Header list of 1vry.pdb file
Complete list - t 20 2 Bytes
HEADER MEMBRANE PROTEIN 20-JUL-05 1VRY
TITLE SECOND AND THIRD TRANSMEMBRANE DOMAINS OF THE ALPHA-1 SUBUNIT OF HUMAN
TITLE 2 GLYCINE RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE RECEPTOR ALPHA-1 CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND AND THIRD TRANSMEMBRANE DOMAINS;
COMPND 5 SYNONYM: GLYCINE RECEPTOR 48 KDA SUBUNIT, STRYCHNINE BINDING SUBUNIT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GLRA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLYSS
KEYWDS GLYCINE RECEPTOR, SECOND TRANSMEMBRANE DOMAIN, THIRD TRANSMEMBRANE
KEYWDS 2 DOMAIN, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.MA,Z.LIU,L.LI,P.TANG,Y.XU
REVDAT 3 20-OCT-21 1VRY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1VRY 1 VERSN
REVDAT 1 26-JUL-05 1VRY 0
SPRSDE 26-JUL-05 1VRY 1ZHD
JRNL AUTH D.MA,Z.LIU,L.LI,P.TANG,Y.XU
JRNL TITL STRUCTURE AND DYNAMICS OF THE SECOND AND THIRD TRANSMEMBRANE
JRNL TITL 2 DOMAINS OF HUMAN GLYCINE RECEPTOR.
JRNL REF BIOCHEMISTRY V. 44 8790 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15952785
JRNL DOI 10.1021/BI050256N
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.6
REMARK 3 AUTHORS : SCHWIETERS, C.D. ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VRY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000003000.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM TM23 U-15N, TRIFLUOROETHANOL
REMARK 210 -D2; 1MM TM23 U-15N,13C,
REMARK 210 TRIFLUOROETHANOL-D2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 2D TOCSY; 3D HNCA; 3D HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE SGI6X,
REMARK 210 XPLOR-NIH 2.9.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 15N FILTERED
REMARK 210 NOESY SPECTROSCOPY AND H/D EXCHANGE EXPERIMENTS TOGETHER WITH HA
REMARK 210 AND CA CHEMICAL SHIFT INDEXES FOR IDENTIFICATION OF INTRAHELICAL
REMARK 210 HYDROGEN BONDING.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LYS A 58
REMARK 465 LYS A 59
REMARK 465 LYS A 60
REMARK 465 LYS A 61
REMARK 465 HIS A 62
REMARK 465 ARG A 63
REMARK 465 LEU A 64
REMARK 465 LEU A 65
REMARK 465 GLU A 66
REMARK 465 HIS A 67
REMARK 465 HIS A 68
REMARK 465 HIS A 69
REMARK 465 HIS A 70
REMARK 465 HIS A 71
REMARK 465 HIS A 72
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 TRP A 34 H CYS A 38 1.57
REMARK 500 O LEU A 35 H LEU A 39 1.58
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 VAL A 1 -74.20 -60.33
REMARK 500 1 SER A 21 -58.67 -174.20
REMARK 500 1 LYS A 24 -51.01 -177.99
REMARK 500 1 ASP A 32 -33.47 161.25
REMARK 500 2 VAL A 1 -74.05 -60.21
REMARK 500 2 ALA A 20 -50.77 -177.30
REMARK 500 2 LEU A 22 53.71 -175.53
REMARK 500 2 LYS A 24 -46.95 -177.46
REMARK 500 2 ASP A 32 -37.00 177.62
REMARK 500 3 VAL A 1 -73.03 -58.12
REMARK 500 3 ARG A 19 -70.86 -161.75
REMARK 500 3 ALA A 20 -56.90 178.51
REMARK 500 3 SER A 21 133.59 -177.26
REMARK 500 3 LEU A 22 65.78 -170.16
REMARK 500 3 LYS A 24 -100.85 -159.55
REMARK 500 3 ASP A 32 -38.26 177.88
REMARK 500 3 SER A 56 -131.92 -165.46
REMARK 500 4 VAL A 1 -72.90 -58.56
REMARK 500 4 ALA A 20 -48.56 -174.32
REMARK 500 4 LEU A 22 62.73 -179.88
REMARK 500 4 LYS A 24 -46.08 -174.31
REMARK 500 4 ASP A 32 -37.04 179.72
REMARK 500 5 VAL A 1 -73.81 -59.83
REMARK 500 5 ARG A 19 -79.93 -167.61
REMARK 500 5 ALA A 20 -45.44 168.41
REMARK 500 5 LEU A 22 61.90 -170.50
REMARK 500 5 LYS A 24 -51.34 -176.90
REMARK 500 5 ASP A 32 -38.18 179.39
REMARK 500 5 SER A 56 122.33 58.33
REMARK 500 6 VAL A 1 -74.33 -60.18
REMARK 500 6 ARG A 19 -36.83 71.27
REMARK 500 6 LEU A 22 61.51 -174.83
REMARK 500 6 LYS A 24 -51.82 -171.97
REMARK 500 6 ASP A 32 -34.12 165.15
REMARK 500 7 VAL A 1 -73.48 -58.03
REMARK 500 7 ARG A 19 -65.47 -164.12
REMARK 500 7 ALA A 20 -44.84 171.71
REMARK 500 7 LEU A 22 60.20 -176.18
REMARK 500 7 LYS A 24 -48.91 -175.79
REMARK 500 7 ASP A 32 -38.87 179.26
REMARK 500 7 SER A 56 -139.48 -157.48
REMARK 500 8 VAL A 1 -72.00 -65.21
REMARK 500 8 ARG A 19 -49.13 -151.00
REMARK 500 8 ALA A 20 -52.82 -169.78
REMARK 500 8 LEU A 22 55.46 -176.15
REMARK 500 8 LYS A 24 -48.11 -177.17
REMARK 500 8 ASP A 32 -38.25 178.29
REMARK 500 8 ALA A 36 39.89 -82.89
REMARK 500 8 VAL A 37 -49.59 -163.14
REMARK 500 8 SER A 56 57.14 70.25
REMARK 500
REMARK 500 THIS ENTRY HAS 130 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VRY A -2 57 UNP P23415 GLRA1_HUMAN 278 337
SEQADV 1VRY LEU A -3 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY LEU A 11 UNP P23415 MET 291 ENGINEERED MUTATION
SEQADV 1VRY LEU A 35 UNP P23415 MET 315 ENGINEERED MUTATION
SEQADV 1VRY LYS A 58 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY LYS A 59 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY LYS A 60 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY LYS A 61 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY HIS A 62 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY ARG A 63 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY LEU A 64 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY LEU A 65 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY GLU A 66 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY HIS A 67 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY HIS A 68 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY HIS A 69 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY HIS A 70 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY HIS A 71 UNP P23415 CLONING ARTIFACT
SEQADV 1VRY HIS A 72 UNP P23415 CLONING ARTIFACT
SEQRES 1 A 76 LEU PRO ALA ARG VAL GLY LEU GLY ILE THR THR VAL LEU
SEQRES 2 A 76 THR LEU THR THR GLN SER SER GLY SER ARG ALA SER LEU
SEQRES 3 A 76 PRO LYS VAL SER TYR VAL LYS ALA ILE ASP ILE TRP LEU
SEQRES 4 A 76 ALA VAL CYS LEU LEU PHE VAL PHE SER ALA LEU LEU GLU
SEQRES 5 A 76 TYR ALA ALA VAL ASN PHE VAL SER ARG LYS LYS LYS LYS
SEQRES 6 A 76 HIS ARG LEU LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 LEU A -3 GLY A 17 1 21
HELIX 2 2 LYS A 24 TRP A 34 1 11
HELIX 3 3 TRP A 34 SER A 56 1 23
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 20 2 Bytes