Header list of 2mob.pdb file
Complete list - r 16 2 Bytes
HEADER OXIDOREDUCTASE 10-MAR-99 2MOB
TITLE METHANE MONOOXYGENASE COMPONENT B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (METHANE MONOOXYGENASE REGULATORY PROTEIN B);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: METHANE MONOOXYGENASE COMPONENT B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOSINUS TRICHOSPORIUM;
SOURCE 3 ORGANISM_TAXID: 426;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, MONOOXYGENASE, METHANE OXIDATION
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.L.CHANG,B.J.WALLAR,J.D.LIPSCOMB,K.H.MAYO
REVDAT 3 16-MAR-22 2MOB 1 REMARK
REVDAT 2 24-FEB-09 2MOB 1 VERSN
REVDAT 1 11-AUG-99 2MOB 0
JRNL AUTH S.L.CHANG,B.J.WALLAR,J.D.LIPSCOMB,K.H.MAYO
JRNL TITL SOLUTION STRUCTURE OF COMPONENT B FROM METHANE MONOOXYGENASE
JRNL TITL 2 DERIVED THROUGH HETERONUCLEAR NMR AND MOLECULAR MODELING.
JRNL REF BIOCHEMISTRY V. 38 5799 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10231531
JRNL DOI 10.1021/BI982992F
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THESE STRUCTURES WERE CALCULATED BY X-PLOR 3.851 SIMULATED
REMARK 3 ANNEALING PROTOCOL (
REMARK 3 NILGES ET AL., FEBS LETT. 229, 317-324) USING 1182 NOE, 98 PHI
REMARK 3 ANGLE, AND 60
REMARK 3 HYDROGEN BONDING CONSTRAINTS.
REMARK 4
REMARK 4 2MOB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000617.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C,
REMARK 210 15N-LABELED PROTEIN.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 HIS A 5
REMARK 465 ASN A 6
REMARK 465 ALA A 7
REMARK 465 TYR A 8
REMARK 465 ASN A 9
REMARK 465 ALA A 10
REMARK 465 GLY A 11
REMARK 465 ILE A 12
REMARK 465 MET A 13
REMARK 465 GLN A 14
REMARK 465 LYS A 15
REMARK 465 THR A 16
REMARK 465 GLY A 17
REMARK 465 LYS A 18
REMARK 465 ALA A 19
REMARK 465 PHE A 20
REMARK 465 ALA A 21
REMARK 465 ASP A 22
REMARK 465 GLU A 23
REMARK 465 PHE A 24
REMARK 465 PHE A 25
REMARK 465 ALA A 26
REMARK 465 GLU A 27
REMARK 465 GLU A 28
REMARK 465 ASN A 29
REMARK 465 GLN A 30
REMARK 465 VAL A 31
REMARK 465 VAL A 32
REMARK 465 HIS A 33
REMARK 465 GLU A 34
REMARK 465 MET A 129
REMARK 465 GLY A 130
REMARK 465 LEU A 131
REMARK 465 ASP A 132
REMARK 465 ARG A 133
REMARK 465 ALA A 134
REMARK 465 LEU A 135
REMARK 465 THR A 136
REMARK 465 ASP A 137
REMARK 465 ILE A 138
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 O ILE A 51 H ILE A 55 1.42
REMARK 500 O VAL A 56 H GLY A 60 1.44
REMARK 500 O LEU A 118 H THR A 120 1.45
REMARK 500 O ILE A 52 H LEU A 57 1.51
REMARK 500 O LEU A 104 H VAL A 108 1.53
REMARK 500 H LEU A 42 O TRP A 76 1.58
REMARK 500 O ILE A 48 H ILE A 52 1.59
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 1 ASN A 36 -57.08 68.96
REMARK 500 1 ALA A 37 132.96 -29.87
REMARK 500 1 LYS A 44 -93.14 -88.95
REMARK 500 1 SER A 45 178.01 89.36
REMARK 500 1 ASP A 46 -87.41 62.93
REMARK 500 1 ASP A 49 -32.57 -37.83
REMARK 500 1 ALA A 62 -82.63 -87.50
REMARK 500 1 SER A 66 111.86 179.96
REMARK 500 1 ALA A 73 73.66 18.64
REMARK 500 1 LYS A 97 -124.17 -138.23
REMARK 500 1 PHE A 99 -44.01 -23.66
REMARK 500 1 VAL A 108 1.66 -65.86
REMARK 500 1 SER A 109 -33.80 -35.42
REMARK 500 1 SER A 110 39.16 -88.02
REMARK 500 1 VAL A 112 -84.66 16.56
REMARK 500 1 ARG A 114 178.92 43.49
REMARK 500 1 SER A 126 -89.25 -120.45
REMARK 500 2 ALA A 37 146.38 -37.41
REMARK 500 2 LYS A 44 95.90 -64.09
REMARK 500 2 ASP A 46 -58.96 74.82
REMARK 500 2 ILE A 48 -71.16 -63.23
REMARK 500 2 ASP A 49 -34.20 -36.80
REMARK 500 2 ALA A 62 -84.80 -94.47
REMARK 500 2 SER A 66 111.57 179.37
REMARK 500 2 ALA A 73 86.78 -53.81
REMARK 500 2 LYS A 97 -134.41 -133.05
REMARK 500 2 PHE A 99 -42.29 -26.56
REMARK 500 2 SER A 109 -27.96 -35.10
REMARK 500 2 SER A 110 8.34 -66.68
REMARK 500 2 THR A 111 38.55 -86.14
REMARK 500 2 ALA A 115 83.79 -160.67
REMARK 500 2 SER A 126 -76.07 -86.68
REMARK 500 3 ASN A 36 -13.13 77.31
REMARK 500 3 LYS A 44 -81.27 -88.51
REMARK 500 3 SER A 45 92.97 67.99
REMARK 500 3 ASP A 46 -80.44 170.96
REMARK 500 3 LYS A 61 12.57 -67.60
REMARK 500 3 SER A 66 112.09 179.44
REMARK 500 3 ALA A 73 94.40 -25.99
REMARK 500 3 ALA A 88 -29.90 -150.35
REMARK 500 3 ALA A 91 -38.08 -38.61
REMARK 500 3 LYS A 97 -151.69 -175.99
REMARK 500 3 PHE A 99 -44.58 -21.30
REMARK 500 3 SER A 109 -27.22 -35.88
REMARK 500 3 THR A 111 42.89 -89.49
REMARK 500 3 ALA A 115 73.77 -170.36
REMARK 500 3 LEU A 118 39.61 -86.64
REMARK 500 3 GLU A 127 105.49 -37.65
REMARK 500 4 ASN A 36 -92.86 -129.86
REMARK 500 4 ALA A 37 127.28 -27.25
REMARK 500
REMARK 500 THIS ENTRY HAS 263 RAMACHANDRAN OUTLIERS.
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 1 ARG A 114 0.30 SIDE CHAIN
REMARK 500 2 ARG A 114 0.30 SIDE CHAIN
REMARK 500 3 ARG A 114 0.17 SIDE CHAIN
REMARK 500 4 ARG A 114 0.28 SIDE CHAIN
REMARK 500 5 ARG A 114 0.32 SIDE CHAIN
REMARK 500 6 ARG A 114 0.30 SIDE CHAIN
REMARK 500 7 ARG A 114 0.29 SIDE CHAIN
REMARK 500 8 ARG A 114 0.31 SIDE CHAIN
REMARK 500 9 ARG A 114 0.28 SIDE CHAIN
REMARK 500 10 ARG A 114 0.32 SIDE CHAIN
REMARK 500 11 ARG A 114 0.31 SIDE CHAIN
REMARK 500 12 ARG A 114 0.29 SIDE CHAIN
REMARK 500 13 ARG A 114 0.16 SIDE CHAIN
REMARK 500 14 ARG A 114 0.31 SIDE CHAIN
REMARK 500 15 ARG A 114 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2MOB A 1 138 UNP P27356 MMOB_METTR 1 138
SEQRES 1 A 138 MET SER SER ALA HIS ASN ALA TYR ASN ALA GLY ILE MET
SEQRES 2 A 138 GLN LYS THR GLY LYS ALA PHE ALA ASP GLU PHE PHE ALA
SEQRES 3 A 138 GLU GLU ASN GLN VAL VAL HIS GLU SER ASN ALA VAL VAL
SEQRES 4 A 138 LEU VAL LEU MET LYS SER ASP GLU ILE ASP ALA ILE ILE
SEQRES 5 A 138 GLU ASP ILE VAL LEU LYS GLY GLY LYS ALA LYS ASN PRO
SEQRES 6 A 138 SER ILE VAL VAL GLU ASP LYS ALA GLY PHE TRP TRP ILE
SEQRES 7 A 138 LYS ALA ASP GLY ALA ILE GLU ILE ASP ALA ALA GLU ALA
SEQRES 8 A 138 GLY GLU LEU LEU GLY LYS PRO PHE SER VAL TYR ASP LEU
SEQRES 9 A 138 LEU ILE ASN VAL SER SER THR VAL GLY ARG ALA TYR THR
SEQRES 10 A 138 LEU GLY THR LYS PHE THR ILE THR SER GLU LEU MET GLY
SEQRES 11 A 138 LEU ASP ARG ALA LEU THR ASP ILE
HELIX 1 1 GLU A 47 ILE A 55 1 9
HELIX 2 2 GLY A 59 ALA A 62 1 4
HELIX 3 3 ALA A 89 LEU A 94 1 6
HELIX 4 4 PRO A 98 SER A 110 5 13
SHEET 1 A 3 VAL A 38 VAL A 41 0
SHEET 2 A 3 TRP A 76 ALA A 80 -1 N ALA A 80 O VAL A 38
SHEET 3 A 3 VAL A 68 ASP A 71 -1 N GLU A 70 O TRP A 77
SHEET 1 B 3 ALA A 83 ASP A 87 0
SHEET 2 B 3 LYS A 121 THR A 125 -1 N ILE A 124 O ILE A 84
SHEET 3 B 3 ALA A 115 LEU A 118 -1 N LEU A 118 O LYS A 121
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
MODEL 1
Complete list - r 16 2 Bytes