HEADER MEMBRANE PROTEIN 11-SEP-13 2MDK
TITLE NMR SOLUTION STRUCTURE OF MSP-P56S DOMAIN/VAPB IN DPC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN B/C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-125;
COMPND 5 SYNONYM: VAMP-B/VAMP-C, VAMP-ASSOCIATED PROTEIN B/C, VAP-B/VAP-C;
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: VAPB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PGEX-4T-1
KEYWDS MSP-P56S DOMAIN, VAPB, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR H.QIN,L.LIM,J.SONG
REVDAT 1 30-OCT-13 2MDK 0
JRNL AUTH H.QIN,L.LIM,J.SONG
JRNL TITL MSP-P56S DOMAIN, VAPB IN DPC
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MDK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB103507.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20 MM DPC-1, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D CBCA(CO)NH; 3D 1H-15N TOCSY;
REMARK 210 3D 1H-15N NOESY; 3D HCCH-TOCSY;
REMARK 210 3D HBHA(CO)NH; 3D HN(CO)CA; 3D
REMARK 210 HNCACB; 3D HNCO; 3D C(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS
REMARK 210 METHOD USED : DGSA-DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 ILE A 60 H ALA A 63 1.50
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 LYS A 3 89.72 -57.62
REMARK 500 1 SER A 9 73.77 -64.50
REMARK 500 1 PRO A 12 92.23 -60.99
REMARK 500 1 GLU A 15 101.14 66.59
REMARK 500 1 LEU A 16 111.05 156.51
REMARK 500 1 LYS A 17 -80.75 59.02
REMARK 500 1 PHE A 18 -49.72 -174.62
REMARK 500 1 ASN A 34 107.04 -54.71
REMARK 500 1 ASN A 39 160.94 74.76
REMARK 500 1 CYS A 41 -170.79 -178.20
REMARK 500 1 VAL A 44 -64.14 -127.29
REMARK 500 1 LYS A 45 -80.44 153.99
REMARK 500 1 CYS A 53 119.97 110.98
REMARK 500 1 VAL A 54 106.32 -45.64
REMARK 500 1 SER A 66 22.98 -79.72
REMARK 500 1 ASN A 68 -105.53 168.49
REMARK 500 1 LEU A 73 -68.13 -96.97
REMARK 500 1 ASN A 81 52.13 162.98
REMARK 500 1 LYS A 85 90.61 37.66
REMARK 500 1 LYS A 87 133.36 177.80
REMARK 500 1 ALA A 95 -67.31 159.65
REMARK 500 1 PRO A 96 79.25 -20.19
REMARK 500 1 ALA A 109 -157.32 76.13
REMARK 500 2 ALA A 2 76.45 -103.70
REMARK 500 2 LYS A 3 64.12 38.68
REMARK 500 2 SER A 9 23.11 42.42
REMARK 500 2 HIS A 14 153.27 57.86
REMARK 500 2 LEU A 16 -101.05 -57.46
REMARK 500 2 PHE A 18 -84.24 69.71
REMARK 500 2 ARG A 19 89.79 -57.66
REMARK 500 2 LEU A 32 56.72 -69.30
REMARK 500 2 ARG A 38 91.61 29.90
REMARK 500 2 ASN A 39 -69.44 -154.50
REMARK 500 2 VAL A 40 -67.93 -121.64
REMARK 500 2 PHE A 42 -39.99 -159.84
REMARK 500 2 LYS A 43 75.65 -64.54
REMARK 500 2 VAL A 44 39.03 39.95
REMARK 500 2 LYS A 45 -80.54 -104.75
REMARK 500 2 THR A 47 175.67 52.07
REMARK 500 2 ARG A 50 -66.10 -98.72
REMARK 500 2 ARG A 51 -63.35 -168.37
REMARK 500 2 CYS A 53 -41.85 171.81
REMARK 500 2 ILE A 60 -63.45 71.69
REMARK 500 2 SER A 66 61.40 -107.68
REMARK 500 2 LEU A 73 -68.01 -172.92
REMARK 500 2 GLN A 74 104.57 -48.34
REMARK 500 2 PHE A 76 -65.84 67.10
REMARK 500 2 ASP A 77 46.76 80.32
REMARK 500 2 TYR A 78 78.58 38.79
REMARK 500 2 PRO A 80 64.05 -66.78
REMARK 500
REMARK 500 THIS ENTRY HAS 303 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19489 RELATED DB: BMRB
DBREF 2MDK A 1 125 UNP O95292 VAPB_HUMAN 1 125
SEQADV 2MDK SER A 56 UNP O95292 PRO 56 ENGINEERED MUTATION
SEQRES 1 A 125 MET ALA LYS VAL GLU GLN VAL LEU SER LEU GLU PRO GLN
SEQRES 2 A 125 HIS GLU LEU LYS PHE ARG GLY PRO PHE THR ASP VAL VAL
SEQRES 3 A 125 THR THR ASN LEU LYS LEU GLY ASN PRO THR ASP ARG ASN
SEQRES 4 A 125 VAL CYS PHE LYS VAL LYS THR THR ALA PRO ARG ARG TYR
SEQRES 5 A 125 CYS VAL ARG SER ASN SER GLY ILE ILE ASP ALA GLY ALA
SEQRES 6 A 125 SER ILE ASN VAL SER VAL MET LEU GLN PRO PHE ASP TYR
SEQRES 7 A 125 ASP PRO ASN GLU LYS SER LYS HIS LYS PHE MET VAL GLN
SEQRES 8 A 125 SER MET PHE ALA PRO THR ASP THR SER ASP MET GLU ALA
SEQRES 9 A 125 VAL TRP LYS GLU ALA LYS PRO GLU ASP LEU MET ASP SER
SEQRES 10 A 125 LYS LEU ARG CYS VAL PHE GLU LEU
HELIX 1 1 PRO A 21 LYS A 31 1 11
HELIX 2 2 MET A 89 MET A 93 5 5
HELIX 3 3 THR A 97 ALA A 109 1 13
HELIX 4 4 ALA A 109 LEU A 125 1 17
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
(ATOM LINES ARE NOT SHOWN.)
END
