Header list of 1mwb.pdb file
Complete list - r 25 2 Bytes
HEADER OXYGEN STORAGE/TRANSPORT 27-SEP-02 1MWB
TITLE SOLUTION STRUCTURE OF THE RECOMBINANT HEMOGLOBIN FROM THE
TITLE 2 CYANOBACTERIUM SYNECHOCYSTIS SP. PCC 6803 IN ITS HEMICHROME STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYANOGLOBIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HEMOGLOBIN, HB;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803;
SOURCE 5 GENE: SLR2097 (GLBN);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET3C
KEYWDS GLOBIN, CYANOGLOBIN, OXYGEN STORAGE-TRANSPORT COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.J.FALZONE,B.C.VU,N.L.SCOTT,J.T.LECOMTE
REVDAT 3 13-JUL-11 1MWB 1 VERSN
REVDAT 2 24-FEB-09 1MWB 1 VERSN
REVDAT 1 04-DEC-02 1MWB 0
JRNL AUTH C.J.FALZONE,B.C.VU,N.L.SCOTT,J.T.LECOMTE
JRNL TITL THE SOLUTION STRUCTURE OF THE RECOMBINANT HEMOGLOBIN FROM
JRNL TITL 2 THE CYANOBACTERIUM SYNECHOCYSTIS SP. PCC 6803 IN ITS
JRNL TITL 3 HEMICHROME STATE
JRNL REF J.MOL.BIOL. V. 324 1015 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12470956
JRNL DOI 10.1016/S0022-2836(02)01093-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.FALZONE,J.T.LECOMTE
REMARK 1 TITL ASSIGNMENT OF THE 1H, 13C, AND 15N SIGNALS OF SYNECHOCYSTIS
REMARK 1 TITL 2 SP. PCC 6803 METHEMOGLOBIN
REMARK 1 REF J.BIOMOL.NMR V. 23 71 2002
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1015337100759
REMARK 1 REFERENCE 2
REMARK 1 AUTH N.L.SCOTT,J.T.LECOMTE
REMARK 1 TITL CLONING, EXPRESSION, PURIFICATION, AND PRELIMINARY
REMARK 1 TITL 2 CHARACTERIZATION OF A PUTATIVE HEMOGLOBIN FROM THE
REMARK 1 TITL 3 CYANOBACTERIUM SYNECHOCYSTIS SP. PCC 6803
REMARK 1 REF PROTEIN SCI. V. 9 587 2000
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR-NIH 1.2.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-02.
REMARK 100 THE RCSB ID CODE IS RCSB017245.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 - 2 MM PROTEIN, 20 MM K OR
REMARK 210 NA PHOSPHATE; 0.6 - 2 MM PROTEIN,
REMARK 210 20 MM K OR NA PHOSPHATE; 1 MM U-
REMARK 210 15N PROTEIN, 20 MM K OR NA
REMARK 210 PHOSPHATE; 1 MM U-15N, 13C
REMARK 210 PROTEIN, 20 MM K OR NA PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C-SEPARATED_
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY; J-
REMARK 210 MODULATED 1H-15N HSQC; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851, FELIX 2000,
REMARK 210 XWINNMR 2.5, NMRPIPE 2.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSIONAL ANGLE DATABASE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST ENERGY
REMARK 210 AND LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS IS A LOW-SPIN FE(+3) COMPLEX. STANDARD METHODS AS
REMARK 210 APPLIED TO DIMAGNETIC PROTEINS WERE USED TO DETERMINE THE
REMARK 210 STRUCTURE.
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 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 HZ1 LYS A 20 HH21 ARG A 24 1.27
REMARK 500 HZ1 LYS A 20 HE ARG A 24 1.28
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 2 ALA A 114 109.38 -49.74
REMARK 500 3 THR A 58 74.41 -60.56
REMARK 500 3 ALA A 114 108.50 -49.24
REMARK 500 3 VAL A 121 -70.62 -82.99
REMARK 500 4 THR A 11 -139.61 -174.37
REMARK 500 4 ARG A 64 -7.02 -54.49
REMARK 500 5 THR A 11 -126.17 49.69
REMARK 500 5 ASP A 59 111.00 56.29
REMARK 500 6 ALA A 114 108.94 -48.74
REMARK 500 8 PRO A 115 -2.66 -58.43
REMARK 500 8 VAL A 121 -70.94 -78.54
REMARK 500 9 ASP A 59 -44.14 -165.72
REMARK 500 9 LYS A 60 12.89 -156.92
REMARK 500 10 ASP A 59 -174.03 -59.71
REMARK 500 10 GLU A 75 -60.08 -97.73
REMARK 500 10 ALA A 114 109.11 -49.44
REMARK 500 11 THR A 11 -89.29 44.83
REMARK 500 12 THR A 11 -101.69 39.75
REMARK 500 12 ARG A 64 -15.87 -47.25
REMARK 500 12 ALA A 114 108.18 -49.32
REMARK 500 13 ALA A 114 109.84 -48.99
REMARK 500 14 THR A 11 -157.08 -174.31
REMARK 500 15 THR A 12 -13.28 -49.86
REMARK 500 15 ASP A 59 127.36 59.43
REMARK 500 15 ASN A 123 65.44 -63.70
REMARK 500 16 THR A 11 -165.86 48.00
REMARK 500 16 ALA A 114 108.99 -48.78
REMARK 500 16 LEU A 122 47.09 -93.69
REMARK 500 17 LEU A 4 -17.79 -47.86
REMARK 500 17 ALA A 114 108.84 -49.57
REMARK 500 17 ASN A 123 -68.56 59.29
REMARK 500 18 THR A 12 -15.54 -44.51
REMARK 500 18 THR A 58 74.79 -61.07
REMARK 500 19 ALA A 114 109.10 -48.83
REMARK 500 20 LYS A 60 70.54 58.00
REMARK 500 20 ALA A 114 109.63 -49.20
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 1 HEM A 125 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 70 NE2
REMARK 620 2 HEM A 125 NA 90.3
REMARK 620 3 HEM A 125 NB 90.2 90.0
REMARK 620 4 HEM A 125 NC 90.1 179.4 89.5
REMARK 620 5 HEM A 125 ND 90.4 90.5 179.2 89.9
REMARK 620 6 HIS A 46 NE2 179.7 89.4 89.8 90.2 89.6
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 HEM A 125
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS INFORMED THAT MET 1 IN SWISSPROT P73925
REMARK 999 WAS CLEAVED POST-TRANSLATIONALLY
DBREF 1MWB A 2 124 UNP P73925 GLBN_SYNY3 2 124
SEQRES 1 A 123 SER THR LEU TYR GLU LYS LEU GLY GLY THR THR ALA VAL
SEQRES 2 A 123 ASP LEU ALA VAL ASP LYS PHE TYR GLU ARG VAL LEU GLN
SEQRES 3 A 123 ASP ASP ARG ILE LYS HIS PHE PHE ALA ASP VAL ASP MET
SEQRES 4 A 123 ALA LYS GLN ARG ALA HIS GLN LYS ALA PHE LEU THR TYR
SEQRES 5 A 123 ALA PHE GLY GLY THR ASP LYS TYR ASP GLY ARG TYR MET
SEQRES 6 A 123 ARG GLU ALA HIS LYS GLU LEU VAL GLU ASN HIS GLY LEU
SEQRES 7 A 123 ASN GLY GLU HIS PHE ASP ALA VAL ALA GLU ASP LEU LEU
SEQRES 8 A 123 ALA THR LEU LYS GLU MET GLY VAL PRO GLU ASP LEU ILE
SEQRES 9 A 123 ALA GLU VAL ALA ALA VAL ALA GLY ALA PRO ALA HIS LYS
SEQRES 10 A 123 ARG ASP VAL LEU ASN GLN
HET HEM A 125 73
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 SER A 2 LYS A 7 5 6
HELIX 2 2 GLY A 10 ASP A 28 1 19
HELIX 3 3 ASP A 28 ALA A 36 1 9
HELIX 4 4 ASP A 39 GLY A 56 1 18
HELIX 5 5 GLY A 63 HIS A 77 1 15
HELIX 6 6 ASN A 80 GLY A 99 1 20
HELIX 7 7 PRO A 101 ALA A 114 1 14
HELIX 8 8 ALA A 114 ASN A 123 1 10
LINK FE HEM A 125 NE2 HIS A 70 1555 1555 2.20
LINK FE HEM A 125 NE2 HIS A 46 1555 1555 2.20
SITE 1 AC1 4 HIS A 46 HIS A 70 LEU A 73 VAL 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 25 2 Bytes