| 1 | HEADER PEPTIDE/ANTIBIOTIC 20-SEP-00 1FVM
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| 2 | TITLE COMPLEX OF VANCOMYCIN WITH DI-ACETYL-LYS-D-ALA-D-ALA
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| 3 | COMPND MOL_ID: 1;
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| 4 | COMPND 2 MOLECULE: VANCOMYCIN;
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| 5 | COMPND 3 CHAIN: A, B, C, D, E, F;
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| 6 | COMPND 4 ENGINEERED: YES;
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| 7 | COMPND 5 MOL_ID: 2;
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| 8 | COMPND 6 MOLECULE: DI-ACETYL-LYS-D-ALA-D-ALA;
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| 9 | COMPND 7 CHAIN: G, H, I, J, K, L;
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| 10 | COMPND 8 ENGINEERED: YES
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| 11 | SOURCE MOL_ID: 1;
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| 12 | SOURCE 2 SYNTHETIC: YES;
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| 13 | SOURCE 3 ORGANISM_SCIENTIFIC: AMYCOLATOPSIS ORIENTALIS;
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| 14 | SOURCE 4 ORGANISM_TAXID: 31958;
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| 15 | SOURCE 5 OTHER_DETAILS: SEQUENCE OCCURS IN NOCARDIA ORIENTALIS;
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| 16 | SOURCE 6 MOL_ID: 2;
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| 17 | SOURCE 7 SYNTHETIC: YES
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| 18 | KEYWDS PEPTIDE-ANTIBIOTIC COMPLEX, GLYCOPEPTIDE, ANTIBIOTIC,
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| 19 | KEYWDS 2 VANCOM CELL WALL PRECURSOR,
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| 20 | KEYWDS 3 STRUCTURAL PROTEIN-ANTIBIOTIC COMPLEX
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| 21 | EXPDTA X-RAY DIFFRACTION
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| 22 | AUTHOR Y.NITANAI,K.KAKOI,K.AOKI
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| 23 | REVDAT 5 27-JUL-11 1FVM 1 REMARK
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| 24 | REVDAT 4 2 13-JUL-11 1FVM 1 VERSN
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| 25 | REVDAT 3 3 24-FEB-09 1FVM 1 VERSN
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| 26 | REVDAT 2 4 31-DEC-02 1FVM 1 REMARK
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| 27 | REVDAT 1 5 01-NOV-00 1FVM 0
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| 28 | JRNL AUTH Y.NITANAI,T.KIKUCHI,K.KAKOI,S.HANAMAKI,I.FUJISAWA,K.AOKI
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| 29 | JRNL TITL CRYSTAL STRUCTURES OF THE COMPLEXES BETWEEN VANCOMYCIN AND
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| 30 | JRNL TITL 2 CELL-WALL PRECURSOR ANALOGS.
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| 31 | JRNL REF J.MOL.BIOL. V. 385 1422 2009
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| 32 | JRNL REFN ISSN 0022-2836
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| 33 | JRNL PMID 18976660
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| 34 | JRNL DOI 10.1016/J.JMB.2008.10.026
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| 35 | REMARK 2
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| 36 | REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
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| 37 | REMARK 3
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| 38 | REMARK 3 REFINEMENT.
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| 39 | REMARK 3 PROGRAM : X-PLOR 3.851
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| 40 | REMARK 3 AUTHORS : BRUNGER
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| 41 | REMARK 3
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| 42 | REMARK 3 DATA USED IN REFINEMENT.
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| 43 | REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
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| 44 | REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
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| 45 | REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
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| 46 | REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
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| 47 | REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
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| 48 | REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
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| 49 | REMARK 3 NUMBER OF REFLECTIONS : 7864
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| 50 | REMARK 3
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| 51 | REMARK 3 FIT TO DATA USED IN REFINEMENT.
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| 52 | REMARK 3 CROSS-VALIDATION METHOD : NULL
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| 53 | REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
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| 54 | REMARK 3 R VALUE (WORKING SET) : 0.144
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| 55 | REMARK 3 FREE R VALUE : NULL
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| 56 | REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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| 57 | REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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| 58 | REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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| 59 | REMARK 3
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| 60 | REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
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| 61 | REMARK 3 TOTAL NUMBER OF BINS USED : 20
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| 62 | REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
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| 63 | REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
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| 64 | REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.70
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| 65 | REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 382
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| 66 | REMARK 3 BIN R VALUE (WORKING SET) : 0.1480
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| 67 | REMARK 3 BIN FREE R VALUE : NULL
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| 68 | REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
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| 69 | REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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| 70 | REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
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| 71 | REMARK 3
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| 72 | REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
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| 73 | REMARK 3 PROTEIN ATOMS : 636
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| 74 | REMARK 3 NUCLEIC ACID ATOMS : 0
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| 75 | REMARK 3 HETEROGEN ATOMS : 126
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| 76 | REMARK 3 SOLVENT ATOMS : 112
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| 77 | REMARK 3
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| 78 | REMARK 3 B VALUES.
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| 79 | REMARK 3 FROM WILSON PLOT (A**2) : 6.80
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| 80 | REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.50
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| 81 | REMARK 3 OVERALL ANISOTROPIC B VALUE.
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| 82 | REMARK 3 B11 (A**2) : NULL
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| 83 | REMARK 3 B22 (A**2) : NULL
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| 84 | REMARK 3 B33 (A**2) : NULL
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| 85 | REMARK 3 B12 (A**2) : NULL
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| 86 | REMARK 3 B13 (A**2) : NULL
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| 87 | REMARK 3 B23 (A**2) : NULL
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| 88 | REMARK 3
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| 89 | REMARK 3 ESTIMATED COORDINATE ERROR.
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| 90 | REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.13
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| 91 | REMARK 3 ESD FROM SIGMAA (A) : 0.07
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| 92 | REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
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| 93 | REMARK 3
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| 94 | REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
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| 95 | REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
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| 96 | REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
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| 97 | REMARK 3
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| 98 | REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
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| 99 | REMARK 3 BOND LENGTHS (A) : 0.009
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| 100 | REMARK 3 BOND ANGLES (DEGREES) : 1.05
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| 101 | REMARK 3 DIHEDRAL ANGLES (DEGREES) : 0.76
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| 102 | REMARK 3 IMPROPER ANGLES (DEGREES) : 1.34
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| 103 | REMARK 3
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| 104 | REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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| 105 | REMARK 3
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| 106 | REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
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| 107 | REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; 1.500
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| 108 | REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
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| 109 | REMARK 3 SIDE-CHAIN BOND (A**2) : 1.350 ; 2.000
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| 110 | REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.970 ; 2.500
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| 111 | REMARK 3
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| 112 | REMARK 3 NCS MODEL : NULL
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| 113 | REMARK 3
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| 114 | REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
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| 115 | REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
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| 116 | REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
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| 117 | REMARK 3
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| 118 | REMARK 3 PARAMETER FILE 1 : PARAM19X.SOL
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| 119 | REMARK 3 PARAMETER FILE 2 : NULL
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| 120 | REMARK 3 TOPOLOGY FILE 1 : TOPH19.SOL
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| 121 | REMARK 3 TOPOLOGY FILE 2 : NULL
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| 122 | REMARK 3
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| 123 | REMARK 3 OTHER REFINEMENT REMARKS: NULL
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| 124 | REMARK 4
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| 125 | REMARK 4 1FVM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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| 126 | REMARK 100
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| 127 | REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-00.
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| 128 | REMARK 100 THE RCSB ID CODE IS RCSB011937.
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| 129 | REMARK 200
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| 130 | REMARK 200 EXPERIMENTAL DETAILS
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| 131 | REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
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| 132 | REMARK 200 DATE OF DATA COLLECTION : 24-JUN-00
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| 133 | REMARK 200 TEMPERATURE (KELVIN) : 120
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| 134 | REMARK 200 PH : 8.5
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| 135 | REMARK 200 NUMBER OF CRYSTALS USED : 1
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| 136 | REMARK 200
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| 137 | REMARK 200 SYNCHROTRON (Y/N) : Y
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| 138 | REMARK 200 RADIATION SOURCE : PHOTON FACTORY
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| 139 | REMARK 200 BEAMLINE : BL-6A
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| 140 | REMARK 200 X-RAY GENERATOR MODEL : NULL
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| 141 | REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
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| 142 | REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
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| 143 | REMARK 200 MONOCHROMATOR : FOCUSSING SILICON CRYSTAL
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| 144 | REMARK 200 OPTICS : MIRRORS
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| 145 | REMARK 200
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| 146 | REMARK 200 DETECTOR TYPE : CCD
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| 147 | REMARK 200 DETECTOR MANUFACTURER : ADSC QUAMTUM 4R
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| 148 | REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
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| 149 | REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
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| 150 | REMARK 200
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| 151 | REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8400
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| 152 | REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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| 153 | REMARK 200 RESOLUTION RANGE LOW (A) : 25.500
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| 154 | REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
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| 155 | REMARK 200
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| 156 | REMARK 200 OVERALL.
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| 157 | REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
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| 158 | REMARK 200 DATA REDUNDANCY : 6.800
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| 159 | REMARK 200 R MERGE (I) : 0.04600
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| 160 | REMARK 200 R SYM (I) : 0.04300
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| 161 | REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
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| 162 | REMARK 200
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| 163 | REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
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| 164 | REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
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| 165 | REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
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| 166 | REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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| 167 | REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
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| 168 | REMARK 200 R MERGE FOR SHELL (I) : 0.07200
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| 169 | REMARK 200 R SYM FOR SHELL (I) : 0.06600
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| 170 | REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.500
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| 171 | REMARK 200
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| 172 | REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
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| 173 | REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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| 174 | REMARK 200 SOFTWARE USED: AMORE
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| 175 | REMARK 200 STARTING MODEL: PDB ENTRY 1AA5
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| 176 | REMARK 200
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| 177 | REMARK 200 REMARK: NULL
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| 178 | REMARK 280
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| 179 | REMARK 280 CRYSTAL
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| 180 | REMARK 280 SOLVENT CONTENT, VS (%): 37.10
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| 181 | REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
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| 182 | REMARK 280
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| 183 | REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE PREPARED AT 293K FROM A
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| 184 | REMARK 280 SOLUTION CONTAINING 6.6 MM VANCOMYCIN, 6.6 MM DI- ACETYL-LYS -D-
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| 185 | REMARK 280 ALA-D-ALA, 3.3 % (V/V) ETHANOL, AND 0.66 M TRIS BUFFER PH 8.5, BY
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| 186 | REMARK 280 EQUILIBRATING THE SOLUTION AGAINST A RESERVOIR SOLUTION
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| 187 | REMARK 280 CONTAINING 10 % (V/V) ETHANOL AND 0.2 M TRIS BUFFER PH 8.5, VAPOR
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| 188 | REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
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| 189 | REMARK 290
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| 190 | REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
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| 191 | REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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| 192 | REMARK 290
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| 193 | REMARK 290 SYMOP SYMMETRY
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| 194 | REMARK 290 NNNMMM OPERATOR
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| 195 | REMARK 290 1555 X,Y,Z
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| 196 | REMARK 290 2555 -X+1/2,-Y,Z+1/2
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| 197 | REMARK 290 3555 -X,Y+1/2,-Z+1/2
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| 198 | REMARK 290 4555 X+1/2,-Y+1/2,-Z
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| 199 | REMARK 290
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| 200 | REMARK 290 WHERE NNN -> OPERATOR NUMBER
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| 201 | REMARK 290 MMM -> TRANSLATION VECTOR
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| 202 | REMARK 290
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| 203 | REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
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| 204 | REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
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| 205 | REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
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| 206 | REMARK 290 RELATED MOLECULES.
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| 207 | REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
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| 208 | REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
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| 209 | REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
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| 210 | REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 17.81850
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| 211 | REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
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| 212 | REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.86400
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| 213 | REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
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| 214 | REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.21250
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| 215 | REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.86400
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| 216 | REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.81850
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| 217 | REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 18.21250
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| 218 | REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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| 219 | REMARK 290
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| 220 | REMARK 290 REMARK: NULL
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| 221 | REMARK 300
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| 222 | REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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| 223 | REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
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| 224 | REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
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| 225 | REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
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| 226 | REMARK 300 BURIED SURFACE AREA.
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| 227 | REMARK 350
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| 228 | REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
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| 229 | REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
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| 230 | REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
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| 231 | REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
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| 232 | REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
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| 233 | REMARK 350
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| 234 | REMARK 350 BIOMOLECULE: 1
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| 235 | REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
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| 236 | REMARK 350 SOFTWARE USED: PISA 1.18
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| 237 | REMARK 350 TOTAL BURIED SURFACE AREA: 910 ANGSTROM**2
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| 238 | REMARK 350 SURFACE AREA OF THE COMPLEX: 1540 ANGSTROM**2
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| 239 | REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.9 KCAL/MOL
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| 240 | REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G
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| 241 | REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
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| 242 | REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
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| 243 | REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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| 244 | REMARK 350
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| 245 | REMARK 350 BIOMOLECULE: 2
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| 246 | REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
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| 247 | REMARK 350 SOFTWARE USED: PISA 1.18
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| 248 | REMARK 350 TOTAL BURIED SURFACE AREA: 960 ANGSTROM**2
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| 249 | REMARK 350 SURFACE AREA OF THE COMPLEX: 1480 ANGSTROM**2
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| 250 | REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.6 KCAL/MOL
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| 251 | REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H
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| 252 | REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
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| 253 | REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
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| 254 | REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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| 255 | REMARK 350
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| 256 | REMARK 350 BIOMOLECULE: 3
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| 257 | REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
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| 258 | REMARK 350 SOFTWARE USED: PISA 1.18
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| 259 | REMARK 350 TOTAL BURIED SURFACE AREA: 940 ANGSTROM**2
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| 260 | REMARK 350 SURFACE AREA OF THE COMPLEX: 1540 ANGSTROM**2
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| 261 | REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.6 KCAL/MOL
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| 262 | REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
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| 263 | REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
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| 264 | REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
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| 265 | REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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| 266 | REMARK 350
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| 267 | REMARK 350 BIOMOLECULE: 4
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| 268 | REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
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| 269 | REMARK 350 SOFTWARE USED: PISA 1.18
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| 270 | REMARK 350 TOTAL BURIED SURFACE AREA: 800 ANGSTROM**2
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| 271 | REMARK 350 SURFACE AREA OF THE COMPLEX: 1630 ANGSTROM**2
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| 272 | REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.7 KCAL/MOL
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| 273 | REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J
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| 274 | REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
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| 275 | REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
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| 276 | REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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| 277 | REMARK 350
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| 278 | REMARK 350 BIOMOLECULE: 5
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| 279 | REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
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| 280 | REMARK 350 SOFTWARE USED: PISA 1.18
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| 281 | REMARK 350 TOTAL BURIED SURFACE AREA: 970 ANGSTROM**2
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| 282 | REMARK 350 SURFACE AREA OF THE COMPLEX: 1430 ANGSTROM**2
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| 283 | REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.2 KCAL/MOL
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| 284 | REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K
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| 285 | REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
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| 286 | REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
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| 287 | REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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| 288 | REMARK 350
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| 289 | REMARK 350 BIOMOLECULE: 6
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| 290 | REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
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| 291 | REMARK 350 SOFTWARE USED: PISA 1.18
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| 292 | REMARK 350 TOTAL BURIED SURFACE AREA: 820 ANGSTROM**2
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| 293 | REMARK 350 SURFACE AREA OF THE COMPLEX: 1640 ANGSTROM**2
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| 294 | REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.7 KCAL/MOL
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| 295 | REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L
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| 296 | REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
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| 297 | REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
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| 298 | REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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| 299 | REMARK 400
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| 300 | REMARK 400 COMPOUND
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| 301 | REMARK 400 VANCOMYCIN IS A TRICYCLIC GLYCOPEPTIDE. THE SCAFFOLD IS
|
|---|
| 302 | REMARK 400 A HEPTAPEPTIDE WITH THE CONFIGURATION D-D-L-D-D-L-L. IT IS
|
|---|
| 303 | REMARK 400 FURTHER GLYCOSYLATED BY A DISACCHARIDE MADE OF D-GLUCOSE
|
|---|
| 304 | REMARK 400 AND VANCOSAMINE.
|
|---|
| 305 | REMARK 400 HERE, VANCOMYCIN IS REPRESENTED BY GROUPING TOGETHER THE
|
|---|
| 306 | REMARK 400 SEQUENCE (SEQRES) AND THE TWO LIGANDS (HET) BGC AND RER.
|
|---|
| 307 | REMARK 400
|
|---|
| 308 | REMARK 400 GROUP: 1
|
|---|
| 309 | REMARK 400 NAME: VANCOMYCIN
|
|---|
| 310 | REMARK 400 CHAIN: A, B, C , D, E, F
|
|---|
| 311 | REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 7
|
|---|
| 312 | REMARK 400 COMPONENT_2: SUGAR RESIDUES 8, 9
|
|---|
| 313 | REMARK 400 DESCRIPTION: VANCOMYCIN IS A TRICYCLIC GLYCOPEPTIDE,
|
|---|
| 314 | REMARK 400 GLYCOSYLATED BY A DISACCHARIDE (RESIDUES 8
|
|---|
| 315 | REMARK 400 AND 9) ON RESIDUE 4.
|
|---|
| 316 | REMARK 500
|
|---|
| 317 | REMARK 500 GEOMETRY AND STEREOCHEMISTRY
|
|---|
| 318 | REMARK 500 SUBTOPIC: TORSION ANGLES
|
|---|
| 319 | REMARK 500
|
|---|
| 320 | REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
|
|---|
| 321 | REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
|
|---|
| 322 | REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
|
|---|
| 323 | REMARK 500
|
|---|
| 324 | REMARK 500 STANDARD TABLE:
|
|---|
| 325 | REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
|
|---|
| 326 | REMARK 500
|
|---|
| 327 | REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
|
|---|
| 328 | REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
|
|---|
| 329 | REMARK 500
|
|---|
| 330 | REMARK 500 M RES CSSEQI PSI PHI
|
|---|
| 331 | REMARK 500 ASN B 3 -58.41 -126.84
|
|---|
| 332 | REMARK 500 ASN D 3 -62.46 -102.93
|
|---|
| 333 | REMARK 500 ASN E 3 -71.29 -114.68
|
|---|
| 334 | REMARK 500 ASN F 3 -68.28 -105.07
|
|---|
| 335 | REMARK 500
|
|---|
| 336 | REMARK 500 REMARK: NULL
|
|---|
| 337 | REMARK 800
|
|---|
| 338 | REMARK 800 SITE
|
|---|
| 339 | REMARK 800 SITE_IDENTIFIER: AC1
|
|---|
| 340 | REMARK 800 EVIDENCE_CODE: SOFTWARE
|
|---|
| 341 | REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF VANCOMYCIN
|
|---|
| 342 | REMARK 800
|
|---|
| 343 | REMARK 800 SITE_IDENTIFIER: AC2
|
|---|
| 344 | REMARK 800 EVIDENCE_CODE: SOFTWARE
|
|---|
| 345 | REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF VANCOMYCIN
|
|---|
| 346 | REMARK 800
|
|---|
| 347 | REMARK 800 SITE_IDENTIFIER: AC3
|
|---|
| 348 | REMARK 800 EVIDENCE_CODE: SOFTWARE
|
|---|
| 349 | REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF VANCOMYCIN
|
|---|
| 350 | REMARK 800
|
|---|
| 351 | REMARK 800 SITE_IDENTIFIER: AC4
|
|---|
| 352 | REMARK 800 EVIDENCE_CODE: SOFTWARE
|
|---|
| 353 | REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF VANCOMYCIN
|
|---|
| 354 | REMARK 800
|
|---|
| 355 | REMARK 800 SITE_IDENTIFIER: AC5
|
|---|
| 356 | REMARK 800 EVIDENCE_CODE: SOFTWARE
|
|---|
| 357 | REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF VANCOMYCIN
|
|---|
| 358 | REMARK 800
|
|---|
| 359 | REMARK 800 SITE_IDENTIFIER: AC6
|
|---|
| 360 | REMARK 800 EVIDENCE_CODE: SOFTWARE
|
|---|
| 361 | REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF VANCOMYCIN
|
|---|
| 362 | REMARK 900
|
|---|
| 363 | REMARK 900 RELATED ENTRIES
|
|---|
| 364 | REMARK 900 RELATED ID: 1AA5 RELATED DB: PDB
|
|---|
| 365 | REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN
|
|---|
| 366 | REMARK 900 RELATED ID: 1C0Q RELATED DB: PDB
|
|---|
| 367 | REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN COMPLEXED WITH 2-ACETOXY-D-
|
|---|
| 368 | REMARK 900 PROPANOIC ACID
|
|---|
| 369 | REMARK 900 RELATED ID: 1C0R RELATED DB: PDB
|
|---|
| 370 | REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN WITH D-LACTIC ACID
|
|---|
| 371 | REMARK 900 RELATED ID: 1GAC RELATED DB: PDB
|
|---|
| 372 | REMARK 900 SOLUTION STRUCTURE OF A82846B COMPLEXED WITH ITS CELL WALL
|
|---|
| 373 | REMARK 900 PENTAPEPTIDE FRAGMENT
|
|---|
| 374 | REMARK 900 RELATED ID: 1GHG RELATED DB: PDB
|
|---|
| 375 | REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON
|
|---|
| 376 | REMARK 900 RELATED ID: 1PN3 RELATED DB: PDB
|
|---|
| 377 | REMARK 900 CRYSTAL STRUCTURE OF TDP-EPI-VANCOSAMINYLTRANSFERASE GTFA
|
|---|
| 378 | REMARK 900 COMPLEXD WITH TDP AND DESVANCOSAMINYL VANCOMYCIN
|
|---|
| 379 | REMARK 900 RELATED ID: 1PNV RELATED DB: PDB
|
|---|
| 380 | REMARK 900 CRYSTAL STRUCTURE OF TDP-EPI-VANCOSAMINYLTRANSFERASE GTFA
|
|---|
| 381 | REMARK 900 COMPLEXED WITH TDP AND VANCOMYCIN
|
|---|
| 382 | REMARK 900 RELATED ID: 1QD8 RELATED DB: PDB
|
|---|
| 383 | REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN COMPLEXED WITH N-ACETYL
|
|---|
| 384 | REMARK 900 GLYCIN
|
|---|
| 385 | REMARK 900 RELATED ID: 1RRV RELATED DB: PDB
|
|---|
| 386 | REMARK 900 CRYSTAL STRUCTURE OF TDP-VANCOSAMINYLTRANSFERASE GTFD
|
|---|
| 387 | REMARK 900 COMPLEXED WITH TDP AND DESVANCOSAMINYL VANCOMYCIN.
|
|---|
| 388 | REMARK 900 RELATED ID: 1SHO RELATED DB: PDB
|
|---|
| 389 | REMARK 900 CRYSTAL STRUCTURE OF VANCOMYCIN
|
|---|
| 390 | DBREF 1FVM A 1 7 NOR NOR00681 NOR00681 1 7
|
|---|
| 391 | SEQRES 1 A 7 MLU OMZ ASN GHP GHP OMY 3FG
|
|---|
| 392 | HET MLU A 1 9
|
|---|
| 393 | HET OMZ A 2 14
|
|---|
| 394 | HET GHP A 4 11
|
|---|
| 395 | HET GHP A 5 11
|
|---|
| 396 | HET OMY A 6 14
|
|---|
| 397 | HET 3FG A 7 13
|
|---|
| 398 | HET BGC A 8 11
|
|---|
| 399 | HET RER A 9 10
|
|---|
| 400 | HETNAM MLU N-METHYLLEUCINE
|
|---|
| 401 | HETNAM OMZ (BETAR)-3-CHLORO-BETA-HYDROXY-D-TYROSINE
|
|---|
| 402 | HETNAM GHP (2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC ACID
|
|---|
| 403 | HETNAM OMY (BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE
|
|---|
| 404 | HETNAM 3FG (2S)-AMINO(3,5-DIHYDROXYPHENYL)ETHANOIC ACID
|
|---|
| 405 | HETNAM DLS DI-ACETYL-LYSINE
|
|---|
| 406 | HETNAM DAL D-ALANINE
|
|---|
| 407 | HETNAM BGC BETA-D-GLUCOSE
|
|---|
| 408 | HETNAM RER (1R,3S,4S,5S)-3-AMINO-2,3,6-TRIDEOXY-3-METHYL-ALPHA-L-
|
|---|
| 409 | HETNAM 2 RER ARABINO-HEXOPYRANOSE
|
|---|
| 410 | HETSYN RER VANCOSAMINE
|
|---|
| 411 | FORMUL 1 MLU 6(C7 H15 N O2)
|
|---|
| 412 | FORMUL 1 OMZ 6(C9 H10 CL N O4)
|
|---|
| 413 | FORMUL 1 GHP 12(C8 H9 N O3)
|
|---|
| 414 | FORMUL 1 OMY 6(C9 H10 CL N O4)
|
|---|
| 415 | FORMUL 1 3FG 6(C8 H9 N O4)
|
|---|
| 416 | FORMUL 7 DLS 6(C10 H18 N2 O4)
|
|---|
| 417 | FORMUL 7 DAL 12(C3 H7 N O2)
|
|---|
| 418 | FORMUL 3 BGC 6(C6 H12 O6)
|
|---|
| 419 | FORMUL 3 RER 6(C7 H15 N O3)
|
|---|
| 420 | FORMUL 9 HOH *112(H2 O)
|
|---|
| 421 | LINK C MLU A 1 N OMZ A 2 1555 1555 1.350
|
|---|
| 422 | LINK C OMZ A 2 N ASN A 3 1555 1555 1.360
|
|---|
| 423 | LINK OH OMZ A 2 C5 GHP A 4 1555 1555 1.410
|
|---|
| 424 | LINK C ASN A 3 N GHP A 4 1555 1555 1.330
|
|---|
| 425 | LINK C GHP A 4 N GHP A 5 1555 1555 1.340
|
|---|
| 426 | LINK C3 GHP A 4 OCZ OMY A 6 1555 1555 1.400
|
|---|
| 427 | LINK O4 GHP A 4 C1 BGC A 8 1555 1555 1.390
|
|---|
| 428 | LINK C GHP A 5 N OMY A 6 1555 1555 1.350
|
|---|
| 429 | LINK C3 GHP A 5 CG1 3FG A 7 1555 1555 1.500
|
|---|
| 430 | LINK C OMY A 6 N 3FG A 7 1555 1555 1.340
|
|---|
| 431 | LINK O2 BGC A 8 C1 RER A 9 1555 1555 1.420
|
|---|
| 432 | LINK C OMY B 6 N 3FG B 7 1555 1555 1.330
|
|---|
| 433 | LINK C ASN E 3 N GHP E 4 1555 1555 1.320
|
|---|
| 434 | LINK C OMY E 6 N 3FG E 7 1555 1555 1.340
|
|---|
| 435 | CISPEP 1 GHP A 5 OMY A 6 0 1.25
|
|---|
| 436 | SITE 1 AC1 43 HOH A2001 HOH A2005 HOH A2006 HOH A2007
|
|---|
| 437 | SITE 2 AC1 43 HOH A2008 HOH A2009 HOH A2010 HOH A2011
|
|---|
| 438 | SITE 3 AC1 43 HOH A2012 HOH A2013 HOH A2014 HOH A2015
|
|---|
| 439 | SITE 4 AC1 43 HOH A2017 HOH A2018 HOH A2019 HOH A2020
|
|---|
| 440 | SITE 5 AC1 43 ASN B 3 GHP B 4 GHP B 5 OMY B 6
|
|---|
| 441 | SITE 6 AC1 43 BGC B 8 RER B 9 HOH B2004 HOH B2008
|
|---|
| 442 | SITE 7 AC1 43 HOH B2015 GHP C 5 MLU D 1 OMZ D 2
|
|---|
| 443 | SITE 8 AC1 43 ASN D 3 GHP D 5 3FG D 7 MLU E 1
|
|---|
| 444 | SITE 9 AC1 43 BGC E 8 HOH E2001 HOH E2020 MLU F 1
|
|---|
| 445 | SITE 10 AC1 43 BGC F 8 RER F 9 DLS G 1 DAL G 2
|
|---|
| 446 | SITE 11 AC1 43 DAL G 3 HOH G2002 DLS J 1
|
|---|
| 447 | SITE 1 AC2 37 OMZ A 2 ASN A 3 GHP A 4 GHP A 5
|
|---|
| 448 | SITE 2 AC2 37 OMY A 6 BGC A 8 RER A 9 HOH A2006
|
|---|
| 449 | SITE 3 AC2 37 HOH B2002 HOH B2003 HOH B2004 HOH B2007
|
|---|
| 450 | SITE 4 AC2 37 HOH B2008 HOH B2009 HOH B2010 HOH B2011
|
|---|
| 451 | SITE 5 AC2 37 HOH B2012 HOH B2013 HOH B2014 HOH B2015
|
|---|
| 452 | SITE 6 AC2 37 MLU C 1 MLU D 1 OMY D 6 3FG D 7
|
|---|
| 453 | SITE 7 AC2 37 RER D 9 HOH D2008 HOH D2009 HOH E2004
|
|---|
| 454 | SITE 8 AC2 37 MLU F 1 OMZ F 2 ASN F 3 GHP F 5
|
|---|
| 455 | SITE 9 AC2 37 3FG F 7 DLS H 1 DAL H 2 DAL H 3
|
|---|
| 456 | SITE 10 AC2 37 DLS J 1
|
|---|
| 457 | SITE 1 AC3 35 3FG A 7 HOH A2012 MLU B 1 HOH B2014
|
|---|
| 458 | SITE 2 AC3 35 HOH C2003 HOH C2004 HOH C2006 HOH C2008
|
|---|
| 459 | SITE 3 AC3 35 HOH C2009 HOH C2010 HOH C2011 HOH C2012
|
|---|
| 460 | SITE 4 AC3 35 HOH C2013 HOH C2014 OMZ D 2 ASN D 3
|
|---|
| 461 | SITE 5 AC3 35 GHP D 4 GHP D 5 OMY D 6 BGC D 8
|
|---|
| 462 | SITE 6 AC3 35 RER D 9 HOH D2005 HOH D2008 GHP E 5
|
|---|
| 463 | SITE 7 AC3 35 3FG E 7 HOH E2013 HOH E2019 HOH E2021
|
|---|
| 464 | SITE 8 AC3 35 3FG F 7 DLS H 1 DLS I 1 DAL I 2
|
|---|
| 465 | SITE 9 AC3 35 DAL I 3 DLS K 1 HOH K2001
|
|---|
| 466 | SITE 1 AC4 47 MLU A 1 ASN A 3 GHP A 4 GHP A 5
|
|---|
| 467 | SITE 2 AC4 47 3FG A 7 RER A 9 HOH A2012 GHP B 5
|
|---|
| 468 | SITE 3 AC4 47 OMY B 6 3FG B 7 RER B 9 HOH B2014
|
|---|
| 469 | SITE 4 AC4 47 OMZ C 2 ASN C 3 GHP C 4 GHP C 5
|
|---|
| 470 | SITE 5 AC4 47 OMY C 6 BGC C 8 HOH C2010 HOH C2012
|
|---|
| 471 | SITE 6 AC4 47 HOH D2001 HOH D2003 HOH D2004 HOH D2005
|
|---|
| 472 | SITE 7 AC4 47 HOH D2007 HOH D2008 HOH D2009 HOH D2010
|
|---|
| 473 | SITE 8 AC4 47 HOH D2011 HOH D2012 HOH D2013 MLU E 1
|
|---|
| 474 | SITE 9 AC4 47 OMZ E 2 ASN E 3 HOH E2003 HOH E2004
|
|---|
| 475 | SITE 10 AC4 47 MLU F 1 GHP F 5 OMY F 6 3FG F 7
|
|---|
| 476 | SITE 11 AC4 47 DAL G 2 HOH G2002 DLS J 1 DAL J 2
|
|---|
| 477 | SITE 12 AC4 47 DAL J 3 DLS L 1 DAL L 3
|
|---|
| 478 | SITE 1 AC5 40 MLU A 1 ASN A 3 RER A 9 HOH A2014
|
|---|
| 479 | SITE 2 AC5 40 HOH A2019 HOH B2010 MLU C 1 OMZ C 2
|
|---|
| 480 | SITE 3 AC5 40 RER C 9 HOH C2003 OMZ D 2 RER D 9
|
|---|
| 481 | SITE 4 AC5 40 HOH D2003 HOH E2001 HOH E2003 HOH E2004
|
|---|
| 482 | SITE 5 AC5 40 HOH E2006 HOH E2007 HOH E2008 HOH E2010
|
|---|
| 483 | SITE 6 AC5 40 HOH E2011 HOH E2012 HOH E2013 HOH E2015
|
|---|
| 484 | SITE 7 AC5 40 HOH E2017 HOH E2018 HOH E2019 HOH E2020
|
|---|
| 485 | SITE 8 AC5 40 HOH E2021 OMZ F 2 ASN F 3 GHP F 4
|
|---|
| 486 | SITE 9 AC5 40 GHP F 5 OMY F 6 BGC F 8 RER F 9
|
|---|
| 487 | SITE 10 AC5 40 DLS K 1 DAL K 2 DAL K 3 DLS L 1
|
|---|
| 488 | SITE 1 AC6 45 GHP A 5 3FG A 7 HOH A2009 HOH A2011
|
|---|
| 489 | SITE 2 AC6 45 MLU B 1 ASN B 3 GHP B 4 GHP B 5
|
|---|
| 490 | SITE 3 AC6 45 3FG B 7 HOH B2003 RER C 9 MLU D 1
|
|---|
| 491 | SITE 4 AC6 45 3FG D 7 RER D 9 HOH D2007 OMZ E 2
|
|---|
| 492 | SITE 5 AC6 45 ASN E 3 GHP E 4 GHP E 5 OMY E 6
|
|---|
| 493 | SITE 6 AC6 45 BGC E 8 RER E 9 HOH E2003 HOH E2017
|
|---|
| 494 | SITE 7 AC6 45 HOH F2001 HOH F2002 HOH F2003 HOH F2004
|
|---|
| 495 | SITE 8 AC6 45 HOH F2006 HOH F2007 HOH F2008 HOH F2009
|
|---|
| 496 | SITE 9 AC6 45 HOH F2010 HOH F2011 HOH F2012 HOH F2013
|
|---|
| 497 | SITE 10 AC6 45 HOH F2014 DLS G 1 DAL H 2 DLS J 1
|
|---|
| 498 | SITE 11 AC6 45 DAL J 3 DLS L 1 DAL L 2 DAL L 3
|
|---|
| 499 | SITE 12 AC6 45 HOH L2002
|
|---|
| 500 | CRYST1 35.637 36.425 65.728 90.00 90.00 90.00 P 21 21 21 24
|
|---|
| 501 | ORIGX1 1.000000 0.000000 0.000000 0.00000
|
|---|
| 502 | ORIGX2 0.000000 1.000000 0.000000 0.00000
|
|---|
| 503 | ORIGX3 0.000000 0.000000 1.000000 0.00000
|
|---|
| 504 | SCALE1 0.028061 0.000000 0.000000 0.00000
|
|---|
| 505 | SCALE2 0.000000 0.027454 0.000000 0.00000
|
|---|
| 506 | SCALE3 0.000000 0.000000 0.015214 0.00000
|
|---|
| 507 | HETATM 1 N MLU A 1 -3.746 5.901 32.054 1.00 10.57 N
|
|---|
| 508 | HETATM 2 CN MLU A 1 -3.475 7.242 32.631 1.00 8.78 C
|
|---|
| 509 | HETATM 3 CA MLU A 1 -2.685 5.427 31.112 1.00 9.32 C
|
|---|
| 510 | HETATM 4 C MLU A 1 -1.421 5.090 31.923 1.00 8.61 C
|
|---|
| 511 | HETATM 5 O MLU A 1 -1.513 4.700 33.076 1.00 9.05 O
|
|---|
| 512 | HETATM 6 CB MLU A 1 -3.118 4.163 30.379 1.00 9.04 C
|
|---|
| 513 | HETATM 7 CG MLU A 1 -4.319 4.218 29.421 1.00 9.77 C
|
|---|
| 514 | HETATM 8 CD1 MLU A 1 -4.059 5.124 28.278 1.00 10.82 C
|
|---|
| 515 | HETATM 9 CD2 MLU A 1 -4.576 2.810 28.898 1.00 9.78 C
|
|---|
| 516 | HETATM 10 N OMZ A 2 -0.235 5.218 31.294 1.00 6.08 N
|
|---|
| 517 | HETATM 11 CA OMZ A 2 0.978 4.864 32.003 1.00 5.01 C
|
|---|
| 518 | HETATM 12 C OMZ A 2 1.662 3.635 31.326 1.00 4.61 C
|
|---|
| 519 | HETATM 13 O OMZ A 2 2.575 3.062 31.906 1.00 5.14 O
|
|---|
| 520 | HETATM 14 CB OMZ A 2 2.027 6.038 32.141 1.00 4.44 C
|
|---|
| 521 | HETATM 15 OC OMZ A 2 1.433 7.179 32.740 1.00 4.06 O
|
|---|
| 522 | HETATM 16 CG OMZ A 2 2.569 6.364 30.789 1.00 3.67 C
|
|---|
| 523 | HETATM 17 CD1 OMZ A 2 3.801 5.827 30.401 1.00 4.01 C
|
|---|
| 524 | HETATM 18 CD2 OMZ A 2 1.864 7.179 29.891 1.00 3.84 C
|
|---|
| 525 | HETATM 19 CE1 OMZ A 2 4.303 6.094 29.141 1.00 4.09 C
|
|---|
| 526 | HETATM 20 CL OMZ A 2 5.831 5.416 28.686 1.00 8.11 CL
|
|---|
| 527 | HETATM 21 CE2 OMZ A 2 2.373 7.428 28.646 1.00 4.57 C
|
|---|
| 528 | HETATM 22 CZ OMZ A 2 3.591 6.878 28.268 1.00 4.83 C
|
|---|
| 529 | HETATM 23 OH OMZ A 2 4.054 7.131 26.998 1.00 5.04 O
|
|---|
| 530 | ATOM 24 N ASN A 3 1.188 3.256 30.112 1.00 4.73 N
|
|---|
| 531 | ATOM 25 CA ASN A 3 1.417 1.890 29.560 1.00 3.50 C
|
|---|
| 532 | ATOM 26 C ASN A 3 2.244 1.907 28.261 1.00 4.88 C
|
|---|
| 533 | ATOM 27 O ASN A 3 3.333 1.308 28.249 1.00 5.87 O
|
|---|
| 534 | ATOM 28 CB ASN A 3 0.102 1.184 29.350 1.00 3.14 C
|
|---|
| 535 | ATOM 29 CG ASN A 3 -0.781 1.101 30.578 1.00 4.06 C
|
|---|
| 536 | ATOM 30 OD1 ASN A 3 -0.314 1.300 31.722 1.00 4.73 O
|
|---|
| 537 | ATOM 31 ND2 ASN A 3 -2.053 0.803 30.327 1.00 2.84 N
|
|---|
| 538 | HETATM 32 N GHP A 4 1.738 2.541 27.211 1.00 5.12 N
|
|---|
| 539 | HETATM 33 CA GHP A 4 2.385 2.522 25.880 1.00 3.80 C
|
|---|
| 540 | HETATM 34 C GHP A 4 1.348 2.089 24.857 1.00 2.61 C
|
|---|
| 541 | HETATM 35 O GHP A 4 0.200 2.489 24.883 1.00 1.31 O
|
|---|
| 542 | HETATM 36 C1 GHP A 4 2.989 3.880 25.476 1.00 4.69 C
|
|---|
| 543 | HETATM 37 C2 GHP A 4 3.283 4.160 24.166 1.00 4.12 C
|
|---|
| 544 | HETATM 38 C3 GHP A 4 3.817 5.405 23.798 1.00 4.42 C
|
|---|
| 545 | HETATM 39 C4 GHP A 4 4.054 6.371 24.759 1.00 4.66 C
|
|---|
| 546 | HETATM 40 O4 GHP A 4 4.566 7.616 24.439 1.00 5.85 O
|
|---|
| 547 | HETATM 41 C5 GHP A 4 3.772 6.098 26.079 1.00 3.99 C
|
|---|
| 548 | HETATM 42 C6 GHP A 4 3.241 4.865 26.431 1.00 4.60 C
|
|---|
| 549 | HETATM 43 N GHP A 5 1.822 1.258 23.915 1.00 0.96 N
|
|---|
| 550 | HETATM 44 CA GHP A 5 1.166 1.059 22.652 1.00 1.29 C
|
|---|
| 551 | HETATM 45 C GHP A 5 2.246 0.795 21.569 1.00 2.40 C
|
|---|
| 552 | HETATM 46 O GHP A 5 3.327 0.339 21.938 1.00 4.26 O
|
|---|
| 553 | HETATM 47 C1 GHP A 5 0.162 -0.091 22.505 1.00 1.47 C
|
|---|
| 554 | HETATM 48 C2 GHP A 5 -1.092 0.174 22.007 1.00 1.74 C
|
|---|
| 555 | HETATM 49 C3 GHP A 5 -2.027 -0.838 21.722 1.00 1.60 C
|
|---|
| 556 | HETATM 50 C4 GHP A 5 -1.648 -2.172 21.974 1.00 3.17 C
|
|---|
| 557 | HETATM 51 O4 GHP A 5 -2.557 -3.167 21.701 1.00 1.84 O
|
|---|
| 558 | HETATM 52 C5 GHP A 5 -0.388 -2.443 22.487 1.00 2.35 C
|
|---|
| 559 | HETATM 53 C6 GHP A 5 0.520 -1.423 22.757 1.00 1.94 C
|
|---|
| 560 | HETATM 54 N OMY A 6 1.982 1.063 20.272 1.00 2.26 N
|
|---|
| 561 | HETATM 55 CA OMY A 6 0.799 1.608 19.695 1.00 2.41 C
|
|---|
| 562 | HETATM 56 OCZ OMY A 6 4.127 5.744 22.477 1.00 3.34 O
|
|---|
| 563 | HETATM 57 CE2 OMY A 6 4.110 4.269 20.620 1.00 3.22 C
|
|---|
| 564 | HETATM 58 CE1 OMY A 6 2.025 5.179 21.396 1.00 4.18 C
|
|---|
| 565 | HETATM 59 CZ OMY A 6 3.417 5.078 21.512 1.00 3.75 C
|
|---|
| 566 | HETATM 60 CG OMY A 6 2.023 3.674 19.561 1.00 2.22 C
|
|---|
| 567 | HETATM 61 CD2 OMY A 6 3.426 3.573 19.645 1.00 3.21 C
|
|---|
| 568 | HETATM 62 CD1 OMY A 6 1.333 4.501 20.447 1.00 2.93 C
|
|---|
| 569 | HETATM 63 CB OMY A 6 1.205 2.764 18.680 1.00 1.63 C
|
|---|
| 570 | HETATM 64 CL OMY A 6 1.100 6.199 22.491 1.00 5.78 CL
|
|---|
| 571 | HETATM 65 O OMY A 6 0.409 -0.463 18.522 1.00 2.26 O
|
|---|
| 572 | HETATM 66 C OMY A 6 -0.081 0.543 19.032 1.00 1.86 C
|
|---|
| 573 | HETATM 67 ODE OMY A 6 1.911 2.221 17.605 1.00 3.88 O
|
|---|
| 574 | HETATM 68 N 3FG A 7 -1.392 0.809 19.070 1.00 1.71 N
|
|---|
| 575 | HETATM 69 OD1 3FG A 7 -4.360 -0.595 23.349 1.00 3.94 O
|
|---|
| 576 | HETATM 70 CD1 3FG A 7 -4.452 -0.308 22.038 1.00 2.77 C
|
|---|
| 577 | HETATM 71 CG1 3FG A 7 -3.359 -0.414 21.175 1.00 2.34 C
|
|---|
| 578 | HETATM 72 CZ 3FG A 7 -5.715 0.107 21.567 1.00 2.86 C
|
|---|
| 579 | HETATM 73 CD2 3FG A 7 -5.894 0.415 20.242 1.00 2.08 C
|
|---|
| 580 | HETATM 74 OD2 3FG A 7 -7.059 0.824 19.723 1.00 4.33 O
|
|---|
| 581 | HETATM 75 CG2 3FG A 7 -4.804 0.303 19.348 1.00 1.77 C
|
|---|
| 582 | HETATM 76 CB 3FG A 7 -3.545 -0.110 19.807 1.00 2.44 C
|
|---|
| 583 | HETATM 77 CA 3FG A 7 -2.357 -0.246 18.836 1.00 2.54 C
|
|---|
| 584 | HETATM 78 C 3FG A 7 -2.843 -0.276 17.326 1.00 3.22 C
|
|---|
| 585 | HETATM 79 O 3FG A 7 -3.443 -1.350 17.022 1.00 3.30 O
|
|---|
| 586 | HETATM 80 OXT 3FG A 7 -2.621 0.668 16.610 1.00 2.62 O
|
|---|
| 587 | TER 81 3FG A 7
|
|---|
| 588 | HETATM 649 C2 BGC A 8 6.098 9.043 23.441 1.00 5.35 C
|
|---|
| 589 | HETATM 650 C3 BGC A 8 7.539 9.282 23.038 1.00 6.82 C
|
|---|
| 590 | HETATM 651 C4 BGC A 8 8.436 8.896 24.249 1.00 6.08 C
|
|---|
| 591 | HETATM 652 C5 BGC A 8 8.090 7.464 24.707 1.00 7.35 C
|
|---|
| 592 | HETATM 653 C6 BGC A 8 8.882 6.966 25.969 1.00 7.83 C
|
|---|
| 593 | HETATM 654 C1 BGC A 8 5.878 7.663 23.980 1.00 5.36 C
|
|---|
| 594 | HETATM 655 O2 BGC A 8 5.254 9.272 22.275 1.00 4.98 O
|
|---|
| 595 | HETATM 656 O3 BGC A 8 7.794 10.614 22.633 1.00 6.23 O
|
|---|
| 596 | HETATM 657 O4 BGC A 8 9.802 8.940 23.867 1.00 7.22 O
|
|---|
| 597 | HETATM 658 O5 BGC A 8 6.725 7.410 25.070 1.00 5.94 O
|
|---|
| 598 | HETATM 659 O6 BGC A 8 8.640 7.743 27.058 1.00 10.67 O
|
|---|
| 599 | HETATM 660 C1 RER A 9 4.555 10.505 22.211 1.00 4.96 C
|
|---|
| 600 | HETATM 661 C2 RER A 9 4.078 10.655 20.777 1.00 4.02 C
|
|---|
| 601 | HETATM 662 C3 RER A 9 2.866 9.782 20.445 1.00 5.16 C
|
|---|
| 602 | HETATM 663 N3 RER A 9 2.216 10.356 19.185 1.00 4.91 N
|
|---|
| 603 | HETATM 664 C3A RER A 9 3.232 8.374 20.073 1.00 3.64 C
|
|---|
| 604 | HETATM 665 C4 RER A 9 1.810 9.767 21.589 1.00 4.90 C
|
|---|
| 605 | HETATM 666 O4 RER A 9 1.224 11.137 21.530 1.00 5.02 O
|
|---|
| 606 | HETATM 667 C5 RER A 9 2.481 9.533 22.942 1.00 4.79 C
|
|---|
| 607 | HETATM 668 O5 RER A 9 3.529 10.479 23.167 1.00 3.94 O
|
|---|
| 608 | HETATM 669 C5A RER A 9 1.502 9.676 24.125 1.00 4.87 C
|
|---|
| 609 | END
|
|---|
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