Header list of 1pc2.pdb file
Complete list - b 23 2 Bytes
HEADER UNKNOWN FUNCTION 15-MAY-03 1PC2
TITLE SOLUTION STRUCTURE OF HUMAN MITOCHONDRIA FISSION PROTEIN FIS1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOCHONDRIA FISSION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FIS1, SIMILAR TO CGI-135 PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FIS1;
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: PET21
KEYWDS MITOCHONDRIA, FISSION, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SUZUKI,R.J.YOULE,N.TJANDRA
REVDAT 3 23-FEB-22 1PC2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PC2 1 VERSN
REVDAT 1 09-DEC-03 1PC2 0
JRNL AUTH M.SUZUKI,S.Y.JEONG,M.KARBOWSKI,R.J.YOULE,N.TJANDRA
JRNL TITL THE SOLUTION STRUCTURE OF HUMAN MITOCHONDRIA FISSION PROTEIN
JRNL TITL 2 FIS1 REVEALS A NOVEL TPR-LIKE HELIX BUNDLE
JRNL REF J.MOL.BIOL. V. 334 445 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14623186
JRNL DOI 10.1016/J.JMB.2003.09.064
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, XPLOR-NIH 2.0.6
REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PC2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019224.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 10MM TRIS ACETATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN U-15N; 1MM PROTEIN U
REMARK 210 -15N,13C; 1MM PROTEIN U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_NOESY; 4D_
REMARK 210 13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, PIPP 4.2.8, XPLOR
REMARK 210 -NIH 2.0.6
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 O ARG A 112 H LYS A 116 1.53
REMARK 500 H SER A 66 OE1 GLU A 69 1.54
REMARK 500 O LEU A 84 H GLU A 86 1.55
REMARK 500 O GLN A 70 H VAL A 74 1.60
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 2 75.92 -69.64
REMARK 500 1 LEU A 8 -87.89 -65.24
REMARK 500 1 SER A 66 -165.80 -70.63
REMARK 500 1 LEU A 84 32.06 -67.52
REMARK 500 1 LYS A 85 -37.56 64.91
REMARK 500 1 GLU A 86 95.86 -51.50
REMARK 500 1 ASP A 121 3.91 -66.26
REMARK 500 1 LEU A 123 108.61 53.61
REMARK 500 1 VAL A 124 -161.81 -69.25
REMARK 500 1 MET A 126 -120.73 47.74
REMARK 500 1 LEU A 134 -153.30 -76.30
REMARK 500 1 VAL A 136 63.68 -69.30
REMARK 500 1 ALA A 137 98.49 52.25
REMARK 500 1 LEU A 139 -95.14 -71.90
REMARK 500 1 ALA A 140 -92.83 -72.31
REMARK 500 1 ILE A 143 -23.36 -160.59
REMARK 500 1 LEU A 145 -158.51 -68.54
REMARK 500 1 HIS A 149 79.85 -68.06
REMARK 500 1 HIS A 150 117.63 -169.29
REMARK 500 1 HIS A 151 -150.40 -64.86
REMARK 500 2 GLU A 2 20.38 -74.55
REMARK 500 2 ALA A 3 -175.49 53.80
REMARK 500 2 VAL A 4 91.07 50.24
REMARK 500 2 GLU A 7 137.42 62.11
REMARK 500 2 SER A 45 -162.82 -101.49
REMARK 500 2 SER A 66 -166.94 -64.80
REMARK 500 2 LEU A 84 29.08 -70.91
REMARK 500 2 LYS A 85 2.59 55.52
REMARK 500 2 ASP A 121 8.14 -68.88
REMARK 500 2 VAL A 129 -8.80 -146.29
REMARK 500 2 MET A 132 74.28 59.30
REMARK 500 2 ALA A 133 27.45 -171.41
REMARK 500 2 LEU A 134 36.35 -70.90
REMARK 500 2 ALA A 137 -81.38 -65.57
REMARK 500 2 LEU A 145 -150.24 -73.49
REMARK 500 2 HIS A 148 -156.75 -164.45
REMARK 500 2 HIS A 149 60.81 -173.67
REMARK 500 2 HIS A 151 -125.38 51.17
REMARK 500 3 GLU A 2 -2.76 -152.88
REMARK 500 3 ALA A 3 104.32 -168.67
REMARK 500 3 VAL A 4 67.78 -67.34
REMARK 500 3 LEU A 5 -154.46 52.47
REMARK 500 3 LEU A 8 -80.92 -72.98
REMARK 500 3 SER A 66 -175.94 -64.52
REMARK 500 3 LEU A 84 20.69 -69.21
REMARK 500 3 LYS A 85 -8.31 65.53
REMARK 500 3 GLU A 86 97.66 -67.45
REMARK 500 3 ASP A 121 21.80 -75.21
REMARK 500 3 VAL A 124 -158.18 -95.76
REMARK 500 3 MET A 126 -104.02 -56.28
REMARK 500
REMARK 500 THIS ENTRY HAS 409 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PC2 A 1 145 UNP Q9Y3D6 TTC11_HUMAN 1 145
SEQADV 1PC2 GLU A 146 UNP Q9Y3D6 EXPRESSION TAG
SEQADV 1PC2 HIS A 147 UNP Q9Y3D6 EXPRESSION TAG
SEQADV 1PC2 HIS A 148 UNP Q9Y3D6 EXPRESSION TAG
SEQADV 1PC2 HIS A 149 UNP Q9Y3D6 EXPRESSION TAG
SEQADV 1PC2 HIS A 150 UNP Q9Y3D6 EXPRESSION TAG
SEQADV 1PC2 HIS A 151 UNP Q9Y3D6 EXPRESSION TAG
SEQADV 1PC2 HIS A 152 UNP Q9Y3D6 EXPRESSION TAG
SEQRES 1 A 152 MET GLU ALA VAL LEU ASN GLU LEU VAL SER VAL GLU ASP
SEQRES 2 A 152 LEU LEU LYS PHE GLU LYS LYS PHE GLN SER GLU LYS ALA
SEQRES 3 A 152 ALA GLY SER VAL SER LYS SER THR GLN PHE GLU TYR ALA
SEQRES 4 A 152 TRP CYS LEU VAL ARG SER LYS TYR ASN ASP ASP ILE ARG
SEQRES 5 A 152 LYS GLY ILE VAL LEU LEU GLU GLU LEU LEU PRO LYS GLY
SEQRES 6 A 152 SER LYS GLU GLU GLN ARG ASP TYR VAL PHE TYR LEU ALA
SEQRES 7 A 152 VAL GLY ASN TYR ARG LEU LYS GLU TYR GLU LYS ALA LEU
SEQRES 8 A 152 LYS TYR VAL ARG GLY LEU LEU GLN THR GLU PRO GLN ASN
SEQRES 9 A 152 ASN GLN ALA LYS GLU LEU GLU ARG LEU ILE ASP LYS ALA
SEQRES 10 A 152 MET LYS LYS ASP GLY LEU VAL GLY MET ALA ILE VAL GLY
SEQRES 11 A 152 GLY MET ALA LEU GLY VAL ALA GLY LEU ALA GLY LEU ILE
SEQRES 12 A 152 GLY LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 VAL A 11 ALA A 27 1 17
HELIX 2 2 LYS A 32 VAL A 43 1 12
HELIX 3 3 ASN A 48 LEU A 62 1 15
HELIX 4 4 LYS A 67 ARG A 83 1 17
HELIX 5 5 TYR A 87 THR A 100 1 14
HELIX 6 6 ASN A 105 LYS A 120 1 16
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