Header list of 2hyn.pdb file
Complete list - ar 9 Bytes
HEADER MEMBRANE PROTEIN/SIGNALING PROTEIN 07-AUG-06 2HYN
TITLE COMPLETE ENSEMBLE OF NMR STRUCTURES OF UNPHOSPHORYLATED HUMAN
TITLE 2 PHOSPHOLAMBAN PENTAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARDIAC PHOSPHOLAMBAN;
COMPND 3 CHAIN: A, B, C, D, E;
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 GENE: PLN;
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: PMALC2X
KEYWDS SYMMETRIC HOMO-OLIGOMER, PENTAMER, PROTEIN COMPLEX, LEU/ILE ZIPPER,
KEYWDS 2 SUPER COIL, CHANNEL, MEMBRANE PROTEIN-SIGNALING PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 184
AUTHOR S.POTLURI,A.K.YAN,J.J.CHOU,B.R.DONALD,C.BAILEY-KELLOGG
REVDAT 5 09-MAR-22 2HYN 1 REMARK
REVDAT 4 24-FEB-09 2HYN 1 VERSN
REVDAT 3 12-SEP-06 2HYN 1 REMARK
REVDAT 2 05-SEP-06 2HYN 1 JRNL
REVDAT 1 29-AUG-06 2HYN 0
JRNL AUTH S.POTLURI,A.K.YAN,J.J.CHOU,B.R.DONALD,C.BAILEY-KELLOGG
JRNL TITL STRUCTURE DETERMINATION OF SYMMETRIC HOMO-OLIGOMERS BY A
JRNL TITL 2 COMPLETE SEARCH OF SYMMETRY CONFIGURATION SPACE, USING NMR
JRNL TITL 3 RESTRAINTS AND VAN DER WAALS PACKING.
JRNL REF PROTEINS V. 65 203 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16897780
JRNL DOI 10.1002/PROT.21091
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.OXENOID,J.J.CHOU
REMARK 1 TITL THE STRUCTURE OF PHOSPHOLAMBAN PENTAMER REVEALS A
REMARK 1 TITL 2 CHANNEL-LIKE ARCHITECTURE IN MEMBRANES
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 102 10870 2005
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : COMPLETE SCS SEARCH 0, CNS 1.1
REMARK 3 AUTHORS : S. POTLURI, A.K. YAN, B. R. DONALD, C. BAILEY
REMARK 3 -KELLOGG (COMPLETE SCS SEARCH), A.T.BRUNGER,
REMARK 3 P.D.ADAMS, G.M.CLORE, W.L.DELANO,P.GROS,
REMARK 3 R.W.GROSSE-KUNSTLEVE, J.-S.JIANG,J.KUSZEWSKI,
REMARK 3 M.NILGES, N.S.PANNU, R.J.READ,L.M.RICE, T.SIMONSON,
REMARK 3 G.L.WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. MONOMER STRUCTURE: DETERMINED
REMARK 3 WITH SIMULATED ANNEALING PROTOCOL THAT REFINES ALL
REMARK 3 INTRAMONOMER NOES, SIDECHAIN J-COUPLINGS, AND BACKBONE RDCS.
REMARK 3 2. PENTAMER STRUCTURE: DETERMINED BY OUR COMPLETE
REMARK 3 SCS APPROACH. TRADITIONAL NMR PROTOCOLS FOR
REMARK 3 SYMMETRIC HOMO-OLIGOMERS (USED FOR STRUCTURES OF PDB ID 1ZLL)
REMARK 3 ARE BASED ON SIMULATED ANNEALING TECHNIQUES AND COULD GET
REMARK 3 TRAPPED IN LOCAL MINIMA. OUR COMPLETE SCS SEARCH APPROACH
REMARK 3 AVOIDS BIAS AND RETURNS ALL CONSISTENT, WELL-PACKED STRUCTURES
REMARK 3 TO WITHIN A USER-DEFINED SIMILARITY LEVEL. ENERGY-MINIMIZATION
REMARK 3 IS USED ONLY AT A LATER STAGE AFTER THE ENSEMBLE OF STRUCTURES
REMARK 3 THAT SATISFY THE DATA HAVE BEEN IDENTIFIED, HENCE ENSURING
REMARK 3 THAT NO CONSISTENT WELL-PACKED CONFORMATION IS MISSED.
REMARK 4
REMARK 4 2HYN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000038916.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 25 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.2 MM PHOSPHOLAMBAN PENTAMER, U
REMARK 210 -15N, 13C, 85% 2H, 25 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 50 MM BME, 200
REMARK 210 MM DPC, 95% H2O, 5% D2O;0.2 MM
REMARK 210 PHOSPHOLAMBAN PENTAMER, U-15N,
REMARK 210 13C, 85% 2H, 25 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 50 MM BME, 200
REMARK 210 MM DPC, 4% STRETCHED
REMARK 210 POLYACRYLAMIDE GEL,95% H2O, 5%
REMARK 210 D2O;0.2 MM PHOSPHOLAMBAN
REMARK 210 PENTAMER, U-15N,13C, 25 MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 50 MM
REMARK 210 BME, 200 MM 2H-DPC, 95% H2O, 5%
REMARK 210 D2O;0.2 MM PHOSPHOLAMBAN
REMARK 210 PENTAMER, 10% 13C-LABELED, 25 MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 50 MM
REMARK 210 BME, 200 MM DPC, 95% H2O, 5% D2O;
REMARK 210 0.2 MM PHOSPHOLAMBAN PENTAMER,
REMARK 210 50% U-15N,13C AND 50% UNLABELED,
REMARK 210 25MM SODIUM PHOSPHATE BUFFER, 50
REMARK 210 MM BME, 200 MM 2H-DPC, 95% H2O,
REMARK 210 5% D2O;0.2 MM PHOSPHOLAMBAN
REMARK 210 PENTAMER, 50% U-15N, U-2H AND 50%
REMARK 210 UNLABELED,25MM SODIUM PHOSPHATE
REMARK 210 BUFFER, 50 MM BME, 200 MM 2H-DPC,
REMARK 210 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TROSY-HNCA, HNCACB, HNCACO,
REMARK 210 MEASUREMENT OF 1H-15N, 13C'-
REMARK 210 13CA, AND 13C'-15N RDCS USING 3D
REMARK 210 HNCO BASED EXPERIMENTS, HCCONH,
REMARK 210 CCONH, 15N-EDITED NOESY, 13C-
REMARK 210 EDITED NOESY, 13C- HSQC FOR
REMARK 210 METHYL STEREOSPECIFIC ASSIGNMENT,
REMARK 210 DOUBLE 13C- FILTERED, 15N-
REMARK 210 EDITED NOESY, 3D 15N-EDITED
REMARK 210 NOESY, 2D SPIN-ECHO DIFFERENCE
REMARK 210 EXPERIMENTS FOR MEASURING 3-BOND
REMARK 210 J(NCG) AND J(CCG) COUPLINGS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : ADAVNCE, DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : COMPLETE SCS SEARCH, ENERGY
REMARK 210 -MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 184
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 184
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES WERE
REMARK 210 SUBMITTED. OUR METHOD GUARANTEES
REMARK 210 THAT THE ENSEMBLE REPRESENTS ALL
REMARK 210 STRUCTURES THAT SATISFY THE DATA
REMARK 210 AND HAVE GOOD VDW PACKING WITHIN
REMARK 210 A USER-DEFINED SIMILARITY LEVEL
REMARK 210 (CHOSEN AS 1 A).
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 GLU A 2 -45.83 75.47
REMARK 500 1 PRO A 21 29.63 -78.82
REMARK 500 1 GLN A 22 -70.79 64.63
REMARK 500 1 CYS A 41 -70.29 -59.35
REMARK 500 1 GLU B 2 -46.00 75.62
REMARK 500 1 PRO B 21 29.64 -78.84
REMARK 500 1 GLN B 22 -70.79 64.69
REMARK 500 1 CYS B 41 -70.23 -59.36
REMARK 500 1 GLU C 2 -45.92 75.54
REMARK 500 1 PRO C 21 29.69 -78.83
REMARK 500 1 GLN C 22 -70.75 64.54
REMARK 500 1 CYS C 41 -70.27 -59.42
REMARK 500 1 GLU D 2 -45.95 75.55
REMARK 500 1 PRO D 21 29.61 -78.74
REMARK 500 1 GLN D 22 -70.83 64.64
REMARK 500 1 CYS D 41 -70.23 -59.46
REMARK 500 1 GLU E 2 -45.91 75.56
REMARK 500 1 PRO E 21 29.55 -78.72
REMARK 500 1 GLN E 22 -70.69 64.60
REMARK 500 1 CYS E 41 -70.27 -59.43
REMARK 500 2 GLU A 2 -46.06 75.63
REMARK 500 2 PRO A 21 29.87 -78.58
REMARK 500 2 GLN A 22 -71.04 64.56
REMARK 500 2 GLU B 2 -46.00 75.61
REMARK 500 2 PRO B 21 29.94 -78.59
REMARK 500 2 GLN B 22 -70.88 64.45
REMARK 500 2 GLU C 2 -46.01 75.56
REMARK 500 2 PRO C 21 30.00 -78.54
REMARK 500 2 GLN C 22 -70.94 64.48
REMARK 500 2 GLU D 2 -46.03 75.61
REMARK 500 2 PRO D 21 29.78 -78.49
REMARK 500 2 GLN D 22 -71.02 64.67
REMARK 500 2 GLU E 2 -46.04 75.61
REMARK 500 2 PRO E 21 29.89 -78.56
REMARK 500 2 GLN E 22 -71.00 64.53
REMARK 500 3 GLU A 2 -45.93 75.55
REMARK 500 3 PRO A 21 29.77 -78.58
REMARK 500 3 GLN A 22 -70.64 64.50
REMARK 500 3 GLU B 2 -45.96 75.66
REMARK 500 3 PRO B 21 29.78 -78.70
REMARK 500 3 GLN B 22 -70.70 64.61
REMARK 500 3 GLU C 2 -45.87 75.55
REMARK 500 3 PRO C 21 29.54 -78.79
REMARK 500 3 GLN C 22 -70.58 64.66
REMARK 500 3 GLU D 2 -45.91 75.55
REMARK 500 3 PRO D 21 29.68 -78.62
REMARK 500 3 GLN D 22 -70.80 64.65
REMARK 500 3 GLU E 2 -45.89 75.55
REMARK 500 3 PRO E 21 29.58 -78.85
REMARK 500 3 GLN E 22 -70.63 64.67
REMARK 500
REMARK 500 THIS ENTRY HAS 2796 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZLL RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH STRUCTURE DETERMINED THROUGH TRADITIONAL NMR
REMARK 900 PROTOCOLS
DBREF 2HYN A 1 52 UNP P26678 PPLA_HUMAN 1 52
DBREF 2HYN B 1 52 UNP P26678 PPLA_HUMAN 1 52
DBREF 2HYN C 1 52 UNP P26678 PPLA_HUMAN 1 52
DBREF 2HYN D 1 52 UNP P26678 PPLA_HUMAN 1 52
DBREF 2HYN E 1 52 UNP P26678 PPLA_HUMAN 1 52
SEQRES 1 A 52 MET GLU LYS VAL GLN TYR LEU THR ARG SER ALA ILE ARG
SEQRES 2 A 52 ARG ALA SER THR ILE GLU MET PRO GLN GLN ALA ARG GLN
SEQRES 3 A 52 LYS LEU GLN ASN LEU PHE ILE ASN PHE CYS LEU ILE LEU
SEQRES 4 A 52 ILE CYS LEU LEU LEU ILE CYS ILE ILE VAL MET LEU LEU
SEQRES 1 B 52 MET GLU LYS VAL GLN TYR LEU THR ARG SER ALA ILE ARG
SEQRES 2 B 52 ARG ALA SER THR ILE GLU MET PRO GLN GLN ALA ARG GLN
SEQRES 3 B 52 LYS LEU GLN ASN LEU PHE ILE ASN PHE CYS LEU ILE LEU
SEQRES 4 B 52 ILE CYS LEU LEU LEU ILE CYS ILE ILE VAL MET LEU LEU
SEQRES 1 C 52 MET GLU LYS VAL GLN TYR LEU THR ARG SER ALA ILE ARG
SEQRES 2 C 52 ARG ALA SER THR ILE GLU MET PRO GLN GLN ALA ARG GLN
SEQRES 3 C 52 LYS LEU GLN ASN LEU PHE ILE ASN PHE CYS LEU ILE LEU
SEQRES 4 C 52 ILE CYS LEU LEU LEU ILE CYS ILE ILE VAL MET LEU LEU
SEQRES 1 D 52 MET GLU LYS VAL GLN TYR LEU THR ARG SER ALA ILE ARG
SEQRES 2 D 52 ARG ALA SER THR ILE GLU MET PRO GLN GLN ALA ARG GLN
SEQRES 3 D 52 LYS LEU GLN ASN LEU PHE ILE ASN PHE CYS LEU ILE LEU
SEQRES 4 D 52 ILE CYS LEU LEU LEU ILE CYS ILE ILE VAL MET LEU LEU
SEQRES 1 E 52 MET GLU LYS VAL GLN TYR LEU THR ARG SER ALA ILE ARG
SEQRES 2 E 52 ARG ALA SER THR ILE GLU MET PRO GLN GLN ALA ARG GLN
SEQRES 3 E 52 LYS LEU GLN ASN LEU PHE ILE ASN PHE CYS LEU ILE LEU
SEQRES 4 E 52 ILE CYS LEU LEU LEU ILE CYS ILE ILE VAL MET LEU LEU
HELIX 1 1 GLU A 2 ALA A 15 1 14
HELIX 2 2 GLN A 22 LEU A 52 1 31
HELIX 3 3 GLU B 2 ALA B 15 1 14
HELIX 4 4 GLN B 22 LEU B 52 1 31
HELIX 5 5 GLU C 2 ALA C 15 1 14
HELIX 6 6 GLN C 22 LEU C 52 1 31
HELIX 7 7 GLU D 2 ALA D 15 1 14
HELIX 8 8 GLN D 22 LEU D 52 1 31
HELIX 9 9 GLU E 2 ALA E 15 1 14
HELIX 10 10 GLN E 22 LEU E 52 1 31
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 - ar 9 Bytes