Header list of 1myf.pdb file
Complete list - b 23 2 Bytes
HEADER OXYGEN TRANSPORT 02-DEC-94 1MYF
TITLE SOLUTION STRUCTURE OF CARBONMONOXY MYOGLOBIN DETERMINED FROM NMR
TITLE 2 DISTANCE AND CHEMICAL SHIFT CONSTRAINTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOGLOBIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;
SOURCE 3 ORGANISM_COMMON: SPERM WHALE;
SOURCE 4 ORGANISM_TAXID: 9755
KEYWDS OXYGEN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR K.OSAPAY,Y.THERIAULT,P.E.WRIGHT,D.A.CASE
REVDAT 4 23-FEB-22 1MYF 1 REMARK LINK
REVDAT 3 24-FEB-09 1MYF 1 VERSN
REVDAT 2 01-APR-03 1MYF 1 JRNL
REVDAT 1 27-FEB-95 1MYF 0
JRNL AUTH K.OSAPAY,Y.THERIAULT,P.E.WRIGHT,D.A.CASE
JRNL TITL SOLUTION STRUCTURE OF CARBONMONOXY MYOGLOBIN DETERMINED FROM
JRNL TITL 2 NUCLEAR MAGNETIC RESONANCE DISTANCE AND CHEMICAL SHIFT
JRNL TITL 3 CONSTRAINTS.
JRNL REF J.MOL.BIOL. V. 244 183 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 7966330
JRNL DOI 10.1006/JMBI.1994.1718
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.P.GIPPERT,P.F.YIP,P.E.WRIGHT,D.A.CASE
REMARK 1 TITL COMPUTATIONAL METHODS FOR DETERMINING PROTEIN STRUCTURES
REMARK 1 TITL 2 FROM NMR DATA
REMARK 1 REF BIOCHEM.PHARM. V. 40 15 1990
REMARK 1 REFN ISSN 0006-2952
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO),
REMARK 3 PEARLMAN,CASE,CALDWELL,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MYF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175185.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
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 : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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: 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 1 VAL A 68 CA - CB - CG1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 1 HIS A 82 CB - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 1 TYR A 103 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 TYR A 146 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 VAL A 68 CA - CB - CG1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 2 TYR A 103 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 3 TYR A 146 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 4 VAL A 68 CA - CB - CG1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 5 VAL A 68 CA - CB - CG1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 6 VAL A 68 CA - CB - CG1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 6 TYR A 151 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 7 HIS A 48 CB - CG - CD2 ANGL. DEV. = -13.3 DEGREES
REMARK 500 7 VAL A 68 CA - CB - CG1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 7 PRO A 88 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 8 TYR A 103 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 9 VAL A 68 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 10 VAL A 68 CA - CB - CG1 ANGL. DEV. = 10.6 DEGREES
REMARK 500 11 VAL A 68 CA - CB - CG1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 11 TYR A 103 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 11 TYR A 146 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 12 HIS A 48 CB - CG - CD2 ANGL. DEV. = -13.3 DEGREES
REMARK 500 12 VAL A 68 CA - CB - CG1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 12 PRO A 88 C - N - CA ANGL. DEV. = 9.7 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 1 GLU A 52 62.65 35.06
REMARK 500 1 ALA A 53 103.53 73.04
REMARK 500 1 GLU A 54 42.98 -75.53
REMARK 500 1 LYS A 56 -83.98 -141.48
REMARK 500 1 ALA A 57 55.86 32.08
REMARK 500 1 GLU A 59 -72.19 65.05
REMARK 500 1 LYS A 79 55.27 33.75
REMARK 500 1 HIS A 82 65.38 -13.07
REMARK 500 1 ALA A 84 -23.37 70.03
REMARK 500 1 GLU A 85 -66.09 -146.35
REMARK 500 1 LEU A 86 -50.04 74.21
REMARK 500 1 LYS A 87 -56.92 -26.37
REMARK 500 1 LYS A 98 54.84 97.47
REMARK 500 1 ILE A 99 -100.97 40.93
REMARK 500 1 LYS A 102 -74.81 33.62
REMARK 500 1 TYR A 151 -64.46 -125.58
REMARK 500 2 HIS A 81 61.74 -117.03
REMARK 500 2 ALA A 94 -63.39 -93.12
REMARK 500 2 ASP A 122 -49.25 -165.23
REMARK 500 2 GLN A 152 -50.98 67.15
REMARK 500 3 GLU A 18 37.50 106.45
REMARK 500 3 ALA A 19 24.86 45.04
REMARK 500 3 ASP A 20 54.12 -94.04
REMARK 500 3 THR A 51 -160.76 -161.54
REMARK 500 3 ALA A 53 -45.72 81.14
REMARK 500 3 HIS A 81 56.24 -107.69
REMARK 500 3 GLU A 83 -48.06 174.30
REMARK 500 3 ALA A 94 -79.29 -72.59
REMARK 500 3 LYS A 98 -54.85 -172.89
REMARK 500 3 ILE A 99 -75.72 108.63
REMARK 500 4 SER A 3 -177.01 -170.48
REMARK 500 4 SER A 35 -72.03 -64.29
REMARK 500 4 PRO A 37 -21.02 -35.40
REMARK 500 4 GLU A 52 77.05 -65.89
REMARK 500 4 ALA A 53 -50.19 -163.54
REMARK 500 4 HIS A 81 66.05 -114.18
REMARK 500 4 HIS A 82 -100.28 -112.87
REMARK 500 4 GLU A 83 -40.27 74.12
REMARK 500 4 ALA A 94 -71.39 -76.23
REMARK 500 4 LYS A 98 82.82 75.71
REMARK 500 4 ILE A 99 -84.61 18.79
REMARK 500 4 PRO A 100 102.96 -22.66
REMARK 500 4 ASP A 122 -44.36 -160.70
REMARK 500 5 GLU A 38 -44.48 -143.80
REMARK 500 5 ASP A 44 -67.97 68.01
REMARK 500 5 ARG A 45 34.63 -161.98
REMARK 500 5 LYS A 47 -1.52 35.26
REMARK 500 5 HIS A 48 -2.25 -172.81
REMARK 500 5 LYS A 50 -60.85 -151.68
REMARK 500 5 SER A 58 84.82 -68.85
REMARK 500
REMARK 500 THIS ENTRY HAS 142 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 HIS A 81 0.08 SIDE CHAIN
REMARK 500 1 TYR A 103 0.16 SIDE CHAIN
REMARK 500 1 PHE A 106 0.08 SIDE CHAIN
REMARK 500 1 HIS A 116 0.09 SIDE CHAIN
REMARK 500 2 TYR A 103 0.07 SIDE CHAIN
REMARK 500 2 HIS A 116 0.08 SIDE CHAIN
REMARK 500 3 PHE A 46 0.11 SIDE CHAIN
REMARK 500 3 TYR A 103 0.14 SIDE CHAIN
REMARK 500 3 PHE A 106 0.07 SIDE CHAIN
REMARK 500 3 HIS A 119 0.10 SIDE CHAIN
REMARK 500 3 TYR A 151 0.12 SIDE CHAIN
REMARK 500 4 PHE A 46 0.08 SIDE CHAIN
REMARK 500 4 TYR A 103 0.08 SIDE CHAIN
REMARK 500 4 PHE A 106 0.09 SIDE CHAIN
REMARK 500 4 TYR A 151 0.08 SIDE CHAIN
REMARK 500 5 PHE A 46 0.10 SIDE CHAIN
REMARK 500 5 HIS A 48 0.12 SIDE CHAIN
REMARK 500 5 TYR A 103 0.16 SIDE CHAIN
REMARK 500 6 TYR A 103 0.15 SIDE CHAIN
REMARK 500 6 TYR A 151 0.17 SIDE CHAIN
REMARK 500 7 PHE A 46 0.13 SIDE CHAIN
REMARK 500 7 HIS A 48 0.25 SIDE CHAIN
REMARK 500 7 TYR A 103 0.11 SIDE CHAIN
REMARK 500 7 PHE A 106 0.09 SIDE CHAIN
REMARK 500 8 TYR A 103 0.08 SIDE CHAIN
REMARK 500 8 HIS A 113 0.10 SIDE CHAIN
REMARK 500 8 HIS A 119 0.09 SIDE CHAIN
REMARK 500 9 PHE A 46 0.08 SIDE CHAIN
REMARK 500 9 TYR A 103 0.15 SIDE CHAIN
REMARK 500 10 PHE A 46 0.12 SIDE CHAIN
REMARK 500 10 PHE A 106 0.10 SIDE CHAIN
REMARK 500 10 HIS A 113 0.11 SIDE CHAIN
REMARK 500 11 PHE A 46 0.11 SIDE CHAIN
REMARK 500 11 HIS A 48 0.12 SIDE CHAIN
REMARK 500 11 TYR A 103 0.10 SIDE CHAIN
REMARK 500 11 ARG A 118 0.10 SIDE CHAIN
REMARK 500 11 PHE A 138 0.09 SIDE CHAIN
REMARK 500 12 PHE A 46 0.13 SIDE CHAIN
REMARK 500 12 HIS A 48 0.25 SIDE CHAIN
REMARK 500 12 TYR A 103 0.11 SIDE CHAIN
REMARK 500 12 PHE A 106 0.09 SIDE CHAIN
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 154 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 93 NE2
REMARK 620 2 HEM A 154 NA 91.1
REMARK 620 3 HEM A 154 NB 87.1 88.6
REMARK 620 4 HEM A 154 NC 93.5 175.3 91.1
REMARK 620 5 HEM A 154 ND 91.9 90.5 178.6 89.9
REMARK 620 6 CMO A 155 C 175.5 93.3 93.2 82.0 87.9
REMARK 620 7 CMO A 155 O 173.9 95.0 93.8 80.4 87.3 1.7
REMARK 620 N 1 2 3 4 5 6
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 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 155
DBREF 1MYF A 1 153 UNP P02185 MYG_PHYCA 1 153
SEQRES 1 A 153 VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS VAL
SEQRES 2 A 153 TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN
SEQRES 3 A 153 ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU THR
SEQRES 4 A 153 LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR GLU
SEQRES 5 A 153 ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY
SEQRES 6 A 153 VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS LYS
SEQRES 7 A 153 LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA GLN
SEQRES 8 A 153 SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR LEU
SEQRES 9 A 153 GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS SER
SEQRES 10 A 153 ARG HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA
SEQRES 11 A 153 MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE ALA
SEQRES 12 A 153 ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY
HET HEM A 154 73
HET CMO A 155 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 GLU A 4 SER A 35 1 32
HELIX 2 2 PRO A 37 LYS A 42 1 6
HELIX 3 3 ASP A 44 LYS A 47 1 4
HELIX 4 4 ASP A 60 LYS A 77 1 18
HELIX 5 5 LYS A 87 THR A 95 1 9
HELIX 6 6 ILE A 101 ARG A 118 5 18
HELIX 7 7 ALA A 125 GLU A 148 1 24
LINK NE2 HIS A 93 FE HEM A 154 1555 1555 2.01
LINK FE HEM A 154 C CMO A 155 1555 1555 1.74
LINK FE HEM A 154 O CMO A 155 1555 1555 2.86
SITE 1 AC1 14 THR A 39 PHE A 43 ARG A 45 HIS A 64
SITE 2 AC1 14 THR A 67 VAL A 68 LEU A 72 SER A 92
SITE 3 AC1 14 HIS A 93 HIS A 97 TYR A 103 LEU A 104
SITE 4 AC1 14 ILE A 107 CMO A 155
SITE 1 AC2 4 PHE A 43 HIS A 64 VAL A 68 HEM A 154
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 - b 23 2 Bytes