Header list of 1afo.pdb file
Complete list - t 27 2 Bytes
HEADER INTEGRAL MEMBRANE PROTEIN 11-MAR-97 1AFO
TITLE DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOPHORIN A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRANSMEMBRANE PEPTIDE;
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 STRAIN: MG-T7;
SOURCE 6 ORGAN: PLASMA;
SOURCE 7 CELL: ERYTHROCYTE;
SOURCE 8 CELLULAR_LOCATION: PLASMA MEMBRANE;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: MG-T7;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS INTEGRAL MEMBRANE PROTEIN, HUMAN GLYCOPHORIN A, TRANSMEMBRANE HELIX
KEYWDS 2 INTERACTIONS, MEMBRANE PROTEIN FOLDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.R.MACKENZIE,J.H.PRESTEGARD,D.M.ENGELMAN
REVDAT 4 27-OCT-21 1AFO 1 REMARK
REVDAT 3 24-FEB-09 1AFO 1 VERSN
REVDAT 2 01-APR-03 1AFO 1 JRNL
REVDAT 1 17-SEP-97 1AFO 0
JRNL AUTH K.R.MACKENZIE,J.H.PRESTEGARD,D.M.ENGELMAN
JRNL TITL A TRANSMEMBRANE HELIX DIMER: STRUCTURE AND IMPLICATIONS.
JRNL REF SCIENCE V. 276 131 1997
JRNL REFN ISSN 0036-8075
JRNL PMID 9082985
JRNL DOI 10.1126/SCIENCE.276.5309.131
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.R.MACKENZIE
REMARK 1 TITL STRUCTURE DETERMINATION OF THE DIMERIC MEMBRANE SPANNING
REMARK 1 TITL 2 DOMAIN OF GLYCOPHORIN A IN DETERGENT MICELLES BY TRIPLE
REMARK 1 TITL 3 RESONANCE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF THESIS, YALE UNIVERSITY 1996
REMARK 1 PUBL NEW HAVEN : YALE UNIVERSITY (THESIS)
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.R.MACKENZIE,J.H.PRESTEGARD,D.M.ENGELMAN
REMARK 1 TITL LEUCINE SIDE-CHAIN ROTAMERS IN A GLYCOPHORIN A TRANSMEMBRANE
REMARK 1 TITL 2 PEPTIDE AS REVEALED BY THREE-BOND CARBON-CARBON COUPLINGS
REMARK 1 TITL 3 AND 13C CHEMICAL SHIFTS
REMARK 1 REF J.BIOMOL.NMR V. 7 256 1996
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AFO 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_1000170757.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; CBCACONH; HCCH-TOCSY; 15N
REMARK 210 NOESY-HSQC; 13C NOESY-HSQC; HNHA;
REMARK 210 SPIN-ECHO DIFF CT HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA; VARIAN
REMARK 210 SPECTROMETER MANUFACTURER : GE; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING HYBRID
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 38
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 LEU A 64 -165.82 46.11
REMARK 500 1 ALA A 65 31.32 -163.00
REMARK 500 1 HIS A 67 -53.27 170.12
REMARK 500 1 SER A 69 174.92 51.29
REMARK 500 1 ILE A 99 -112.97 -82.55
REMARK 500 1 LYS A 100 -174.81 47.63
REMARK 500 1 HIS B 66 114.11 77.93
REMARK 500 1 HIS B 67 38.02 168.20
REMARK 500 1 PHE B 68 -88.24 -141.98
REMARK 500 1 GLU B 72 -73.71 -66.30
REMARK 500 1 ILE B 99 102.18 94.28
REMARK 500 2 GLN A 63 143.07 179.89
REMARK 500 2 ALA A 65 60.50 64.15
REMARK 500 2 HIS A 67 74.19 -152.35
REMARK 500 2 PHE A 68 84.37 -58.74
REMARK 500 2 SER A 69 -152.28 -104.06
REMARK 500 2 GLU A 70 -55.38 168.68
REMARK 500 2 PRO A 71 83.54 -58.12
REMARK 500 2 GLU A 72 -72.18 -67.51
REMARK 500 2 LEU B 64 159.23 67.71
REMARK 500 2 ALA B 65 68.97 -165.87
REMARK 500 2 SER B 69 -152.33 -150.57
REMARK 500 2 GLU B 70 98.23 73.34
REMARK 500 2 PRO B 71 58.48 -62.28
REMARK 500 2 GLU B 72 -74.95 -65.15
REMARK 500 2 LYS B 100 -162.83 -115.08
REMARK 500 3 LEU A 64 173.51 -53.98
REMARK 500 3 ALA A 65 104.28 -166.49
REMARK 500 3 HIS A 66 -148.84 -70.32
REMARK 500 3 HIS A 67 -175.60 -65.94
REMARK 500 3 SER A 69 157.82 -46.62
REMARK 500 3 GLU A 72 -74.68 -63.21
REMARK 500 3 HIS B 67 -169.49 -163.84
REMARK 500 3 PHE B 68 -56.15 75.94
REMARK 500 3 PRO B 71 106.43 -59.72
REMARK 500 4 ALA A 65 24.52 -144.24
REMARK 500 4 HIS A 66 77.86 51.41
REMARK 500 4 HIS A 67 -55.30 -158.88
REMARK 500 4 PHE A 68 -62.92 68.38
REMARK 500 4 SER A 69 48.12 76.17
REMARK 500 4 GLU A 70 101.54 55.46
REMARK 500 4 GLU A 72 -70.77 -59.29
REMARK 500 4 GLN B 63 167.03 61.01
REMARK 500 4 LEU B 64 -28.80 175.80
REMARK 500 4 HIS B 66 63.82 -154.74
REMARK 500 4 HIS B 67 69.29 -101.28
REMARK 500 4 PHE B 68 90.23 -67.17
REMARK 500 4 SER B 69 109.37 75.90
REMARK 500 4 GLU B 72 -74.76 -48.54
REMARK 500 4 ILE B 99 -131.52 -79.71
REMARK 500
REMARK 500 THIS ENTRY HAS 191 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 ARG A 96 0.31 SIDE CHAIN
REMARK 500 1 ARG A 97 0.24 SIDE CHAIN
REMARK 500 1 ARG B 96 0.25 SIDE CHAIN
REMARK 500 1 ARG B 97 0.31 SIDE CHAIN
REMARK 500 2 ARG A 96 0.23 SIDE CHAIN
REMARK 500 2 ARG A 97 0.18 SIDE CHAIN
REMARK 500 2 ARG B 96 0.19 SIDE CHAIN
REMARK 500 2 ARG B 97 0.31 SIDE CHAIN
REMARK 500 3 ARG A 96 0.20 SIDE CHAIN
REMARK 500 3 ARG A 97 0.27 SIDE CHAIN
REMARK 500 3 ARG B 96 0.32 SIDE CHAIN
REMARK 500 3 ARG B 97 0.30 SIDE CHAIN
REMARK 500 4 ARG A 96 0.12 SIDE CHAIN
REMARK 500 4 ARG A 97 0.31 SIDE CHAIN
REMARK 500 4 ARG B 96 0.30 SIDE CHAIN
REMARK 500 4 ARG B 97 0.24 SIDE CHAIN
REMARK 500 5 ARG A 96 0.29 SIDE CHAIN
REMARK 500 5 ARG A 97 0.17 SIDE CHAIN
REMARK 500 5 ARG B 96 0.30 SIDE CHAIN
REMARK 500 5 ARG B 97 0.23 SIDE CHAIN
REMARK 500 6 ARG A 96 0.32 SIDE CHAIN
REMARK 500 6 ARG A 97 0.20 SIDE CHAIN
REMARK 500 6 ARG B 96 0.27 SIDE CHAIN
REMARK 500 6 ARG B 97 0.26 SIDE CHAIN
REMARK 500 7 ARG A 96 0.27 SIDE CHAIN
REMARK 500 7 ARG A 97 0.24 SIDE CHAIN
REMARK 500 7 ARG B 96 0.28 SIDE CHAIN
REMARK 500 7 ARG B 97 0.28 SIDE CHAIN
REMARK 500 8 ARG A 96 0.24 SIDE CHAIN
REMARK 500 8 ARG A 97 0.32 SIDE CHAIN
REMARK 500 8 ARG B 96 0.31 SIDE CHAIN
REMARK 500 8 ARG B 97 0.30 SIDE CHAIN
REMARK 500 9 ARG A 96 0.17 SIDE CHAIN
REMARK 500 9 ARG A 97 0.28 SIDE CHAIN
REMARK 500 9 ARG B 96 0.30 SIDE CHAIN
REMARK 500 9 ARG B 97 0.19 SIDE CHAIN
REMARK 500 10 ARG A 96 0.23 SIDE CHAIN
REMARK 500 10 ARG A 97 0.25 SIDE CHAIN
REMARK 500 10 ARG B 96 0.32 SIDE CHAIN
REMARK 500 10 ARG B 97 0.28 SIDE CHAIN
REMARK 500 11 ARG A 96 0.19 SIDE CHAIN
REMARK 500 11 ARG A 97 0.27 SIDE CHAIN
REMARK 500 11 ARG B 96 0.24 SIDE CHAIN
REMARK 500 11 ARG B 97 0.23 SIDE CHAIN
REMARK 500 12 ARG A 96 0.30 SIDE CHAIN
REMARK 500 12 ARG A 97 0.27 SIDE CHAIN
REMARK 500 12 ARG B 96 0.31 SIDE CHAIN
REMARK 500 12 ARG B 97 0.32 SIDE CHAIN
REMARK 500 13 ARG A 96 0.28 SIDE CHAIN
REMARK 500 13 ARG A 97 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 79 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AFO A 62 101 UNP P02724 GLPA_HUMAN 81 120
DBREF 1AFO B 62 101 UNP P02724 GLPA_HUMAN 81 120
SEQRES 1 A 40 VAL GLN LEU ALA HIS HIS PHE SER GLU PRO GLU ILE THR
SEQRES 2 A 40 LEU ILE ILE PHE GLY VAL MET ALA GLY VAL ILE GLY THR
SEQRES 3 A 40 ILE LEU LEU ILE SER TYR GLY ILE ARG ARG LEU ILE LYS
SEQRES 4 A 40 LYS
SEQRES 1 B 40 VAL GLN LEU ALA HIS HIS PHE SER GLU PRO GLU ILE THR
SEQRES 2 B 40 LEU ILE ILE PHE GLY VAL MET ALA GLY VAL ILE GLY THR
SEQRES 3 B 40 ILE LEU LEU ILE SER TYR GLY ILE ARG ARG LEU ILE LYS
SEQRES 4 B 40 LYS
HELIX 1 1 GLU A 72 LEU A 98 1 27
HELIX 2 2 GLU B 72 LEU B 98 1 27
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 - t 27 2 Bytes