Header list of 1mny.pdb file
Complete list - 23 20 Bytes
HEADER ELECTRON TRANSPORT 06-SEP-02 1MNY
TITLE DIMETHYL PROPIONATE ESTER HEME-CONTAINING CYTOCHROME B5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN, RESIDUES 5-98;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NM-522;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC13
KEYWDS HEME, IRON, MICROSOMAL MEMBRANE, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.BANCI,I.BERTINI,B.R.BRANCHINI,P.HAJIEVA,G.A.SPYROULIAS,P.TURANO
REVDAT 3 23-FEB-22 1MNY 1 REMARK LINK
REVDAT 2 24-FEB-09 1MNY 1 VERSN
REVDAT 1 13-NOV-02 1MNY 0
JRNL AUTH L.BANCI,I.BERTINI,B.R.BRANCHINI,P.HAJIEVA,G.A.SPYROULIAS,
JRNL AUTH 2 P.TURANO
JRNL TITL DIMETHYL PROPIONATE ESTER HEME-CONTAINING CYTOCHROME B5:
JRNL TITL 2 STRUCTURE AND STABILITY.
JRNL REF J.BIOL.INORG.CHEM. V. 6 490 2001
JRNL REFN ISSN 0949-8257
JRNL PMID 11472013
JRNL DOI 10.1007/S007750100217
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, AMBER 5.0
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MNY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017042.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100 MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D NOESY-15N HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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: 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 C ASP A 1 H LYS A 2 1.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 1 C LYS A 2 N -0.213
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 ASP A 1 CA - C - N ANGL. DEV. = 15.6 DEGREES
REMARK 500 ASP A 1 O - C - N ANGL. DEV. = -15.1 DEGREES
REMARK 500 LYS A 2 C - N - CA ANGL. DEV. = 31.1 DEGREES
REMARK 500 ASP A 3 OD1 - CG - OD2 ANGL. DEV. = -38.8 DEGREES
REMARK 500 ASP A 3 CB - CG - OD1 ANGL. DEV. = 45.5 DEGREES
REMARK 500 ASP A 3 CB - CG - OD2 ANGL. DEV. = -39.0 DEGREES
REMARK 500 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 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 LYS A 2 -60.76 -134.20
REMARK 500 LYS A 5 68.08 -101.55
REMARK 500 TYR A 6 107.66 -59.75
REMARK 500 LYS A 16 16.42 -155.87
REMARK 500 SER A 18 -52.20 -155.61
REMARK 500 LYS A 19 -64.24 -143.80
REMARK 500 HIS A 26 76.34 68.07
REMARK 500 LYS A 34 52.55 -90.33
REMARK 500 PHE A 35 26.46 -157.82
REMARK 500 LEU A 36 -83.22 -71.98
REMARK 500 GLU A 43 -65.40 -149.66
REMARK 500 ASP A 53 82.77 -66.82
REMARK 500 PHE A 58 -52.12 -142.10
REMARK 500 SER A 64 -168.49 -172.21
REMARK 500 ASP A 66 -45.95 -133.89
REMARK 500 ALA A 88 -61.00 160.59
REMARK 500 PRO A 90 97.46 -67.82
REMARK 500 SER A 91 86.58 -45.28
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 LYS A 2 ASP A 3 -146.07
REMARK 500 ASP A 3 VAL A 4 147.93
REMARK 500 LYS A 89 PRO A 90 135.72
REMARK 500 PRO A 90 SER A 91 48.80
REMARK 500 GLU A 92 THR A 93 -130.78
REMARK 500 THR A 93 LEU A 94 30.80
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 HDM A 95 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HDM A 95 NA 91.0
REMARK 620 3 HDM A 95 NB 100.0 89.0
REMARK 620 4 HDM A 95 NC 90.3 178.6 91.5
REMARK 620 5 HDM A 95 ND 81.8 89.8 177.8 89.7
REMARK 620 6 HIS A 63 NE2 171.1 83.2 86.7 95.4 91.3
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 HDM A 95
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQA RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF REDUCED MICROSOMAL RAT CYTOCHROME B5
REMARK 900 RELATED ID: 1AW3 RELATED DB: PDB
REMARK 900 THE SOLUTION NMR STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5
REMARK 900 RELATED ID: 1BLV RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5 IN THE
REMARK 900 PRESENCE OF 2 M GUANIDINIUM CHLORIDE
DBREF 1MNY A 1 94 UNP P00173 CYB5_RAT 5 98
SEQRES 1 A 94 ASP LYS ASP VAL LYS TYR TYR THR LEU GLU GLU ILE GLN
SEQRES 2 A 94 LYS HIS LYS ASP SER LYS SER THR TRP VAL ILE LEU HIS
SEQRES 3 A 94 HIS LYS VAL TYR ASP LEU THR LYS PHE LEU GLU GLU HIS
SEQRES 4 A 94 PRO GLY GLY GLU GLU VAL LEU ARG GLU GLN ALA GLY GLY
SEQRES 5 A 94 ASP ALA THR GLU ASN PHE GLU ASP VAL GLY HIS SER THR
SEQRES 6 A 94 ASP ALA ARG GLU LEU SER LYS THR TYR ILE ILE GLY GLU
SEQRES 7 A 94 LEU HIS PRO ASP ASP ARG SER LYS ILE ALA LYS PRO SER
SEQRES 8 A 94 GLU THR LEU
HET HDM A 95 81
HETNAM HDM DIMETHYL PROPIONATE ESTER HEME
FORMUL 2 HDM C36 H36 FE N4 O4
HELIX 1 1 THR A 8 GLN A 13 1 6
HELIX 2 2 THR A 33 LEU A 36 5 4
HELIX 3 3 GLU A 43 GLU A 48 1 6
HELIX 4 4 THR A 55 ASP A 60 1 6
HELIX 5 5 ASP A 66 SER A 71 1 6
HELIX 6 6 HIS A 80 ILE A 87 1 8
SHEET 1 A 4 TYR A 6 TYR A 7 0
SHEET 2 A 4 ILE A 75 LEU A 79 1 O GLU A 78 N TYR A 7
SHEET 3 A 4 VAL A 29 ASP A 31 -1 N VAL A 29 O ILE A 76
SHEET 4 A 4 TRP A 22 ILE A 24 -1 N VAL A 23 O TYR A 30
LINK NE2 HIS A 39 FE HDM A 95 1555 1555 2.26
LINK NE2 HIS A 63 FE HDM A 95 1555 1555 1.94
SITE 1 AC1 12 LEU A 25 LEU A 32 PHE A 35 HIS A 39
SITE 2 AC1 12 PRO A 40 VAL A 45 LEU A 46 ASN A 57
SITE 3 AC1 12 PHE A 58 HIS A 63 ALA A 67 SER A 71
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