRANZ,S.ADAM,J.SANTOS-ABERTURAS,L.HORBAL,
JRNL AUTH 2 A.LUZHETSKYY,A.W.TRUMAN,O.V.KALININA,J.KOEHNKE
JRNL TITL THE BOTTROMYCIN EPIMERASE BOTH DEFINES A GROUP OF ATYPICAL
JRNL TITL 2 ALPHA / BETA-HYDROLASE-FOLD ENZYMES.
JRNL REF NAT.CHEM.BIOL. 2020
JRNL REFN ESSN 1552-4469
JRNL PMID 32601484
JRNL DOI 10.1038/S41589-020-0569-Y
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,
REMARK 1 AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,
REMARK 1 AUTH 3 P.H.ZWART,P.D.ADAMS
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR. D BIOL. V. 68 352 2012
REMARK 1 REF 2 CRYSTALLOGR.
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 22505256
REMARK 1 DOI 10.1107/S0907444912001308
REMARK 2
REMARK 2 RESOLUTION. 1.58 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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 32377
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1648
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 44.2200 - 3.6200 0.99 2695 152 0.1568 0.1934
REMARK 3 2 3.6200 - 2.8700 0.99 2595 137 0.1540 0.1667
REMARK 3 3 2.8700 - 2.5100 1.00 2561 153 0.1518 0.1836
REMARK 3 4 2.5100 - 2.2800 1.00 2554 131 0.1562 0.2000
REMARK 3 5 2.2800 - 2.1200 1.00 2578 135 0.1579 0.2160
REMARK 3 6 2.1200 - 1.9900 1.00 2540 133 0.1611 0.1842
REMARK 3 7 1.9900 - 1.8900 1.00 2547 123 0.1749 0.2257
REMARK 3 8 1.8900 - 1.8100 1.00 2564 142 0.1909 0.2171
REMARK 3 9 1.8100 - 1.7400 1.00 2534 129 0.2042 0.2409
REMARK 3 10 1.7400 - 1.6800 1.00 2544 126 0.2194 0.2758
REMARK 3 11 1.6800 - 1.6300 1.00 2495 148 0.2373 0.2565
REMARK 3 12 1.6300 - 1.5800 1.00 2522 139 0.2392 0.3021
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) : 0.151
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.026
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.65
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 : 0.012 2057
REMARK 3 ANGLE : 1.254 2791
REMARK 3 CHIRALITY : 0.066 294
REMARK 3 PLANARITY : 0.008 375
REMARK 3 DIHEDRAL : 14.659 1175
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9014 -8.1231 -11.3881
REMARK 3 T TENSOR
REMARK 3 T11: 0.1111 T22: 0.1366
REMARK 3 T33: 0.1076 T12: 0.0099
REMARK 3 T13: -0.0036 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.1900 L22: 3.4708
REMARK 3 L33: 1.0571 L12: 0.2724
REMARK 3 L13: -0.3025 L23: -0.1929
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: -0.0499 S13: -0.0281
REMARK 3 S21: 0.0988 S22: -0.0122 S23: 0.1044
REMARK 3 S31: 0.0567 S32: -0.0382 S33: -0.0025
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1178 -5.2138 -5.0242
REMARK 3 T TENSOR
REMARK 3 T11: 0.1379 T22: 0.1123
REMARK 3 T33: 0.0979 T12: 0.0224
REMARK 3 T13: -0.0158 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 7.2975 L22: 4.4844
REMARK 3 L33: 6.8413 L12: -0.8861
REMARK 3 L13: -1.2539 L23: -0.6561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0729 S12: -0.3716 S13: -0.0002
REMARK 3 S21: 0.2610 S22: -0.0960 S23: 0.0369
REMARK 3 S31: 0.1364 S32: 0.3152 S33: 0.0928
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6091 -6.4975 -21.8593
REMARK 3 T TENSOR
REMARK 3 T11: 0.1466 T22: 0.1476
REMARK 3 T33: 0.1416 T12: 0.0042
REMARK 3 T13: 0.0071 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 1.7726 L22: 1.3108
REMARK 3 L33: 0.1059 L12: -0.5135
REMARK 3 L13: 0.1913 L23: -0.1481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: 0.1884 S13: 0.0620
REMARK 3 S21: -0.1087 S22: -0.0340 S23: -0.1228
REMARK 3 S31: -0.0143 S32: 0.0752 S33: 0.0311
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7942 -9.5753 -27.5513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1284 T22: 0.1468
REMARK 3 T33: 0.1488 T12: -0.0165
REMARK 3 T13: -0.0171 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 4.1111 L22: 5.9558
REMARK 3 L33: 9.5429 L12: -4.7845
REMARK 3 L13: -4.9217 L23: 6.9820
REMARK 3 S TENSOR
REMARK 3 S11: -0.0633 S12: 0.1983 S13: -0.1977
REMARK 3 S21: -0.1290 S22: -0.1040 S23: 0.1451
REMARK 3 S31: 0.2515 S32: -0.1865 S33: 0.1760
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3066 -3.6917 -16.2385
REMARK 3 T TENSOR
REMARK 3 T11: 0.1581 T22: 0.1413
REMARK 3 T33: 0.1347 T12: -0.0041
REMARK 3 T13: 0.0044 T23: -0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 8.0395 L22: 8.4218
REMARK 3 L33: 6.1305 L12: -7.1994
REMARK 3 L13: 6.2517 L23: -6.4175
REMARK 3 S TENSOR
REMARK 3 S11: -0.1569 S12: -0.0430 S13: 0.3928
REMARK 3 S21: 0.1254 S22: -0.0162 S23: -0.5405
REMARK 3 S31: -0.0895 S32: 0.1096 S33: 0.1487
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3467 -19.6350 -21.9236
REMARK 3 T TENSOR
REMARK 3 T11: 0.1291 T22: 0.0938
REMARK 3 T33: 0.1489 T12: 0.0493
REMARK 3 T13: 0.0240 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 7.1690 L22: 3.4555
REMARK 3 L33: 6.2621 L12: 3.0117
REMARK 3 L13: 3.2525 L23: 2.6325
REMARK 3 S TENSOR
REMARK 3 S11: -0.1065 S12: 0.1549 S13: -0.0634
REMARK 3 S21: -0.0937 S22: 0.1300 S23: -0.2266
REMARK 3 S31: 0.0370 S32: 0.1398 S33: -0.0313
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2569 -23.2017 -19.6032
REMARK 3 T TENSOR
REMARK 3 T11: 0.1854 T22: 0.0900
REMARK 3 T33: 0.1447 T12: 0.0079
REMARK 3 T13: 0.0242 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 4.2576 L22: 7.4512
REMARK 3 L33: 3.7576 L12: 1.7303
REMARK 3 L13: -2.1124 L23: -5.1162
REMARK 3 S TENSOR
REMARK 3 S11: -0.1683 S12: -0.0125 S13: -0.2077
REMARK 3 S21: -0.2764 S22: 0.0674 S23: -0.0693
REMARK 3 S31: 0.1906 S32: -0.0399 S33: 0.0550
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 6T70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104928.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-18
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000031
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 44.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.71200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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: 6T6H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, AMMONIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 1.000000 0.000000 0.000000 33.27200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.71500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.22200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.27200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.71500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.22200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.27200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.71500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.22200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.27200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.71500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 44.22200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN A 304 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 463 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 490 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 551 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 559 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 575 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 583 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 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 VAL A 1
REMARK 465 ARG A 2
REMARK 465 ASP A 3
REMARK 465 GLY A 4
REMARK 465 ASN A 5
REMARK 465 GLY A 6
REMARK 465 THR A 7
REMARK 465 SER A 8
REMARK 465 ARG A 9
REMARK 465 GLU A 263
REMARK 465 GLY A 264
REMARK 465 GLY A 265
REMARK 465 HIS A 266
REMARK 465 GLY A 267
REMARK 465 THR A 268
REMARK 465 GLY A 269
REMARK 465 ASP A 270
REMARK 465 ALA A 271
REMARK 465 PRO A 272
REMARK 465 ALA A 273
REMARK 465 GLU A 274
REMARK 465 ALA A 275
REMARK 465 ARG A 276
REMARK 465 THR A 277
REMARK 465 THR A 278
REMARK 465 GLY A 279
REMARK 465 ASP A 280
REMARK 465 ALA A 281
REMARK 465 PRO A 282
REMARK 465 ALA A 283
REMARK 465 GLU A 284
REMARK 465 ALA A 285
REMARK 465 ARG A 286
REMARK 465 ALA A 287
REMARK 465 SER A 288
REMARK 465 GLY A 289
REMARK 465 THR A 290
REMARK 465 GLY A 291
REMARK 465 VAL A 292
REMARK 465 VAL A 293
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 HE ARG A 102 O HOH A 402 1.44
REMARK 500 HH11 ARG A 100 O HOH A 401 1.50
REMARK 500 HH21 ARG A 10 O HOH A 403 1.51
REMARK 500 NH1 ARG A 100 O HOH A 401 1.91
REMARK 500 NE ARG A 102 O HOH A 402 2.00
REMARK 500 O HOH A 403 O HOH A 505 2.10
REMARK 500 O HOH A 539 O HOH A 582 2.11
REMARK 500 NH2 ARG A 10 O HOH A 403 2.13
REMARK 500 NH2 ARG A 102 O HOH A 402 2.14
REMARK 500 OE1 GLU A 146 O HOH A 404 2.15
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 HE ARG A 199 HE ARG A 199 2555 1.31
REMARK 500 O HOH A 566 O HOH A 591 8544 1.90
REMARK 500 O HOH A 584 O HOH A 599 2455 2.08
REMARK 500 O HOH A 585 O HOH A 601 8444 2.13
REMARK 500 O HOH A 485 O HOH A 485 4555 2.17
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 ALA A 42 37.87 -99.95
REMARK 500 VAL A 76 -70.99 -124.90
REMARK 500 PHE A 109 -126.15 59.46
REMARK 500 HIS A 195 59.41 -119.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 304 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 158 ND1
REMARK 620 2 HOH A 451 O 108.1
REMARK 620 3 HOH A 583 O 122.6 62.7
REMARK 620 4 HIS A 158 ND1 0.0 108.1 122.6
REMARK 620 5 HOH A 583 O 122.6 62.7 0.0 122.6
REMARK 620 6 HOH A 451 O 100.5 125.4 62.7 100.5 62.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MQZ A 306
DBREF 6T70 A 2 293 UNP K4MHV9 K4MHV9_9ACTN 2 293
SEQADV 6T70 HIS A -16 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 HIS A -15 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 HIS A -14 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 HIS A -13 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 HIS A -12 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 HIS A -11 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 SER A -10 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 SER A -9 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 GLY A -8 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 LEU A -7 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 VAL A -6 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 PRO A -5 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 ARG A -4 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 GLY A -3 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 SER A -2 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 HIS A -1 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 MET A 0 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T70 VAL A 1 UNP K4MHV9 EXPRESSION TAG
SEQRES 1 A 310 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 310 GLY SER HIS MET VAL ARG ASP GLY ASN GLY THR SER ARG
SEQRES 3 A 310 ARG ASP VAL PHE GLU VAL PHE SER ARG ASP GLY THR PRO
SEQRES 4 A 310 ILE ARG GLY PHE SER ARG PRO GLY PRO GLY GLU THR VAL
SEQRES 5 A 310 VAL LEU VAL HIS GLY VAL ALA MET ASP ARG ARG ILE TRP
SEQRES 6 A 310 ALA GLU SER GLY PHE LEU ASP ALA LEU PRO ASP ALA HIS
SEQRES 7 A 310 VAL LEU ALA LEU ASP LEU ARG GLY ARG GLY GLU SER GLY
SEQRES 8 A 310 ARG VAL GLY THR ALA GLU GLY HIS ALA LEU ARG ARG TYR
SEQRES 9 A 310 VAL GLU ASP VAL ARG ALA VAL LEU ASP ARG PHE GLY ARG
SEQRES 10 A 310 ALA ARG TYR SER LEU PHE GLY THR PHE PHE GLY GLY ARG
SEQRES 11 A 310 ILE ALA LEU GLN VAL ALA ALA VAL ASP THR ARG VAL ALA
SEQRES 12 A 310 ARG ALA PHE SER PHE CYS ALA HIS ALA GLU GLN VAL GLU
SEQRES 13 A 310 ILE PRO GLU ASP ALA VAL GLU GLU GLU ALA VAL ALA VAL
SEQRES 14 A 310 GLU GLY PRO GLY GLY HIS ALA TYR LEU ARG ASP HIS PHE
SEQRES 15 A 310 THR GLY ARG GLY ALA PRO PRO TRP MET VAL GLU ALA CYS
SEQRES 16 A 310 ALA ARG VAL ASP PRO GLY GLU LEU GLY ALA ALA THR ARG
SEQRES 17 A 310 GLY LEU LEU HIS GLY SER ASP ARG ARG THR GLU ARG GLY
SEQRES 18 A 310 HIS PRO ASP GLN GLU LEU VAL LEU ILE THR ALA ASP GLY
SEQRES 19 A 310 ASP ALA ASP LEU ALA PRO PHE HIS ALA GLY GLU ARG ARG
SEQRES 20 A 310 LEU GLY ALA HIS LEU TRP LEU VAL ASP ALA PRO THR ARG
SEQRES 21 A 310 ILE LYS ALA ALA GLY ARG LEU ALA GLU VAL GLY ARG ARG
SEQRES 22 A 310 VAL ALA GLY VAL LEU ALA GLU GLY GLY HIS GLY THR GLY
SEQRES 23 A 310 ASP ALA PRO ALA GLU ALA ARG THR THR GLY ASP ALA PRO
SEQRES 24 A 310 ALA GLU ALA ARG ALA SER GLY THR GLY VAL VAL
HET CL A 301 1
HET GOL A 302 12
HET SO4 A 303 5
HET ZN A 304 1
HET GOL A 305 12
HET MQZ A 306 122
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETNAM MQZ BOTTROMYCIN A2 DERIVATIVE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CL CL 1-
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 ZN ZN 2+
FORMUL 7 MQZ C42 H62 N8 O8 S2
FORMUL 8 HOH *201(H2 O)
HELIX 1 AA1 ARG A 46 SER A 51 1 6
HELIX 2 AA2 PHE A 53 LEU A 57 5 5
HELIX 3 AA3 ALA A 79 HIS A 82 5 4
HELIX 4 AA4 ALA A 83 GLY A 99 1 17
HELIX 5 AA5 PHE A 109 ASP A 122 1 14
HELIX 6 AA6 PRO A 141 GLY A 154 1 14
HELIX 7 AA7 GLY A 156 ARG A 168 1 13
HELIX 8 AA8 PRO A 171 CYS A 178 1 8
HELIX 9 AA9 ALA A 179 VAL A 181 5 3
HELIX 10 AB1 ASP A 182 LEU A 193 1 12
HELIX 11 AB2 LEU A 221 GLY A 232 1 12
HELIX 12 AB3 THR A 242 ALA A 247 1 6
HELIX 13 AB4 ARG A 249 ALA A 262 1 14
SHEET 1 AA1 8 ASP A 11 PHE A 16 0
SHEET 2 AA1 8 PRO A 22 ARG A 28 -1 O SER A 27 N ASP A 11
SHEET 3 AA1 8 HIS A 61 LEU A 65 -1 O VAL A 62 N ARG A 28
SHEET 4 AA1 8 THR A 34 VAL A 38 1 N VAL A 35 O LEU A 63
SHEET 5 AA1 8 TYR A 103 THR A 108 1 O SER A 104 N VAL A 36
SHEET 6 AA1 8 VAL A 125 PHE A 131 1 O PHE A 131 N GLY A 107
SHEET 7 AA1 8 GLU A 209 ALA A 215 1 O VAL A 211 N SER A 130
SHEET 8 AA1 8 HIS A 234 VAL A 238 1 O TRP A 236 N LEU A 212
LINK ND1 HIS A 158 ZN ZN A 304 1555 1555 2.00
LINK ZN ZN A 304 O HOH A 451 1555 1555 2.43
LINK ZN ZN A 304 O HOH A 583 1555 1555 2.11
LINK ND1 HIS A 158 ZN ZN A 304 1555 2455 2.00
LINK ZN ZN A 304 O HOH A 583 1555 2455 2.11
LINK ZN ZN A 304 O HOH A 451 1555 2455 2.43
SITE 1 AC1 4 GLY A 40 VAL A 41 PHE A 109 PHE A 110
SITE 1 AC2 4 ARG A 100 ALA A 101 ARG A 102 HOH A 427
SITE 1 AC3 9 ARG A 46 ARG A 180 ASP A 182 PRO A 183
SITE 2 AC3 9 GLY A 184 HOH A 411 HOH A 439 HOH A 459
SITE 3 AC3 9 HOH A 497
SITE 1 AC4 3 HIS A 158 HOH A 451 HOH A 583
SITE 1 AC5 3 ARG A 18 ARG A 86 HOH A 538
SITE 1 AC6 15 PHE A 109 PHE A 110 ARG A 113 PRO A 141
SITE 2 AC6 15 GLU A 148 HIS A 164 PHE A 165 ARG A 168
SITE 3 AC6 15 THR A 190 LEU A 193 SER A 197 ILE A 244
SITE 4 AC6 15 HOH A 409 HOH A 499 HOH A 542
CRYST1 66.544 79.430 88.444 90.00 90.00 90.00 I 2 2 2 8
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 0.015028 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012590 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011307 0.00000
TER 3827 ALA A 262
MASTER 517 0 6 13 8 0 11 6 2209 1 155 24
END
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