Header list of 1vre.pdb file
Complete list - v 13 2 Bytes
HEADER HEME PROTEIN 25-MAR-99 1VRE
TITLE SOLUTION STRUCTURE OF COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC
TITLE 2 HEMOGLOBIN-CO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GLOBIN, MONOMERIC COMPONENT M-IV);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GHM4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCERA DIBRANCHIATA;
SOURCE 3 ORGANISM_TAXID: 6350;
SOURCE 4 TISSUE: BLOOD;
SOURCE 5 CELL: ERYTHROCYTE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET9D;
SOURCE 10 OTHER_DETAILS: RECOMBINANT PROTEIN WAS PRODUCED IN E. COLI
KEYWDS HEME PROTEIN, GLOBIN, OXYGEN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR B.F.VOLKMAN,S.L.ALAM,J.D.SATTERLEE,J.L.MARKLEY
REVDAT 5 13-NOV-19 1VRE 1 REMARK ATOM
REVDAT 4 24-FEB-09 1VRE 1 VERSN
REVDAT 3 20-MAY-99 1VRE 1 LINK
REVDAT 2 30-APR-99 1VRE 3 ATOM
REVDAT 1 02-APR-99 1VRE 0
JRNL AUTH B.F.VOLKMAN,S.L.ALAM,J.D.SATTERLEE,J.L.MARKLEY
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF COMPONENT IV
JRNL TITL 2 GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO.
JRNL REF BIOCHEMISTRY V. 37 10906 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9692983
JRNL DOI 10.1021/BI980810B
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.L.ALAM,B.F.VOLKMAN,J.L.MARKLEY,J.D.SATTERLEE
REMARK 1 TITL DETAILED NMR ANALYSIS OF THE HEME-PROTEIN INTERACTIONS IN
REMARK 1 TITL 2 COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO
REMARK 1 REF J.BIOMOL.NMR V. 11 19 1998
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008202621725
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED ITERATIVELY WITH X-PLOR AND
REMARK 3 PERL SCRIPTS WRITTEN IN-HOUSE AS DESCRIBED IN JRNL CITATION ABOVE
REMARK 4
REMARK 4 1VRE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000719.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOEY & QUANTITATIVE J
REMARK 210 -CORRELATION
REMARK 210 SPECTROMETER FIELD STRENGTH : 499.84 MHZ; 500.13 MHZ; 600.13
REMARK 210 MHZ; 750.13 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.843
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY/
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS GREATER THAN
REMARK 210 0.2 ANGSTROM, NO DIHEDRAL
REMARK 210 RESTRAINT VIOLATIONS GREATER
REMARK 210 THAN 2 DEGREES.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: 3D 15N NOESY-HSQC; 3D 13C NOESY-HSQC; 4D 13C/15N NOESY
REMARK 210 -HSQC; 3D HNHB; 3D HNCOHB; 2D JCC; 2D JNC; 3D HNHA; 2D LRCC
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
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 HIS A 72 61.37 -161.73
REMARK 500 1 GLU A 76 43.32 -94.96
REMARK 500 1 LYS A 78 -57.93 -126.04
REMARK 500 1 ILE A 118 43.26 -91.69
REMARK 500 1 LEU A 145 170.28 -58.75
REMARK 500 1 GLN A 146 46.83 36.33
REMARK 500 2 SER A 3 -159.81 -134.27
REMARK 500 2 ASN A 22 19.25 57.15
REMARK 500 2 ALA A 50 39.47 -98.93
REMARK 500 2 SER A 51 22.94 -140.53
REMARK 500 2 HIS A 72 -77.53 -124.01
REMARK 500 2 LEU A 73 -79.52 59.78
REMARK 500 2 TYR A 93 -100.38 -82.46
REMARK 500 2 LYS A 96 -48.99 64.41
REMARK 500 2 HIS A 97 -97.21 -50.00
REMARK 500 2 ILE A 98 154.09 65.40
REMARK 500 2 ILE A 118 53.10 -104.34
REMARK 500 2 MET A 122 86.35 -63.89
REMARK 500 2 SER A 143 -63.41 -95.25
REMARK 500 2 LEU A 145 -168.63 -56.40
REMARK 500 2 GLN A 146 92.75 55.63
REMARK 500 3 SER A 3 -166.52 -118.08
REMARK 500 3 ALA A 50 34.11 -94.73
REMARK 500 3 LEU A 58 -64.00 -91.43
REMARK 500 3 HIS A 72 -83.92 -122.85
REMARK 500 3 LEU A 73 -77.51 60.85
REMARK 500 3 ARG A 117 -68.90 -95.42
REMARK 500 3 MET A 122 90.53 -66.23
REMARK 500 4 CYS A 30 -63.14 -90.15
REMARK 500 4 SER A 51 43.41 -94.30
REMARK 500 4 HIS A 72 44.12 -157.90
REMARK 500 4 GLU A 76 40.48 -102.09
REMARK 500 4 LYS A 78 -35.11 -176.89
REMARK 500 4 TYR A 93 -103.17 -82.46
REMARK 500 4 LYS A 96 -57.63 65.66
REMARK 500 4 HIS A 97 79.53 -62.93
REMARK 500 4 ARG A 117 -86.86 -90.80
REMARK 500 4 MET A 122 80.60 -65.52
REMARK 500 4 GLN A 146 44.81 162.45
REMARK 500 5 LEU A 2 165.56 57.06
REMARK 500 5 SER A 3 -168.66 -128.04
REMARK 500 5 SER A 71 39.40 -88.67
REMARK 500 5 HIS A 72 -62.10 -151.13
REMARK 500 5 LEU A 73 -88.89 42.37
REMARK 500 5 TYR A 93 -167.68 -56.13
REMARK 500 5 LYS A 96 13.89 59.96
REMARK 500 5 ILE A 142 38.07 -91.01
REMARK 500 5 GLN A 146 68.73 -113.19
REMARK 500 6 LEU A 2 163.82 57.30
REMARK 500 6 SER A 3 -158.33 -140.14
REMARK 500
REMARK 500 THIS ENTRY HAS 274 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 7 0.32 SIDE CHAIN
REMARK 500 1 ARG A 89 0.21 SIDE CHAIN
REMARK 500 1 ARG A 117 0.31 SIDE CHAIN
REMARK 500 2 ARG A 7 0.25 SIDE CHAIN
REMARK 500 2 ARG A 89 0.29 SIDE CHAIN
REMARK 500 2 ARG A 117 0.29 SIDE CHAIN
REMARK 500 3 ARG A 7 0.21 SIDE CHAIN
REMARK 500 3 ARG A 89 0.29 SIDE CHAIN
REMARK 500 3 ARG A 117 0.32 SIDE CHAIN
REMARK 500 4 ARG A 7 0.31 SIDE CHAIN
REMARK 500 4 ARG A 89 0.29 SIDE CHAIN
REMARK 500 4 ARG A 117 0.31 SIDE CHAIN
REMARK 500 5 ARG A 7 0.14 SIDE CHAIN
REMARK 500 5 ARG A 89 0.31 SIDE CHAIN
REMARK 500 5 ARG A 117 0.30 SIDE CHAIN
REMARK 500 6 ARG A 7 0.32 SIDE CHAIN
REMARK 500 6 ARG A 89 0.21 SIDE CHAIN
REMARK 500 6 ARG A 117 0.15 SIDE CHAIN
REMARK 500 7 ARG A 7 0.15 SIDE CHAIN
REMARK 500 7 ARG A 89 0.29 SIDE CHAIN
REMARK 500 7 ARG A 117 0.12 SIDE CHAIN
REMARK 500 8 ARG A 7 0.27 SIDE CHAIN
REMARK 500 8 ARG A 89 0.23 SIDE CHAIN
REMARK 500 8 ARG A 117 0.28 SIDE CHAIN
REMARK 500 9 ARG A 7 0.25 SIDE CHAIN
REMARK 500 9 ARG A 89 0.32 SIDE CHAIN
REMARK 500 9 ARG A 117 0.26 SIDE CHAIN
REMARK 500 10 ARG A 7 0.26 SIDE CHAIN
REMARK 500 10 ARG A 89 0.30 SIDE CHAIN
REMARK 500 10 ARG A 117 0.30 SIDE CHAIN
REMARK 500 11 ARG A 7 0.30 SIDE CHAIN
REMARK 500 11 ARG A 89 0.31 SIDE CHAIN
REMARK 500 11 ARG A 117 0.26 SIDE CHAIN
REMARK 500 12 ARG A 7 0.31 SIDE CHAIN
REMARK 500 12 ARG A 89 0.31 SIDE CHAIN
REMARK 500 12 ARG A 117 0.28 SIDE CHAIN
REMARK 500 13 ARG A 7 0.30 SIDE CHAIN
REMARK 500 13 ARG A 89 0.30 SIDE CHAIN
REMARK 500 13 ARG A 117 0.28 SIDE CHAIN
REMARK 500 14 ARG A 7 0.29 SIDE CHAIN
REMARK 500 14 ARG A 89 0.31 SIDE CHAIN
REMARK 500 14 ARG A 117 0.31 SIDE CHAIN
REMARK 500 15 ARG A 7 0.13 SIDE CHAIN
REMARK 500 15 ARG A 89 0.30 SIDE CHAIN
REMARK 500 15 ARG A 117 0.23 SIDE CHAIN
REMARK 500 16 ARG A 7 0.30 SIDE CHAIN
REMARK 500 16 ARG A 89 0.26 SIDE CHAIN
REMARK 500 16 ARG A 117 0.29 SIDE CHAIN
REMARK 500 17 ARG A 7 0.31 SIDE CHAIN
REMARK 500 17 ARG A 89 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 87 PLANE DEVIATIONS.
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 HEM A 148 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 90 NE2
REMARK 620 2 HEM A 148 NA 89.9
REMARK 620 3 HEM A 148 NB 90.1 90.0
REMARK 620 4 HEM A 148 NC 90.5 179.6 90.0
REMARK 620 5 HEM A 148 ND 90.2 90.1 179.7 90.0
REMARK 620 6 CMO A 149 C 179.8 89.9 89.8 89.7 89.9
REMARK 620 7 CMO A 149 O 179.8 89.9 89.9 89.7 89.8 0.0
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: LIG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: HIS A 90 NE2-HEME FE COORDINATE-COVALENT BOND
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 149
DBREF 1VRE A 1 147 UNP P15447 GLB4_GLYDI 1 147
SEQRES 1 A 147 GLY LEU SER ALA ALA GLN ARG GLN VAL VAL ALA SER THR
SEQRES 2 A 147 TRP LYS ASP ILE ALA GLY SER ASP ASN GLY ALA GLY VAL
SEQRES 3 A 147 GLY LYS GLU CYS PHE THR LYS PHE LEU SER ALA HIS HIS
SEQRES 4 A 147 ASP MET ALA ALA VAL PHE GLY PHE SER GLY ALA SER ASP
SEQRES 5 A 147 PRO GLY VAL ALA ASP LEU GLY ALA LYS VAL LEU ALA GLN
SEQRES 6 A 147 ILE GLY VAL ALA VAL SER HIS LEU GLY ASP GLU GLY LYS
SEQRES 7 A 147 MET VAL ALA GLU MET LYS ALA VAL GLY VAL ARG HIS LYS
SEQRES 8 A 147 GLY TYR GLY ASN LYS HIS ILE LYS ALA GLU TYR PHE GLU
SEQRES 9 A 147 PRO LEU GLY ALA SER LEU LEU SER ALA MET GLU HIS ARG
SEQRES 10 A 147 ILE GLY GLY LYS MET ASN ALA ALA ALA LYS ASP ALA TRP
SEQRES 11 A 147 ALA ALA ALA TYR ALA ASP ILE SER GLY ALA LEU ILE SER
SEQRES 12 A 147 GLY LEU GLN SER
HET HEM A 148 73
HET CMO A 149 2
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CMO CARBON MONOXIDE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 CMO C O
HELIX 1 1 ALA A 4 ILE A 17 1 14
HELIX 2 2 ALA A 24 ALA A 37 1 14
HELIX 3 3 ALA A 42 PHE A 45 1 4
HELIX 4 4 PRO A 53 VAL A 70 1 18
HELIX 5 5 MET A 79 GLY A 92 1 14
HELIX 6 6 GLU A 101 ARG A 117 1 17
HELIX 7 7 ALA A 124 GLY A 144 1 21
LINK NE2 HIS A 90 FE HEM A 148 1555 1555 2.20
LINK FE HEM A 148 C CMO A 149 1555 1555 1.90
LINK FE HEM A 148 O CMO A 149 1555 1555 3.03
SITE 1 LIG 1 HIS A 90
SITE 1 AC1 12 MET A 41 VAL A 44 PHE A 45 LEU A 58
SITE 2 AC1 12 VAL A 62 HIS A 90 TYR A 93 ASN A 95
SITE 3 AC1 12 TYR A 102 PHE A 103 LEU A 141 CMO A 149
SITE 1 AC2 5 PHE A 31 PHE A 45 LEU A 58 VAL A 62
SITE 2 AC2 5 HEM A 148
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 - v 13 2 Bytes