Header list of 1m12.pdb file
Complete list - b 23 2 Bytes
HEADER MEMBRANE PROTEIN 17-JUN-02 1M12
TITLE NMR SOLUTION STRUCTURE OF HUMAN SAPOSIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SAPOSIN C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-30B
KEYWDS DISULFIDE BRIDGES, ALPHA-HELICES, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.DE ALBA,S.WEILER,N.TJANDRA
REVDAT 4 23-FEB-22 1M12 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1M12 1 VERSN
REVDAT 2 24-FEB-04 1M12 1 JRNL HEADER
REVDAT 1 29-JUL-03 1M12 0
JRNL AUTH E.DE ALBA,S.WEILER,N.TJANDRA
JRNL TITL SOLUTION STRUCTURE OF HUMAN SAPOSIN C: PH-DEPENDENT
JRNL TITL 2 INTERACTION WITH PHOSPHOLIPID VESICLES.
JRNL REF BIOCHEMISTRY V. 42 14729 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14674747
JRNL DOI 10.1021/BI0301338
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.840
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED WITH:
REMARK 3 1806 NOE-DERIVED DESTANCE CONSTRIANTS (NO INTRA-RESIDUE NOES USED),
REMARK 3 28 HYDROGEN BONDS, 135 DIHEDRAL RESTRAINTS, 276 RESIDUAL DIPOLAR
REMARK 3 COUPLINGS.
REMARK 3 RESIDUES 1-3 AND 79-84 ARE DISORDERED.
REMARK 3 SUPERIMPOSITION OF STRUCTURES IS FROM RESIDUES 4-78.
REMARK 4
REMARK 4 1M12 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016465.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : ~10-20MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N; U-15N, U-13C; U-15N, U
REMARK 210 -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; 3D_13C-
REMARK 210 SEPARATED_TOCSY; CBCACONH,
REMARK 210 HNCACB; EXPERIMENTS FOR RESIDUAL
REMARK 210 DIPOLAR COUPLING MEASUREMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, PIPP 4.2.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 163
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:
REMARK 210 RESIDUAL DIPOLAR COUPLINGS MEASURED IN TWO DIFFERENT ALIGNMENT
REMARK 210 MEDIA.
REMARK 210 PF1 AND FD PHAGES
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 ASN A 22 41.61 81.18
REMARK 500 1 PHE A 32 -9.07 -53.17
REMARK 500 1 PRO A 40 158.92 -45.36
REMARK 500 1 SER A 44 -70.74 -37.23
REMARK 500 1 HIS A 76 19.66 47.36
REMARK 500 1 SER A 79 175.25 -51.34
REMARK 500 1 VAL A 82 94.54 -29.25
REMARK 500 2 ASP A 2 99.27 -61.95
REMARK 500 2 ASN A 22 42.29 81.23
REMARK 500 2 PRO A 40 158.81 -45.67
REMARK 500 2 GLU A 65 27.77 81.08
REMARK 500 2 HIS A 76 18.19 45.96
REMARK 500 2 SER A 79 -4.50 68.51
REMARK 500 2 LEU A 81 -7.59 65.64
REMARK 500 3 ASN A 22 40.56 77.97
REMARK 500 3 PRO A 40 157.88 -43.02
REMARK 500 3 HIS A 76 21.23 47.88
REMARK 500 3 SER A 79 35.89 75.59
REMARK 500 3 PRO A 83 63.88 -65.28
REMARK 500 4 ASN A 22 41.21 78.95
REMARK 500 4 PRO A 40 158.93 -45.40
REMARK 500 4 SER A 44 -72.04 -36.66
REMARK 500 4 HIS A 76 19.88 46.59
REMARK 500 4 SER A 79 40.74 77.91
REMARK 500 4 VAL A 82 94.24 -29.05
REMARK 500 5 ASN A 22 41.07 80.76
REMARK 500 5 PRO A 40 158.46 -42.95
REMARK 500 5 GLU A 64 30.03 -86.43
REMARK 500 5 HIS A 76 23.86 48.16
REMARK 500 5 LEU A 81 -18.57 -44.65
REMARK 500 6 ASN A 22 39.03 81.48
REMARK 500 6 PHE A 32 -9.43 -53.60
REMARK 500 6 PRO A 40 158.73 -45.20
REMARK 500 6 SER A 44 -71.86 -36.80
REMARK 500 6 GLU A 64 31.73 -85.42
REMARK 500 6 HIS A 76 22.66 46.53
REMARK 500 6 PRO A 83 3.11 -63.72
REMARK 500 7 ASN A 22 41.24 79.32
REMARK 500 7 PRO A 40 158.79 -45.44
REMARK 500 7 SER A 44 -73.20 -37.26
REMARK 500 7 GLU A 64 34.60 -86.07
REMARK 500 7 HIS A 76 22.09 46.66
REMARK 500 7 LEU A 81 37.46 -84.83
REMARK 500 7 VAL A 82 151.47 -37.24
REMARK 500 7 PRO A 83 109.43 -42.65
REMARK 500 8 ASN A 22 42.22 78.50
REMARK 500 8 PRO A 40 159.94 -43.71
REMARK 500 8 GLU A 65 30.05 75.57
REMARK 500 8 PRO A 83 9.52 -68.67
REMARK 500 9 ASN A 22 42.06 78.05
REMARK 500
REMARK 500 THIS ENTRY HAS 124 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NKL RELATED DB: PDB
REMARK 900 ANOTHER PROTEIN WITH THE SAPOSIN FOLD
DBREF 1M12 A 1 80 UNP P07602 SAP_HUMAN 311 390
SEQADV 1M12 LEU A 81 UNP P07602 CLONING ARTIFACT
SEQADV 1M12 VAL A 82 UNP P07602 CLONING ARTIFACT
SEQADV 1M12 PRO A 83 UNP P07602 CLONING ARTIFACT
SEQADV 1M12 ARG A 84 UNP P07602 CLONING ARTIFACT
SEQRES 1 A 84 SER ASP VAL TYR CYS GLU VAL CYS GLU PHE LEU VAL LYS
SEQRES 2 A 84 GLU VAL THR LYS LEU ILE ASP ASN ASN LYS THR GLU LYS
SEQRES 3 A 84 GLU ILE LEU ASP ALA PHE ASP LYS MET CYS SER LYS LEU
SEQRES 4 A 84 PRO LYS SER LEU SER GLU GLU CYS GLN GLU VAL VAL ASP
SEQRES 5 A 84 THR TYR GLY SER SER ILE LEU SER ILE LEU LEU GLU GLU
SEQRES 6 A 84 VAL SER PRO GLU LEU VAL CYS SER MET LEU HIS LEU CYS
SEQRES 7 A 84 SER GLY LEU VAL PRO ARG
HELIX 1 1 ASP A 2 ASN A 21 1 20
HELIX 2 2 THR A 24 PHE A 32 1 9
HELIX 3 3 ASP A 33 LYS A 34 5 2
HELIX 4 4 MET A 35 LEU A 39 5 5
HELIX 5 5 LEU A 43 LEU A 63 1 21
HELIX 6 6 GLU A 69 LEU A 75 1 7
SSBOND 1 CYS A 5 CYS A 78 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 72 1555 1555 2.03
SSBOND 3 CYS A 36 CYS A 47 1555 1555 2.01
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