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HEADER HYDROLASE 20-OCT-19 6T6X
TITLE STRUCTURE OF THE BOTTROMYCIN EPIMERASE BOTH IN COMPLEX WITH SUBSTRATE
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 6T6X 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. 1.25 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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 65761
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3282
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 44.7700 - 3.5500 0.94 2770 145 0.1691 0.1889
REMARK 3 2 3.5500 - 2.8200 0.97 2730 145 0.1616 0.1475
REMARK 3 3 2.8200 - 2.4600 0.97 2657 171 0.1576 0.1681
REMARK 3 4 2.4600 - 2.2400 0.97 2693 151 0.1462 0.1340
REMARK 3 5 2.2400 - 2.0800 0.99 2707 137 0.1454 0.1615
REMARK 3 6 2.0800 - 1.9600 0.99 2755 138 0.1436 0.1548
REMARK 3 7 1.9600 - 1.8600 0.99 2723 147 0.1549 0.1647
REMARK 3 8 1.8600 - 1.7800 1.00 2747 149 0.1573 0.1606
REMARK 3 9 1.7800 - 1.7100 0.98 2659 144 0.1678 0.1796
REMARK 3 10 1.7100 - 1.6500 0.99 2731 152 0.1688 0.1897
REMARK 3 11 1.6500 - 1.6000 1.00 2700 116 0.1673 0.1828
REMARK 3 12 1.6000 - 1.5500 1.00 2765 125 0.1678 0.2058
REMARK 3 13 1.5500 - 1.5100 1.00 2720 154 0.1710 0.1856
REMARK 3 14 1.5100 - 1.4700 1.00 2731 151 0.1732 0.1709
REMARK 3 15 1.4700 - 1.4400 1.00 2697 149 0.1799 0.2125
REMARK 3 16 1.4400 - 1.4100 0.99 2703 128 0.1900 0.2108
REMARK 3 17 1.4100 - 1.3800 1.00 2739 147 0.1895 0.2187
REMARK 3 18 1.3800 - 1.3600 1.00 2696 141 0.1990 0.2288
REMARK 3 19 1.3600 - 1.3300 1.00 2725 134 0.2036 0.2259
REMARK 3 20 1.3300 - 1.3100 1.00 2720 121 0.2031 0.2046
REMARK 3 21 1.3100 - 1.2900 1.00 2724 154 0.2009 0.1862
REMARK 3 22 1.2900 - 1.2700 1.00 2682 142 0.2114 0.2101
REMARK 3 23 1.2700 - 1.2500 1.00 2705 141 0.2115 0.2585
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) : 0.101
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.264
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.29
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 : 0.008 2036
REMARK 3 ANGLE : 1.229 2763
REMARK 3 CHIRALITY : 0.081 293
REMARK 3 PLANARITY : 0.008 374
REMARK 3 DIHEDRAL : 15.230 726
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 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5873 -11.3871 -34.6068
REMARK 3 T TENSOR
REMARK 3 T11: 0.0393 T22: 0.0617
REMARK 3 T33: 0.0402 T12: -0.0010
REMARK 3 T13: 0.0020 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.8391 L22: 1.8811
REMARK 3 L33: 1.0837 L12: 0.1361
REMARK 3 L13: -0.0481 L23: -0.0459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: 0.0833 S13: -0.0587
REMARK 3 S21: -0.0821 S22: 0.0288 S23: -0.1160
REMARK 3 S31: 0.0732 S32: 0.0400 S33: -0.0146
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8437 -1.7277 -35.0092
REMARK 3 T TENSOR
REMARK 3 T11: 0.0507 T22: 0.0319
REMARK 3 T33: 0.0327 T12: -0.0107
REMARK 3 T13: 0.0017 T23: 0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 1.6322 L22: 1.7984
REMARK 3 L33: 2.6228 L12: -0.0856
REMARK 3 L13: 0.0524 L23: 1.0224
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: 0.0501 S13: 0.0946
REMARK 3 S21: -0.0842 S22: -0.0439 S23: 0.0408
REMARK 3 S31: 0.0336 S32: -0.0836 S33: 0.0391
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5445 -10.7368 -30.2327
REMARK 3 T TENSOR
REMARK 3 T11: 0.0324 T22: 0.0480
REMARK 3 T33: 0.0570 T12: -0.0144
REMARK 3 T13: -0.0006 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.5075 L22: 1.6931
REMARK 3 L33: 0.9336 L12: 0.2678
REMARK 3 L13: -0.0996 L23: -0.0494
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: 0.0128 S13: 0.0890
REMARK 3 S21: 0.0597 S22: -0.0030 S23: 0.1290
REMARK 3 S31: -0.0215 S32: -0.0584 S33: 0.0183
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7045 -0.3289 -11.6700
REMARK 3 T TENSOR
REMARK 3 T11: 0.1303 T22: 0.1304
REMARK 3 T33: 0.0774 T12: 0.0083
REMARK 3 T13: 0.0150 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 1.4041 L22: 3.7692
REMARK 3 L33: 1.4584 L12: -0.9718
REMARK 3 L13: 0.5258 L23: -0.7502
REMARK 3 S TENSOR
REMARK 3 S11: -0.0705 S12: -0.2473 S13: 0.1060
REMARK 3 S21: 0.3336 S22: 0.0218 S23: 0.0418
REMARK 3 S31: -0.0322 S32: -0.1154 S33: 0.0392
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1898 -9.0376 -17.2529
REMARK 3 T TENSOR
REMARK 3 T11: 0.0886 T22: 0.0871
REMARK 3 T33: 0.0864 T12: 0.0046
REMARK 3 T13: 0.0022 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.9367 L22: 3.7911
REMARK 3 L33: 1.3320 L12: 1.3201
REMARK 3 L13: 0.2531 L23: -1.1827
REMARK 3 S TENSOR
REMARK 3 S11: 0.0604 S12: -0.0894 S13: -0.0321
REMARK 3 S21: 0.2568 S22: -0.0524 S23: 0.0211
REMARK 3 S31: -0.0240 S32: -0.0103 S33: -0.0275
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1717 -8.4506 -25.9977
REMARK 3 T TENSOR
REMARK 3 T11: 0.0584 T22: 0.0897
REMARK 3 T33: 0.0716 T12: -0.0056
REMARK 3 T13: 0.0136 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.8811 L22: 1.3319
REMARK 3 L33: 0.2969 L12: 0.4876
REMARK 3 L13: 0.1908 L23: 0.2344
REMARK 3 S TENSOR
REMARK 3 S11: -0.0464 S12: 0.0195 S13: 0.0905
REMARK 3 S21: -0.0050 S22: 0.0170 S23: 0.2029
REMARK 3 S31: -0.0071 S32: -0.0674 S33: 0.0430
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 222 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8032 -21.4893 -24.0328
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.0477
REMARK 3 T33: 0.0506 T12: -0.0218
REMARK 3 T13: 0.0106 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.8704 L22: 0.8278
REMARK 3 L33: 1.0295 L12: -0.1446
REMARK 3 L13: -0.3238 L23: 0.0378
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: -0.0499 S13: -0.0598
REMARK 3 S21: 0.0682 S22: 0.0300 S23: 0.0791
REMARK 3 S31: 0.1204 S32: -0.0478 S33: 0.0061
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 6T6X 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_1292104925.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-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 : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65761
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 44.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.72500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.200
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 (%): 35.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
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 33.32750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.14250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.66850
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.32750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.14250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.66850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.32750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.14250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.66850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.32750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.14250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 44.66850
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 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 HOH A 403 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 516 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 563 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 613 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 616 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 636 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 HH11 ARG A 100 O HOH A 402 1.44
REMARK 500 OE2 GLU A 80 HH21 ARG A 85 1.53
REMARK 500 OD1 ASP A 163 O HOH A 401 1.80
REMARK 500 O HOH A 560 O HOH A 565 1.82
REMARK 500 O HOH A 414 O HOH A 444 1.84
REMARK 500 O HOH A 615 O HOH A 635 1.86
REMARK 500 O HOH A 646 O HOH A 695 1.88
REMARK 500 O HOH A 472 O HOH A 667 1.91
REMARK 500 O HOH A 435 O HOH A 548 1.92
REMARK 500 O HOH A 682 O HOH A 689 1.94
REMARK 500 O HOH A 426 O HOH A 627 1.95
REMARK 500 O HOH A 541 O HOH A 682 2.01
REMARK 500 O HOH A 429 O HOH A 580 2.01
REMARK 500 O HOH A 507 O HOH A 643 2.03
REMARK 500 O HOH A 414 O HOH A 603 2.03
REMARK 500 NH1 ARG A 100 O HOH A 402 2.06
REMARK 500 OE2 GLU A 80 NH2 ARG A 85 2.07
REMARK 500 O HOH A 497 O HOH A 553 2.11
REMARK 500 O HOH A 410 O HOH A 444 2.12
REMARK 500 OD2 ASP A 44 O HOH A 404 2.15
REMARK 500 O HOH A 404 O HOH A 566 2.15
REMARK 500 O HOH A 431 O HOH A 615 2.15
REMARK 500 OD2 ASP A 220 O HOH A 405 2.16
REMARK 500 O HOH A 431 O HOH A 635 2.16
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 459 O HOH A 459 3554 1.29
REMARK 500 O HOH A 473 O HOH A 473 2555 1.30
REMARK 500 O HOH A 422 O HOH A 565 2555 2.00
REMARK 500 O HOH A 521 O HOH A 557 8444 2.06
REMARK 500 O HOH A 423 O HOH A 459 4554 2.10
REMARK 500 O HOH A 404 O HOH A 418 2555 2.11
REMARK 500 O HOH A 447 O HOH A 635 2555 2.14
REMARK 500 O HOH A 534 O HOH A 651 8544 2.15
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 46.66 -95.72
REMARK 500 VAL A 76 -69.74 -127.93
REMARK 500 PHE A 109 -124.30 57.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MQW A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6T6H RELATED DB: PDB
REMARK 900 CONTAINS APO PROTEIN
DBREF 6T6X A 2 293 UNP K4MHV9 K4MHV9_9ACTN 2 293
SEQADV 6T6X HIS A -16 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X HIS A -15 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X HIS A -14 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X HIS A -13 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X HIS A -12 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X HIS A -11 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X SER A -10 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X SER A -9 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X GLY A -8 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X LEU A -7 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X VAL A -6 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X PRO A -5 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X ARG A -4 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X GLY A -3 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X SER A -2 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X HIS A -1 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X MET A 0 UNP K4MHV9 EXPRESSION TAG
SEQADV 6T6X 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 MQW A 301 108
HETNAM MQW (4~{R})-2-[(1~{R})-1-[[(2~{S})-2-[[(2~{S})-3-METHYL-2-
HETNAM 2 MQW [[(4~{Z},6~{S},9~{S},12~{S})-2,8,11-
HETNAM 3 MQW TRIS(OXIDANYLIDENE)-6,9-DI(PROPAN-2-YL)-1,4,7,10-
HETNAM 4 MQW TETRAZABICYCLO[10.3.0]PENTADEC-4-EN-5-
HETNAM 5 MQW YL]AMINO]BUTANOYL]AMINO]-3-PHENYL-PROPANOYL]AMINO]-3-
HETNAM 6 MQW OXIDANYL-3-OXIDANYLIDENE-PROPYL]-4,5-DIHYDRO-1,3-
HETNAM 7 MQW THIAZOLE-4-CARBOXYLIC ACID
FORMUL 2 MQW C38 H54 N8 O9 S
FORMUL 3 HOH *306(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 ILE A 23 N VAL A 15
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 PHE A 106 N VAL A 38
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 HIS A 234 N LEU A 212
SITE 1 AC1 22 GLY A 40 VAL A 41 PHE A 109 PHE A 110
SITE 2 AC1 22 ARG A 113 CYS A 132 ALA A 133 HIS A 134
SITE 3 AC1 22 GLU A 148 HIS A 164 PHE A 165 MET A 174
SITE 4 AC1 22 THR A 190 LEU A 193 ARG A 243 HOH A 416
SITE 5 AC1 22 HOH A 421 HOH A 451 HOH A 471 HOH A 491
SITE 6 AC1 22 HOH A 519 HOH A 574
CRYST1 66.655 80.285 89.337 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 0.015003 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012456 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011194 0.00000
TER 3822 ALA A 262
MASTER 507 0 1 13 8 0 6 6 2291 1 107 24
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