Header list of 1mh6.pdb file
Complete list - 23 20 Bytes
HEADER PROTEIN BINDING 19-AUG-02 1MH6
TITLE SOLUTION STRUCTURE OF THE TRANSPOSON TN5-ENCODING BLEOMYCIN-BINDING
TITLE 2 PROTEIN, BLMT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BLEOMYCIN RESISTANCE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BLMT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKKTRP
KEYWDS ANTIBIOTIC RESISTANCE, TRANSPOSABLE ELEMENT, PROTEIN BINDING
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR T.KUMAGAI,K.OHTANI,Y.TSUBOI,T.KOIKE,M.SUGIYAMA
REVDAT 3 23-FEB-22 1MH6 1 REMARK
REVDAT 2 24-FEB-09 1MH6 1 VERSN
REVDAT 1 19-FEB-03 1MH6 0
JRNL AUTH T.KUMAGAI,K.OHTANI,Y.TSUBOI,T.KOIKE,M.SUGIYAMA
JRNL TITL SOLUTION STRUCTURE OF THE TRANSPOSON TN5-ENCODING
JRNL TITL 2 BLEOMYCIN-BINDING PROTEIN COMPLEXED WITH AN ACTIVATED
JRNL TITL 3 BLEOMYCIN ANALOGUE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 2000
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MH6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016908.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 0.20
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; HMBC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : ECP
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER 2000
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLU A 298 CB CG CD OE1 OE2
REMARK 470 GLU B 98 CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H ALA A 205 O ASP B 42 1.57
REMARK 500 OD2 ASP A 213 HG SER A 216 1.57
REMARK 500 OD2 ASP B 13 HG SER B 16 1.57
REMARK 500 HH TYR A 273 OE2 GLU A 283 1.58
REMARK 500 HH TYR B 73 OE2 GLU B 83 1.58
REMARK 500 HH TYR A 221 OD2 ASP A 308 1.59
REMARK 500 HH TYR B 21 OD2 ASP B 108 1.59
REMARK 500 C ASP A 242 O ASP B 3 2.09
REMARK 500 O ASP A 203 CA ASP B 42 2.18
REMARK 500 O ASP A 203 N ASP B 42 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 212 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 PHE A 214 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 223 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 240 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 HIS A 250 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 274 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 HIS A 292 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 315 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 PHE B 14 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 23 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 HIS B 50 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG B 65 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 65 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 74 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 90 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 HIS B 92 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG B 115 NE - CZ - NH1 ANGL. DEV. = 3.9 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 ASP A 203 92.42 -60.62
REMARK 500 ASP A 232 -138.95 -112.14
REMARK 500 ALA A 257 39.55 -83.18
REMARK 500 PRO A 294 84.55 -64.35
REMARK 500 TRP A 299 -44.47 -154.90
REMARK 500 ILE A 325 -63.84 -98.72
REMARK 500 ASP B 3 92.42 -60.57
REMARK 500 ASP B 32 -138.92 -112.05
REMARK 500 ALA B 57 39.60 -83.19
REMARK 500 PRO B 94 84.54 -64.33
REMARK 500 TRP B 99 -44.51 -154.92
REMARK 500 ILE B 125 -63.81 -98.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 267 ASP A 268 147.28
REMARK 500 ASP B 67 ASP B 68 147.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 223 0.09 SIDE CHAIN
REMARK 500 ARG B 23 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MH6 A 202 326 UNP P13081 BLE_KLEPN 2 126
DBREF 1MH6 B 2 126 UNP P13081 BLE_KLEPN 2 126
SEQRES 1 A 125 THR ASP GLN ALA THR PRO ASN LEU PRO SER ARG ASP PHE
SEQRES 2 A 125 ASP SER THR ALA ALA PHE TYR GLU ARG LEU GLY PHE GLY
SEQRES 3 A 125 ILE VAL PHE ARG ASP ALA GLY TRP MET ILE LEU GLN ARG
SEQRES 4 A 125 GLY ASP LEU MET LEU GLU PHE PHE ALA HIS PRO GLY LEU
SEQRES 5 A 125 ASP PRO LEU ALA SER TRP PHE SER CYS CYS LEU ARG LEU
SEQRES 6 A 125 ASP ASP LEU ALA GLU PHE TYR ARG GLN CYS LYS SER VAL
SEQRES 7 A 125 GLY ILE GLN GLU THR SER SER GLY TYR PRO ARG ILE HIS
SEQRES 8 A 125 ALA PRO GLU LEU GLN GLU TRP GLY GLY THR MET ALA ALA
SEQRES 9 A 125 LEU VAL ASP PRO ASP GLY THR LEU LEU ARG LEU ILE GLN
SEQRES 10 A 125 ASN GLU LEU LEU ALA GLY ILE SER
SEQRES 1 B 125 THR ASP GLN ALA THR PRO ASN LEU PRO SER ARG ASP PHE
SEQRES 2 B 125 ASP SER THR ALA ALA PHE TYR GLU ARG LEU GLY PHE GLY
SEQRES 3 B 125 ILE VAL PHE ARG ASP ALA GLY TRP MET ILE LEU GLN ARG
SEQRES 4 B 125 GLY ASP LEU MET LEU GLU PHE PHE ALA HIS PRO GLY LEU
SEQRES 5 B 125 ASP PRO LEU ALA SER TRP PHE SER CYS CYS LEU ARG LEU
SEQRES 6 B 125 ASP ASP LEU ALA GLU PHE TYR ARG GLN CYS LYS SER VAL
SEQRES 7 B 125 GLY ILE GLN GLU THR SER SER GLY TYR PRO ARG ILE HIS
SEQRES 8 B 125 ALA PRO GLU LEU GLN GLU TRP GLY GLY THR MET ALA ALA
SEQRES 9 B 125 LEU VAL ASP PRO ASP GLY THR LEU LEU ARG LEU ILE GLN
SEQRES 10 B 125 ASN GLU LEU LEU ALA GLY ILE SER
HELIX 1 1 ASP A 215 GLU A 222 1 8
HELIX 2 2 ARG A 223 GLY A 225 5 3
HELIX 3 3 ASP A 268 GLY A 280 1 13
HELIX 4 4 GLU A 320 ILE A 325 1 6
HELIX 5 5 ASP B 15 GLU B 22 1 8
HELIX 6 6 ARG B 23 GLY B 25 5 3
HELIX 7 7 ASP B 68 GLY B 80 1 13
HELIX 8 8 GLU B 120 ILE B 125 1 6
SHEET 1 A 5 GLN A 204 PRO A 207 0
SHEET 2 A 5 SER B 61 LEU B 66 -1 O CYS B 63 N THR A 206
SHEET 3 A 5 LEU B 113 GLN B 118 1 O ILE B 117 N LEU B 66
SHEET 4 A 5 THR B 102 VAL B 107 -1 N LEU B 106 O LEU B 114
SHEET 5 A 5 ARG B 90 LEU B 96 -1 N ARG B 90 O VAL B 107
SHEET 1 B 4 PRO A 210 SER A 211 0
SHEET 2 B 4 LEU A 243 ALA A 249 1 O PHE A 248 N SER A 211
SHEET 3 B 4 TRP A 235 ARG A 240 -1 N LEU A 238 O LEU A 245
SHEET 4 B 4 GLY A 227 ARG A 231 -1 N GLY A 227 O GLN A 239
SHEET 1 C 5 ARG A 290 LEU A 296 0
SHEET 2 C 5 THR A 302 VAL A 307 -1 O VAL A 307 N ARG A 290
SHEET 3 C 5 LEU A 313 GLN A 318 -1 O LEU A 314 N LEU A 306
SHEET 4 C 5 SER A 261 LEU A 266 1 N LEU A 266 O ILE A 317
SHEET 5 C 5 GLN B 4 PRO B 7 -1 O THR B 6 N CYS A 263
SHEET 1 D 4 PRO B 10 SER B 11 0
SHEET 2 D 4 LEU B 43 ALA B 49 1 O PHE B 48 N SER B 11
SHEET 3 D 4 TRP B 35 ARG B 40 -1 N LEU B 38 O LEU B 45
SHEET 4 D 4 GLY B 27 ARG B 31 -1 N GLY B 27 O GLN B 39
CISPEP 1 TYR A 288 PRO A 289 0 -2.93
CISPEP 2 TYR B 88 PRO B 89 0 -2.95
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 23 20 Bytes