Header list of 1mgx.pdb file
Complete list - 29 20 Bytes
HEADER COAGULATION FACTOR 21-JUN-95 1MGX
TITLE COAGULATION FACTOR, MG(II), NMR, 7 STRUCTURES (BACKBONE ATOMS ONLY)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR IX;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE GLA AND AROMATIC AMINO ACID STACK DOMAINS FROM RESIDUES
COMPND 5 1 - 47;
COMPND 6 EC: 3.4.21.22;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS COAGULATION FACTOR, PLASMA
EXPDTA SOLUTION NMR
NUMMDL 7
AUTHOR S.J.FREEDMAN,B.C.FURIE,B.FURIE,J.D.BALEJA
REVDAT 3 29-NOV-17 1MGX 1 REMARK HELIX
REVDAT 2 24-FEB-09 1MGX 1 VERSN
REVDAT 1 08-NOV-96 1MGX 0
JRNL AUTH S.J.FREEDMAN,M.D.BLOSTEIN,J.D.BALEJA,M.JACOBS,B.C.FURIE,
JRNL AUTH 2 B.FURIE
JRNL TITL IDENTIFICATION OF THE PHOSPHOLIPID BINDING SITE IN THE
JRNL TITL 2 VITAMIN K-DEPENDENT BLOOD COAGULATION PROTEIN FACTOR IX.
JRNL REF J.BIOL.CHEM. V. 271 16227 1996
JRNL REFN ISSN 0021-9258
JRNL PMID 8663165
JRNL DOI 10.1074/JBC.271.27.16227
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MGX 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_1000174996.
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 : 7
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-7
REMARK 470 RES CSSEQI ATOMS
REMARK 470 TYR A 1 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 1 OH
REMARK 470 ASN A 2 CB CG OD1 ND2
REMARK 470 SER A 3 CB OG
REMARK 470 LYS A 5 CB CG CD CE NZ
REMARK 470 LEU A 6 CB CG CD1 CD2
REMARK 470 CGU A 7 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 7 OE22
REMARK 470 CGU A 8 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 8 OE22
REMARK 470 PHE A 9 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 10 CB CG1 CG2
REMARK 470 GLN A 11 CB CG CD OE1 NE2
REMARK 470 ASN A 13 CB CG OD1 ND2
REMARK 470 LEU A 14 CB CG CD1 CD2
REMARK 470 CGU A 15 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 15 OE22
REMARK 470 ARG A 16 CB CG CD NE CZ NH1 NH2
REMARK 470 CGU A 17 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 17 OE22
REMARK 470 CYS A 18 CB SG
REMARK 470 MET A 19 CB CG SD CE
REMARK 470 CGU A 20 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 20 OE22
REMARK 470 CGU A 21 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 21 OE22
REMARK 470 LYS A 22 CB CG CD CE NZ
REMARK 470 CYS A 23 CB SG
REMARK 470 SER A 24 CB OG
REMARK 470 PHE A 25 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CGU A 26 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 26 OE22
REMARK 470 CGU A 27 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 27 OE22
REMARK 470 ALA A 28 CB
REMARK 470 ARG A 29 CB CG CD NE CZ NH1 NH2
REMARK 470 CGU A 30 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 30 OE22
REMARK 470 VAL A 31 CB CG1 CG2
REMARK 470 PHE A 32 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CGU A 33 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 33 OE22
REMARK 470 ASN A 34 CB CG OD1 ND2
REMARK 470 THR A 35 CB OG1 CG2
REMARK 470 CGU A 36 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 36 OE22
REMARK 470 ARG A 37 CB CG CD NE CZ NH1 NH2
REMARK 470 THR A 38 CB OG1 CG2
REMARK 470 THR A 39 CB OG1 CG2
REMARK 470 CGU A 40 CB CG CD1 CD2 OE11 OE12 OE21
REMARK 470 CGU A 40 OE22
REMARK 470 PHE A 41 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 42 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP A 42 CZ2 CZ3 CH2
REMARK 470 LYS A 43 CB CG CD CE NZ
REMARK 470 GLN A 44 CB CG CD OE1 NE2
REMARK 470 TYR A 45 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 45 OH
REMARK 470 VAL A 46 CB CG1 CG2
REMARK 470 ASP A 47 CB CG OD1 OD2
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 SER A 3 -79.69 -133.50
REMARK 500 1 CGU A 7 -22.57 82.74
REMARK 500 1 PHE A 9 23.70 -171.33
REMARK 500 1 VAL A 10 -153.61 -125.04
REMARK 500 1 GLN A 11 132.71 177.84
REMARK 500 1 LEU A 14 -54.09 -137.63
REMARK 500 1 CGU A 17 55.21 -114.48
REMARK 500 1 CYS A 18 -42.86 -170.52
REMARK 500 1 MET A 19 -157.19 -81.60
REMARK 500 1 CGU A 20 21.88 39.97
REMARK 500 1 CGU A 21 -111.10 -175.19
REMARK 500 1 LYS A 22 139.05 176.22
REMARK 500 1 CYS A 23 -99.61 -133.76
REMARK 500 1 SER A 24 148.18 -177.93
REMARK 500 1 CGU A 27 -39.57 84.33
REMARK 500 1 ASN A 34 127.77 -171.45
REMARK 500 1 THR A 38 -46.29 146.81
REMARK 500 1 CGU A 40 31.59 -87.00
REMARK 500 1 PHE A 41 -44.79 -151.21
REMARK 500 1 VAL A 46 -146.09 -103.58
REMARK 500 2 ASN A 2 171.85 -50.72
REMARK 500 2 LEU A 6 43.30 -93.79
REMARK 500 2 CGU A 8 -42.18 -159.00
REMARK 500 2 GLN A 11 -164.76 -70.98
REMARK 500 2 LEU A 14 -51.49 89.28
REMARK 500 2 CGU A 17 49.56 -106.81
REMARK 500 2 CYS A 18 -42.60 -154.94
REMARK 500 2 CGU A 21 146.07 -171.39
REMARK 500 2 CYS A 23 14.78 -145.63
REMARK 500 2 SER A 24 -165.51 49.90
REMARK 500 2 CGU A 27 -34.61 82.80
REMARK 500 2 ASN A 34 95.88 -31.74
REMARK 500 2 ARG A 37 -43.46 86.70
REMARK 500 2 THR A 39 -60.99 74.10
REMARK 500 2 VAL A 46 -145.54 -96.51
REMARK 500 3 ASN A 2 122.65 69.40
REMARK 500 3 SER A 3 -90.99 42.04
REMARK 500 3 LYS A 5 43.70 -142.36
REMARK 500 3 LEU A 6 -78.82 -88.97
REMARK 500 3 CGU A 7 173.01 56.47
REMARK 500 3 CGU A 8 23.80 45.17
REMARK 500 3 PHE A 9 23.10 -167.32
REMARK 500 3 VAL A 10 -142.81 -96.81
REMARK 500 3 LEU A 14 -56.70 -120.95
REMARK 500 3 CGU A 17 -68.61 154.01
REMARK 500 3 MET A 19 -154.90 -143.43
REMARK 500 3 CGU A 20 18.21 42.78
REMARK 500 3 CGU A 21 -169.96 179.51
REMARK 500 3 CYS A 23 -152.23 -110.55
REMARK 500 3 ASN A 34 105.71 -45.30
REMARK 500
REMARK 500 THIS ENTRY HAS 106 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MGX A 1 47 UNP P00740 FA9_HUMAN 47 93
SEQADV 1MGX CGU A 7 UNP P00740 GLU 53 CONFLICT
SEQADV 1MGX CGU A 8 UNP P00740 GLU 54 CONFLICT
SEQADV 1MGX CGU A 15 UNP P00740 GLU 61 CONFLICT
SEQADV 1MGX CGU A 17 UNP P00740 GLU 63 CONFLICT
SEQADV 1MGX CGU A 20 UNP P00740 GLU 66 CONFLICT
SEQADV 1MGX CGU A 21 UNP P00740 GLU 67 CONFLICT
SEQADV 1MGX CGU A 26 UNP P00740 GLU 72 CONFLICT
SEQADV 1MGX CGU A 27 UNP P00740 GLU 73 CONFLICT
SEQADV 1MGX CGU A 30 UNP P00740 GLU 76 CONFLICT
SEQADV 1MGX CGU A 33 UNP P00740 GLU 79 CONFLICT
SEQADV 1MGX CGU A 36 UNP P00740 GLU 82 CONFLICT
SEQADV 1MGX CGU A 40 UNP P00740 GLU 86 CONFLICT
SEQRES 1 A 47 TYR ASN SER GLY LYS LEU CGU CGU PHE VAL GLN GLY ASN
SEQRES 2 A 47 LEU CGU ARG CGU CYS MET CGU CGU LYS CYS SER PHE CGU
SEQRES 3 A 47 CGU ALA ARG CGU VAL PHE CGU ASN THR CGU ARG THR THR
SEQRES 4 A 47 CGU PHE TRP LYS GLN TYR VAL ASP
MODRES 1MGX CGU A 7 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 8 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 15 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 17 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 20 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 21 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 26 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 27 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 30 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 33 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 36 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1MGX CGU A 40 GLU GAMMA-CARBOXY-GLUTAMIC ACID
HET CGU A 7 4
HET CGU A 8 4
HET CGU A 15 4
HET CGU A 17 4
HET CGU A 20 4
HET CGU A 21 4
HET CGU A 26 4
HET CGU A 27 4
HET CGU A 30 4
HET CGU A 33 4
HET CGU A 36 4
HET CGU A 40 4
HETNAM CGU GAMMA-CARBOXY-GLUTAMIC ACID
FORMUL 1 CGU 12(C6 H9 N O6)
HELIX 1 1 LEU A 14 ARG A 16 1 3
HELIX 2 2 PHE A 25 PHE A 32 1 8
HELIX 3 3 THR A 35 TYR A 45 1 11
LINK N CGU A 7 C LEU A 6 1555 1555 1.32
LINK C CGU A 7 N CGU A 8 1555 1555 1.32
LINK C CGU A 8 N PHE A 9 1555 1555 1.32
LINK N CGU A 15 C LEU A 14 1555 1555 1.32
LINK C CGU A 15 N ARG A 16 1555 1555 1.32
LINK N CGU A 17 C ARG A 16 1555 1555 1.32
LINK C CGU A 17 N CYS A 18 1555 1555 1.32
LINK N CGU A 20 C MET A 19 1555 1555 1.32
LINK C CGU A 20 N CGU A 21 1555 1555 1.32
LINK C CGU A 21 N LYS A 22 1555 1555 1.32
LINK N CGU A 26 C PHE A 25 1555 1555 1.32
LINK C CGU A 26 N CGU A 27 1555 1555 1.32
LINK C CGU A 27 N ALA A 28 1555 1555 1.32
LINK N CGU A 30 C ARG A 29 1555 1555 1.32
LINK C CGU A 30 N VAL A 31 1555 1555 1.32
LINK N CGU A 33 C PHE A 32 1555 1555 1.32
LINK C CGU A 33 N ASN A 34 1555 1555 1.32
LINK N CGU A 36 C THR A 35 1555 1555 1.32
LINK C CGU A 36 N ARG A 37 1555 1555 1.32
LINK N CGU A 40 C THR A 39 1555 1555 1.32
LINK C CGU A 40 N PHE A 41 1555 1555 1.32
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 - 29 20 Bytes