HEADER TRANSFERASE/ANTIBIOTIC 03-NOV-12 4HUS
TITLE CRYSTAL STRUCTURE OF STREPTOGRAMIN GROUP A ANTIBIOTIC
TITLE 2 ACETYLTRANSFERASE VATA FROM STAPHYLOCOCCUS AUREUS IN COMPLEX WITH
TITLE 3 VIRGINIAMYCIN M1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VIRGINIAMYCIN A ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 2.3.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 STRAIN: BM3093;
SOURCE 5 GENE: VAT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS STRUCTURAL GENOMICS, ANTIBIOTIC RESISTANCE, CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS OF INFECTIOUS DISEASES (CSGID), NIAID, NATIONAL INSTITUTE
KEYWDS 3 OF ALLERGY AND INFECTIOUS DISEASES, XENOBIOTIC ACYLTRANSFERASE (XAT)
KEYWDS 4 FAMILY, HEXAPEPTIDE REPEAT ACYLTRANSFERASE, STREPTOGRAMIN GROUP A
KEYWDS 5 ANTIBIOTIC ACETYLTRANSFERASE, STREPTOGRAMIN GROUP A ANTIBIOTICS,
KEYWDS 6 STREPTOGRAMIN A, VIRGINIAMYCIN M1, DALFOPRISTIN, ACETYL COENZYME A,
KEYWDS 7 COENZYME A, INTRACELLULAR, TRANSFERASE-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,G.MINASOV,E.EVDOKIMOVA,Z.WAWRZAK,V.YIM,M.KRISHNAMOORTHY,
AUTHOR 2 R.DI LEO,P.COURVALIN,A.SAVCHENKO,W.F.ANDERSON,CENTER FOR STRUCTURAL
AUTHOR 3 GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 4 20-SEP-23 4HUS 1 REMARK SEQADV LINK
REVDAT 3 24-DEC-14 4HUS 1 JRNL
REVDAT 2 24-SEP-14 4HUS 1 JRNL
REVDAT 1 21-NOV-12 4HUS 0
JRNL AUTH P.J.STOGIOS,M.L.KUHN,E.EVDOKIMOVA,P.COURVALIN,W.F.ANDERSON,
JRNL AUTH 2 A.SAVCHENKO
JRNL TITL POTENTIAL FOR REDUCTION OF STREPTOGRAMIN A RESISTANCE
JRNL TITL 2 REVEALED BY STRUCTURAL ANALYSIS OF ACETYLTRANSFERASE VATA.
JRNL REF ANTIMICROB.AGENTS CHEMOTHER. V. 58 7083 2014
JRNL REFN ISSN 0066-4804
JRNL PMID 25223995
JRNL DOI 10.1128/AAC.03743-14
REMARK 2
REMARK 2 RESOLUTION. 2.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 2.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 34991
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1751
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 29.3910 - 5.5378 1.00 2732 143 0.1956 0.2153
REMARK 3 2 5.5378 - 4.4002 1.00 2631 140 0.1464 0.1850
REMARK 3 3 4.4002 - 3.8454 0.99 2564 135 0.1425 0.1595
REMARK 3 4 3.8454 - 3.4944 0.87 2245 118 0.1975 0.2746
REMARK 3 5 3.4944 - 3.2443 1.00 2576 135 0.1852 0.2276
REMARK 3 6 3.2443 - 3.0532 1.00 2576 137 0.2043 0.2524
REMARK 3 7 3.0532 - 2.9005 1.00 2563 135 0.1963 0.2603
REMARK 3 8 2.9005 - 2.7743 1.00 2582 135 0.2060 0.2630
REMARK 3 9 2.7743 - 2.6676 1.00 2535 134 0.1943 0.2597
REMARK 3 10 2.6676 - 2.5756 1.00 2581 136 0.1987 0.2357
REMARK 3 11 2.5756 - 2.4951 1.00 2551 134 0.2167 0.3209
REMARK 3 12 2.4951 - 2.4238 1.00 2526 134 0.2133 0.2803
REMARK 3 13 2.4238 - 2.3600 1.00 2578 135 0.2193 0.2566
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.630
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 : 0.011 5385
REMARK 3 ANGLE : 1.238 7246
REMARK 3 CHIRALITY : 0.075 752
REMARK 3 PLANARITY : 0.004 915
REMARK 3 DIHEDRAL : 15.664 2056
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESI 7:84
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9617 32.1672 -11.0927
REMARK 3 T TENSOR
REMARK 3 T11: 0.1937 T22: 0.2376
REMARK 3 T33: 0.2156 T12: -0.0053
REMARK 3 T13: 0.0766 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 3.4369 L22: 3.7909
REMARK 3 L33: 7.4844 L12: -1.2840
REMARK 3 L13: 2.8674 L23: -2.2088
REMARK 3 S TENSOR
REMARK 3 S11: -0.1083 S12: 0.0593 S13: 0.0050
REMARK 3 S21: 0.2534 S22: 0.0405 S23: -0.1249
REMARK 3 S31: -0.2200 S32: 0.2844 S33: 0.0747
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESI 85:113
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4788 42.2349 -39.6498
REMARK 3 T TENSOR
REMARK 3 T11: 0.4045 T22: 0.2751
REMARK 3 T33: 0.2504 T12: 0.0162
REMARK 3 T13: -0.0996 T23: 0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 9.5470 L22: 4.8407
REMARK 3 L33: 3.0155 L12: -0.2842
REMARK 3 L13: -0.3156 L23: 3.3563
REMARK 3 S TENSOR
REMARK 3 S11: -0.1890 S12: -0.0772 S13: 0.2165
REMARK 3 S21: 0.1770 S22: 0.2344 S23: -0.2685
REMARK 3 S31: -0.1652 S32: -0.0227 S33: -0.0389
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESI 114:216
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1765 30.4968 -3.0655
REMARK 3 T TENSOR
REMARK 3 T11: 0.3198 T22: 0.3869
REMARK 3 T33: 0.4253 T12: 0.0507
REMARK 3 T13: 0.1545 T23: 0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 1.1798 L22: 2.8037
REMARK 3 L33: 3.2783 L12: 0.1920
REMARK 3 L13: -0.3136 L23: 0.4993
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: -0.2436 S13: 0.0108
REMARK 3 S21: 0.5561 S22: 0.0211 S23: 0.4882
REMARK 3 S31: 0.0577 S32: -0.5388 S33: 0.0334
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESI 6:84
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3467 22.8751 -42.9345
REMARK 3 T TENSOR
REMARK 3 T11: 0.1968 T22: 0.3603
REMARK 3 T33: 0.3139 T12: 0.0827
REMARK 3 T13: -0.0304 T23: -0.0730
REMARK 3 L TENSOR
REMARK 3 L11: 5.3023 L22: 8.9644
REMARK 3 L33: 4.8629 L12: 1.7552
REMARK 3 L13: -0.4369 L23: -1.1824
REMARK 3 S TENSOR
REMARK 3 S11: 0.0514 S12: 0.2700 S13: -0.4943
REMARK 3 S21: -0.4723 S22: 0.0354 S23: -0.2049
REMARK 3 S31: 0.3983 S32: 0.4021 S33: -0.0936
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESI 85:113
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6660 -7.1216 -36.4230
REMARK 3 T TENSOR
REMARK 3 T11: 0.8978 T22: 0.4895
REMARK 3 T33: 0.7782 T12: -0.1723
REMARK 3 T13: -0.1096 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 2.1546 L22: 0.6787
REMARK 3 L33: 5.6186 L12: 0.9478
REMARK 3 L13: 1.4900 L23: -0.4584
REMARK 3 S TENSOR
REMARK 3 S11: -0.3139 S12: 0.9417 S13: 0.1837
REMARK 3 S21: -0.8517 S22: 0.3332 S23: 0.3461
REMARK 3 S31: -0.2258 S32: 0.0546 S33: -0.0046
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESI 114:216
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3794 30.5519 -43.6725
REMARK 3 T TENSOR
REMARK 3 T11: 0.2603 T22: 0.3222
REMARK 3 T33: 0.3717 T12: -0.0015
REMARK 3 T13: -0.0844 T23: -0.0591
REMARK 3 L TENSOR
REMARK 3 L11: 2.0678 L22: 4.6127
REMARK 3 L33: 2.7515 L12: -0.8597
REMARK 3 L13: 0.7020 L23: -2.4405
REMARK 3 S TENSOR
REMARK 3 S11: 0.1178 S12: 0.1959 S13: -0.4161
REMARK 3 S21: -0.3878 S22: 0.0801 S23: 0.5337
REMARK 3 S31: 0.1582 S32: -0.3215 S33: -0.1911
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN C AND RESI 7:84
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2260 0.2093 -18.5098
REMARK 3 T TENSOR
REMARK 3 T11: 0.3380 T22: 0.2275
REMARK 3 T33: 0.4101 T12: -0.0085
REMARK 3 T13: -0.0138 T23: 0.0744
REMARK 3 L TENSOR
REMARK 3 L11: 3.8345 L22: 5.0586
REMARK 3 L33: 8.3085 L12: -2.2206
REMARK 3 L13: -2.7096 L23: 3.9359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0936 S12: -0.0770 S13: -0.2745
REMARK 3 S21: 0.1296 S22: 0.0892 S23: -0.0862
REMARK 3 S31: 0.5287 S32: 0.3846 S33: -0.0151
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN C AND RESI 85:113
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6800 20.2398 4.7061
REMARK 3 T TENSOR
REMARK 3 T11: 0.6281 T22: 0.3988
REMARK 3 T33: 0.3544 T12: 0.0181
REMARK 3 T13: 0.1008 T23: 0.0907
REMARK 3 L TENSOR
REMARK 3 L11: 3.8745 L22: 3.2432
REMARK 3 L33: 1.4034 L12: -0.1949
REMARK 3 L13: 1.0210 L23: 1.6953
REMARK 3 S TENSOR
REMARK 3 S11: 0.0947 S12: -0.2546 S13: -0.1853
REMARK 3 S21: 0.4156 S22: 0.0108 S23: 0.2041
REMARK 3 S31: 0.4155 S32: 0.0009 S33: -0.0992
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN C AND RESI 114:215
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8895 -4.8073 -23.3667
REMARK 3 T TENSOR
REMARK 3 T11: 0.5354 T22: 0.3841
REMARK 3 T33: 0.6739 T12: -0.1588
REMARK 3 T13: -0.0175 T23: 0.0535
REMARK 3 L TENSOR
REMARK 3 L11: 2.1030 L22: 4.0969
REMARK 3 L33: 2.5875 L12: 0.6514
REMARK 3 L13: -0.3834 L23: 1.0553
REMARK 3 S TENSOR
REMARK 3 S11: -0.1302 S12: 0.2290 S13: -0.4564
REMARK 3 S21: 0.0109 S22: -0.0284 S23: 0.8025
REMARK 3 S31: 0.7188 S32: -0.3988 S33: 0.1544
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 4HUS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000075946.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37898
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.57600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4E8L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULPHATE, 0.1 M HEPES PH
REMARK 280 7.5, 2% PEG 400, VIRGINIAMYCIN M1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 49.28350
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 49.28350
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 46.65400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 92.36750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.65400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 92.36750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.28350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.65400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 92.36750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.28350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.65400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 92.36750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 GLY A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 LEU A 3
REMARK 465 ASN A 4
REMARK 465 ASN A 5
REMARK 465 ASP A 6
REMARK 465 THR A 219
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 LEU B 3
REMARK 465 ASN B 4
REMARK 465 ASN B 5
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 LEU C 3
REMARK 465 ASN C 4
REMARK 465 ASN C 5
REMARK 465 ASP C 6
REMARK 465 LEU C 216
REMARK 465 ASP C 217
REMARK 465 ASP C 218
REMARK 465 THR C 219
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 213 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
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 TYR A 40 -17.27 72.94
REMARK 500 ARG A 47 17.45 -140.01
REMARK 500 ARG A 100 -138.64 58.09
REMARK 500 LYS A 214 77.13 54.16
REMARK 500 TYR B 40 -12.66 66.01
REMARK 500 ARG B 47 41.11 -145.96
REMARK 500 ARG B 100 -135.61 51.56
REMARK 500 TYR C 40 -7.54 66.42
REMARK 500 ARG C 47 26.40 -141.21
REMARK 500 ARG C 100 -135.04 48.10
REMARK 500 ILE C 169 -62.75 -104.20
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 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 164 O
REMARK 620 2 HOH A 422 O 87.1
REMARK 620 3 ASN B 164 O 84.3 170.1
REMARK 620 4 HOH B 417 O 85.9 93.5 90.7
REMARK 620 5 ASN C 164 O 80.6 91.0 82.8 165.5
REMARK 620 6 HOH C 514 O 170.0 100.7 87.4 99.6 93.0
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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 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 NA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VIR A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 310
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HUR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOGRAMIN GROUP A ANTIBIOTIC
REMARK 900 ACETYLTRANSFERASE VATA FROM STAPHYLOCOCCUS AUREUS IN COMPLEX WITH
REMARK 900 ACETYL COENZYME A
REMARK 900 RELATED ID: CSGID-IDP91546 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4E8L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOGRAMIN GROUP A ANTIBIOTIC
REMARK 900 ACETYLTRANSFERASE VATA FROM STAPHYLOCOCCUS AUREUS
DBREF 4HUS A 1 219 UNP P26839 VATA_STAAU 1 219
DBREF 4HUS B 1 219 UNP P26839 VATA_STAAU 1 219
DBREF 4HUS C 1 219 UNP P26839 VATA_STAAU 1 219
SEQADV 4HUS GLY A 0 UNP P26839 EXPRESSION TAG
SEQADV 4HUS GLY B 0 UNP P26839 EXPRESSION TAG
SEQADV 4HUS GLY C 0 UNP P26839 EXPRESSION TAG
SEQRES 1 A 220 GLY MET ASN LEU ASN ASN ASP HIS GLY PRO ASP PRO GLU
SEQRES 2 A 220 ASN ILE LEU PRO ILE LYS GLY ASN ARG ASN LEU GLN PHE
SEQRES 3 A 220 ILE LYS PRO THR ILE THR ASN GLU ASN ILE LEU VAL GLY
SEQRES 4 A 220 GLU TYR SER TYR TYR ASP SER LYS ARG GLY GLU SER PHE
SEQRES 5 A 220 GLU ASP GLN VAL LEU TYR HIS TYR GLU VAL ILE GLY ASP
SEQRES 6 A 220 LYS LEU ILE ILE GLY ARG PHE CYS SER ILE GLY PRO GLY
SEQRES 7 A 220 THR THR PHE ILE MET ASN GLY ALA ASN HIS ARG MET ASP
SEQRES 8 A 220 GLY SER THR TYR PRO PHE HIS LEU PHE ARG MET GLY TRP
SEQRES 9 A 220 GLU LYS TYR MET PRO SER LEU LYS ASP LEU PRO LEU LYS
SEQRES 10 A 220 GLY ASP ILE GLU ILE GLY ASN ASP VAL TRP ILE GLY ARG
SEQRES 11 A 220 ASP VAL THR ILE MET PRO GLY VAL LYS ILE GLY ASP GLY
SEQRES 12 A 220 ALA ILE ILE ALA ALA GLU ALA VAL VAL THR LYS ASN VAL
SEQRES 13 A 220 ALA PRO TYR SER ILE VAL GLY GLY ASN PRO LEU LYS PHE
SEQRES 14 A 220 ILE ARG LYS ARG PHE SER ASP GLY VAL ILE GLU GLU TRP
SEQRES 15 A 220 LEU ALA LEU GLN TRP TRP ASN LEU ASP MET LYS ILE ILE
SEQRES 16 A 220 ASN GLU ASN LEU PRO PHE ILE ILE ASN GLY ASP ILE GLU
SEQRES 17 A 220 MET LEU LYS ARG LYS ARG LYS LEU LEU ASP ASP THR
SEQRES 1 B 220 GLY MET ASN LEU ASN ASN ASP HIS GLY PRO ASP PRO GLU
SEQRES 2 B 220 ASN ILE LEU PRO ILE LYS GLY ASN ARG ASN LEU GLN PHE
SEQRES 3 B 220 ILE LYS PRO THR ILE THR ASN GLU ASN ILE LEU VAL GLY
SEQRES 4 B 220 GLU TYR SER TYR TYR ASP SER LYS ARG GLY GLU SER PHE
SEQRES 5 B 220 GLU ASP GLN VAL LEU TYR HIS TYR GLU VAL ILE GLY ASP
SEQRES 6 B 220 LYS LEU ILE ILE GLY ARG PHE CYS SER ILE GLY PRO GLY
SEQRES 7 B 220 THR THR PHE ILE MET ASN GLY ALA ASN HIS ARG MET ASP
SEQRES 8 B 220 GLY SER THR TYR PRO PHE HIS LEU PHE ARG MET GLY TRP
SEQRES 9 B 220 GLU LYS TYR MET PRO SER LEU LYS ASP LEU PRO LEU LYS
SEQRES 10 B 220 GLY ASP ILE GLU ILE GLY ASN ASP VAL TRP ILE GLY ARG
SEQRES 11 B 220 ASP VAL THR ILE MET PRO GLY VAL LYS ILE GLY ASP GLY
SEQRES 12 B 220 ALA ILE ILE ALA ALA GLU ALA VAL VAL THR LYS ASN VAL
SEQRES 13 B 220 ALA PRO TYR SER ILE VAL GLY GLY ASN PRO LEU LYS PHE
SEQRES 14 B 220 ILE ARG LYS ARG PHE SER ASP GLY VAL ILE GLU GLU TRP
SEQRES 15 B 220 LEU ALA LEU GLN TRP TRP ASN LEU ASP MET LYS ILE ILE
SEQRES 16 B 220 ASN GLU ASN LEU PRO PHE ILE ILE ASN GLY ASP ILE GLU
SEQRES 17 B 220 MET LEU LYS ARG LYS ARG LYS LEU LEU ASP ASP THR
SEQRES 1 C 220 GLY MET ASN LEU ASN ASN ASP HIS GLY PRO ASP PRO GLU
SEQRES 2 C 220 ASN ILE LEU PRO ILE LYS GLY ASN ARG ASN LEU GLN PHE
SEQRES 3 C 220 ILE LYS PRO THR ILE THR ASN GLU ASN ILE LEU VAL GLY
SEQRES 4 C 220 GLU TYR SER TYR TYR ASP SER LYS ARG GLY GLU SER PHE
SEQRES 5 C 220 GLU ASP GLN VAL LEU TYR HIS TYR GLU VAL ILE GLY ASP
SEQRES 6 C 220 LYS LEU ILE ILE GLY ARG PHE CYS SER ILE GLY PRO GLY
SEQRES 7 C 220 THR THR PHE ILE MET ASN GLY ALA ASN HIS ARG MET ASP
SEQRES 8 C 220 GLY SER THR TYR PRO PHE HIS LEU PHE ARG MET GLY TRP
SEQRES 9 C 220 GLU LYS TYR MET PRO SER LEU LYS ASP LEU PRO LEU LYS
SEQRES 10 C 220 GLY ASP ILE GLU ILE GLY ASN ASP VAL TRP ILE GLY ARG
SEQRES 11 C 220 ASP VAL THR ILE MET PRO GLY VAL LYS ILE GLY ASP GLY
SEQRES 12 C 220 ALA ILE ILE ALA ALA GLU ALA VAL VAL THR LYS ASN VAL
SEQRES 13 C 220 ALA PRO TYR SER ILE VAL GLY GLY ASN PRO LEU LYS PHE
SEQRES 14 C 220 ILE ARG LYS ARG PHE SER ASP GLY VAL ILE GLU GLU TRP
SEQRES 15 C 220 LEU ALA LEU GLN TRP TRP ASN LEU ASP MET LYS ILE ILE
SEQRES 16 C 220 ASN GLU ASN LEU PRO PHE ILE ILE ASN GLY ASP ILE GLU
SEQRES 17 C 220 MET LEU LYS ARG LYS ARG LYS LEU LEU ASP ASP THR
HET SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET NA A 304 1
HET CL A 305 1
HET CL A 306 1
HET CL A 307 1
HET CL A 308 1
HET EDO A 309 4
HET EDO A 310 4
HET EDO A 311 4
HET EDO A 312 4
HET PEG A 313 7
HET PEG A 314 7
HET PEG A 315 7
HET VIR A 316 38
HET SO4 B 301 5
HET SO4 B 302 5
HET SO4 B 303 5
HET CL B 304 1
HET CL B 305 1
HET CL B 306 1
HET EDO B 307 4
HET EDO B 308 4
HET EDO B 309 4
HET EDO B 310 4
HET EDO B 311 4
HET PEG B 312 7
HET PGE B 313 10
HET PGE B 314 10
HET SO4 C 301 5
HET SO4 C 302 5
HET CL C 303 1
HET CL C 304 1
HET EDO C 305 4
HET EDO C 306 4
HET EDO C 307 4
HET EDO C 308 4
HET EDO C 309 4
HET EDO C 310 4
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM VIR VIRGINIAMYCIN M1
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 SO4 8(O4 S 2-)
FORMUL 7 NA NA 1+
FORMUL 8 CL 9(CL 1-)
FORMUL 12 EDO 15(C2 H6 O2)
FORMUL 16 PEG 4(C4 H10 O3)
FORMUL 19 VIR C28 H35 N3 O7
FORMUL 32 PGE 2(C6 H14 O4)
FORMUL 44 HOH *508(H2 O)
HELIX 1 1 LYS A 27 ILE A 30 5 4
HELIX 2 2 PHE A 51 ASP A 53 5 3
HELIX 3 3 TYR A 59 GLY A 63 5 5
HELIX 4 4 ASN A 83 ASN A 86 5 4
HELIX 5 5 PRO A 95 ARG A 100 5 6
HELIX 6 6 GLY A 102 MET A 107 5 6
HELIX 7 7 SER A 109 LEU A 113 5 5
HELIX 8 8 SER A 174 GLN A 185 1 12
HELIX 9 9 TRP A 186 LEU A 189 5 4
HELIX 10 10 ASP A 190 GLY A 204 1 15
HELIX 11 11 ASP A 205 LYS A 214 1 10
HELIX 12 12 LYS B 27 ILE B 30 5 4
HELIX 13 13 PHE B 51 ASP B 53 5 3
HELIX 14 14 ASN B 83 ASN B 86 5 4
HELIX 15 15 PRO B 95 ARG B 100 5 6
HELIX 16 16 GLY B 102 MET B 107 5 6
HELIX 17 17 SER B 109 LEU B 113 5 5
HELIX 18 18 SER B 174 GLN B 185 1 12
HELIX 19 19 TRP B 186 LEU B 189 5 4
HELIX 20 20 ASP B 190 GLY B 204 1 15
HELIX 21 21 ASP B 205 ASP B 217 1 13
HELIX 22 22 LYS C 27 ILE C 30 5 4
HELIX 23 23 SER C 50 ASP C 53 5 4
HELIX 24 24 ASN C 83 ASN C 86 5 4
HELIX 25 25 PRO C 95 ARG C 100 5 6
HELIX 26 26 GLY C 102 MET C 107 5 6
HELIX 27 27 SER C 109 LEU C 113 5 5
HELIX 28 28 SER C 174 GLN C 185 1 12
HELIX 29 29 TRP C 186 LEU C 189 5 4
HELIX 30 30 ASP C 190 GLY C 204 1 15
HELIX 31 31 ASP C 205 LEU C 215 1 11
SHEET 1 A 7 LEU A 23 PHE A 25 0
SHEET 2 A 7 TYR A 42 ASP A 44 -1 O TYR A 43 N GLN A 24
SHEET 3 A 7 SER A 73 ILE A 74 1 O ILE A 74 N ASP A 44
SHEET 4 A 7 TRP A 126 ILE A 127 1 O ILE A 127 N SER A 73
SHEET 5 A 7 ILE A 144 ILE A 145 1 O ILE A 145 N TRP A 126
SHEET 6 A 7 SER A 159 GLY A 162 1 O SER A 159 N ILE A 144
SHEET 7 A 7 LYS A 167 LYS A 171 -1 O LYS A 167 N GLY A 162
SHEET 1 B 4 ILE A 35 VAL A 37 0
SHEET 2 B 4 LEU A 66 ILE A 68 1 O LEU A 66 N LEU A 36
SHEET 3 B 4 ILE A 119 ILE A 121 1 O ILE A 121 N ILE A 67
SHEET 4 B 4 LYS A 138 ILE A 139 1 O ILE A 139 N GLU A 120
SHEET 1 C 4 VAL A 55 LEU A 56 0
SHEET 2 C 4 THR A 79 ILE A 81 1 O PHE A 80 N LEU A 56
SHEET 3 C 4 THR A 132 ILE A 133 1 O ILE A 133 N ILE A 81
SHEET 4 C 4 VAL A 150 VAL A 151 1 O VAL A 151 N THR A 132
SHEET 1 D 7 LEU B 23 PHE B 25 0
SHEET 2 D 7 TYR B 42 ASP B 44 -1 O TYR B 43 N GLN B 24
SHEET 3 D 7 SER B 73 ILE B 74 1 O ILE B 74 N ASP B 44
SHEET 4 D 7 TRP B 126 ILE B 127 1 O ILE B 127 N SER B 73
SHEET 5 D 7 ILE B 144 ILE B 145 1 O ILE B 145 N TRP B 126
SHEET 6 D 7 SER B 159 GLY B 162 1 O SER B 159 N ILE B 144
SHEET 7 D 7 LYS B 167 LYS B 171 -1 O ARG B 170 N ILE B 160
SHEET 1 E 4 ILE B 35 VAL B 37 0
SHEET 2 E 4 LEU B 66 ILE B 68 1 O ILE B 68 N LEU B 36
SHEET 3 E 4 ILE B 119 ILE B 121 1 O ILE B 121 N ILE B 67
SHEET 4 E 4 LYS B 138 ILE B 139 1 O ILE B 139 N GLU B 120
SHEET 1 F 4 VAL B 55 LEU B 56 0
SHEET 2 F 4 THR B 79 ILE B 81 1 O PHE B 80 N LEU B 56
SHEET 3 F 4 THR B 132 ILE B 133 1 O ILE B 133 N ILE B 81
SHEET 4 F 4 VAL B 150 VAL B 151 1 O VAL B 151 N THR B 132
SHEET 1 G 7 LEU C 23 PHE C 25 0
SHEET 2 G 7 TYR C 42 ASP C 44 -1 O TYR C 43 N GLN C 24
SHEET 3 G 7 SER C 73 ILE C 74 1 O ILE C 74 N ASP C 44
SHEET 4 G 7 TRP C 126 ILE C 127 1 O ILE C 127 N SER C 73
SHEET 5 G 7 ILE C 144 ILE C 145 1 O ILE C 145 N TRP C 126
SHEET 6 G 7 SER C 159 GLY C 162 1 O SER C 159 N ILE C 144
SHEET 7 G 7 LYS C 167 LYS C 171 -1 O ARG C 170 N ILE C 160
SHEET 1 H 4 ILE C 35 VAL C 37 0
SHEET 2 H 4 LEU C 66 ILE C 68 1 O ILE C 68 N LEU C 36
SHEET 3 H 4 ILE C 119 ILE C 121 1 O ILE C 121 N ILE C 67
SHEET 4 H 4 LYS C 138 ILE C 139 1 O ILE C 139 N GLU C 120
SHEET 1 I 4 VAL C 55 LEU C 56 0
SHEET 2 I 4 THR C 79 ILE C 81 1 O PHE C 80 N LEU C 56
SHEET 3 I 4 THR C 132 ILE C 133 1 O ILE C 133 N ILE C 81
SHEET 4 I 4 VAL C 150 VAL C 151 1 O VAL C 151 N THR C 132
LINK O ASN A 164 NA NA A 304 1555 1555 2.59
LINK NA NA A 304 O HOH A 422 1555 1555 2.28
LINK NA NA A 304 O ASN B 164 1555 1555 2.53
LINK NA NA A 304 O HOH B 417 1555 1555 2.42
LINK NA NA A 304 O ASN C 164 1555 1555 2.55
LINK NA NA A 304 O HOH C 514 1555 1555 2.48
CISPEP 1 ASN A 164 PRO A 165 0 1.77
CISPEP 2 ASN B 164 PRO B 165 0 0.15
CISPEP 3 ASN C 164 PRO C 165 0 0.71
SITE 1 AC1 4 ARG A 70 LEU A 189 MET A 191 HOH A 503
SITE 1 AC2 4 ASN A 203 ARG C 88 ASP C 112 EDO C 307
SITE 1 AC3 5 LYS A 153 LEU A 166 LYS A 167 PHE A 168
SITE 2 AC3 5 HOH A 478
SITE 1 AC4 6 ASN A 164 HOH A 422 ASN B 164 HOH B 417
SITE 2 AC4 6 ASN C 164 HOH C 514
SITE 1 AC5 3 GLY A 117 ASP A 118 LYS A 138
SITE 1 AC6 2 ARG A 100 HOH A 518
SITE 1 AC7 1 LYS A 171
SITE 1 AC8 1 GLU A 60
SITE 1 AC9 2 GLY A 84 LEU A 216
SITE 1 BC1 2 LYS A 46 ARG A 47
SITE 1 BC2 5 ASP A 53 THR A 79 HOH A 420 HOH A 532
SITE 2 BC2 5 CL B 306
SITE 1 BC3 4 LYS A 138 GLY A 140 VAL A 155 HOH A 562
SITE 1 BC4 5 GLU A 12 LYS A 27 PRO A 28 HOH A 522
SITE 2 BC4 5 ARG B 211
SITE 1 BC5 8 PRO A 76 GLY A 128 ARG A 129 ALA A 146
SITE 2 BC5 8 ALA A 147 HOH A 410 TYR C 57 HOH C 511
SITE 1 BC6 2 ALA A 146 HOH A 454
SITE 1 BC7 17 ASN A 20 LEU A 23 TYR A 42 ASP A 44
SITE 2 BC7 17 HOH A 410 HOH A 412 HOH A 488 HOH A 588
SITE 3 BC7 17 TYR C 59 GLY C 84 ASN C 86 HIS C 87
SITE 4 BC7 17 HIS C 97 LEU C 98 PRO C 108 LEU C 113
SITE 5 BC7 17 HOH C 571
SITE 1 BC8 5 LYS B 153 LEU B 166 LYS B 167 PHE B 168
SITE 2 BC8 5 HOH B 553
SITE 1 BC9 5 LYS B 27 GLY B 38 GLU B 39 ARG B 70
SITE 2 BC9 5 HOH B 449
SITE 1 CC1 2 ARG B 88 ASN C 203
SITE 1 CC2 1 ILE B 139
SITE 1 CC3 2 SER B 174 GLY B 176
SITE 1 CC4 3 EDO A 311 LYS B 46 ARG B 47
SITE 1 CC5 2 LYS B 214 HOH B 527
SITE 1 CC6 7 TRP B 126 GLY B 128 ALA B 146 ALA B 147
SITE 2 CC6 7 PEG B 312 PGE B 314 HOH B 471
SITE 1 CC7 2 ASN B 154 HOH B 531
SITE 1 CC8 4 GLU B 39 ARG B 70 LEU B 189 MET B 191
SITE 1 CC9 2 TYR B 57 TYR B 59
SITE 1 DC1 3 ALA B 146 EDO B 308 HOH B 537
SITE 1 DC2 7 HIS B 87 LEU B 98 TYR C 42 ASP C 44
SITE 2 DC2 7 HOH C 506 HOH C 529 HOH C 632
SITE 1 DC3 11 TYR A 57 HIS A 87 HOH A 476 TYR B 42
SITE 2 DC3 11 ASP B 44 GLY B 75 TRP B 126 ILE B 127
SITE 3 DC3 11 ARG B 129 EDO B 308 HOH B 471
SITE 1 DC4 4 LYS C 27 GLU C 39 ARG C 70 HOH C 579
SITE 1 DC5 4 LYS C 153 LYS C 167 PHE C 168 HOH C 615
SITE 1 DC6 1 ARG C 47
SITE 1 DC7 1 ARG C 100
SITE 1 DC8 2 ALA C 146 ILE C 160
SITE 1 DC9 2 ASN C 13 ILE C 14
SITE 1 EC1 3 PRO A 199 SO4 A 302 MET C 107
SITE 1 EC2 4 LYS C 111 GLN C 185 ASN C 188 HOH C 604
SITE 1 EC3 4 ASP C 10 PRO C 11 GLU C 39 HOH C 611
SITE 1 EC4 3 GLU C 33 ASN C 34 GLU C 60
CRYST1 93.308 184.735 98.567 90.00 90.00 90.00 C 2 2 21 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010717 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005413 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010145 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
