Header list of 1qnd.pdb file
Complete list - r 25 2 Bytes
HEADER TRANSFER PROTEIN 14-OCT-99 1QND
TITLE STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NONSPECIFIC LIPID-TRANSFER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SCP-2, NSL-TP, STEROL CARRIER PROTEIN 2;
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 ORGAN: LIVER;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASMIC;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T/HSCP2
KEYWDS TRANSFER PROTEIN, STEROL CARRIER PROTEIN 2, PROTEIN STRUCTURE,
KEYWDS 2 PROTEIN DYNAMICS, NITROXIDE SPIN LABELS, LIPID BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.LOPEZ-GARCIA,T.SZYPERSKI,J.H.DYER,T.CHOINOWSKI,U.SEEDORF,H.HAUSER,
AUTHOR 2 K.WUTHRICH
REVDAT 5 24-AUG-11 1QND 1 REMARK ATOM VERSN
REVDAT 4 24-FEB-09 1QND 1 VERSN
REVDAT 3 28-FEB-02 1QND 1 AUTHOR REMARK
REVDAT 2 07-AUG-00 1QND 1 SHEET
REVDAT 1 03-JUL-00 1QND 0
JRNL AUTH F.LOPEZ-GARCIA,T.SZYPERSKI,J.H.DYER,T.CHOINOWSKI,U.SEEDORF,
JRNL AUTH 2 H.HAUSER,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE STEROL CARRIER PROTEIN-2: IMPLICATIONS
JRNL TITL 2 FOR THE BIOLOGICAL ROLE
JRNL REF J.MOL.BIOL. V. 295 595 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10623549
JRNL DOI 10.1006/JMBI.1999.3355
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.SZYPERSKI,S.SCHEEK,J.JOHANSSON,G.ASSMANN,U.SEEDORF,
REMARK 1 AUTH 2 K.WUTHRICH
REMARK 1 TITL NMR DETERMINATION OF THE SECONDARY STRUCTURE AND
REMARK 1 TITL 2 THREE-DIMENSIONAL POLYPEPTIDE BACKBONE FOLD OF THE HUMAN
REMARK 1 TITL 3 STEROL CARRIER PROTEIN 2
REMARK 1 REF FEBS LETT. V. 335 18 1993
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 8243660
REMARK 1 DOI 10.1016/0014-5793(93)80431-S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL VERSION 2.6
REMARK 3 AUTHORS : LUGINBUHL, GUNTERT, BILLETER, WUTHRICH
REMARK 3 STRUCTURAL STATISTICS: ATOMIC RMS DIFFERENCES
REMARK 3 BACKBONE(N, CA, C', RESIDUES 8-116) 1.00 A
REMARK 3 BACKBONE(N, CA, C', RESIDUES 8-84) 0.47 A
REMARK 3 BACKBONE(N, CA, C', RESIDUES 85-116) 1.41 A
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL ARTICLE. TORSION ANGLE DYNAMICS CALCULATIONS WERE
REMARK 3 PERFORMED WITH THE PROGRAM DYANA (P.GUNTERT, C.MUMENTHALER,
REMARK 3 K.WUTHRICH, J.MOL.BIOL. (1997) VOL. 273, 283-298 FOR THE
REMARK 3 RESTRAINED ENERGY REFINEMENT. THE PROGRAM OPAL (P. LUGINBHUL,
REMARK 3 P. GUNTERT, M. BILLETER, K. WUTHRICH J. BIOMOL. NMR (1996),
REMARK 3 VOL.8, 136-146) WAS USED. THE AVERAGE OF THE RMSD VALUES IN A
REMARK 3 PAIRWISE COMPARISON OF THE 20 NMR CONFORMERS TO THE MEAN
REMARK 3 STRUCTURE AS DESCRIBED IN THE PAPER CITED ON *JRNL* RECORDS
REMARK 3 ABOVE IS 1.0 ANGSTROM FOR THE BACKBONE ATOMS OF RESIDUES 8-
REMARK 3 116. THE AVERAGE OF THE RMSD VALUES IN A PAIRWISE COMPARISON
REMARK 3 TO THE MEAN STRUCTURE FOR RESIDUES 8-84, THUS INCLUDING THE
REMARK 3 BEST DEFINED FRAGMENT, IS 0.47 ANGSTROMS. THE AVERAGE OF THE
REMARK 3 RMSD VALUES IN A PAIRWISE COMPARISON TO THE MEAN STRUCTURE FOR
REMARK 3 RESIDUES 85-116, THUS INCLUDING THE WORSE DEFINED RESIDUES IS
REMARK 3 1.41 ANGSTROMS.
REMARK 4
REMARK 4 1QND COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-99.
REMARK 100 THE PDBE ID CODE IS EBI-4082.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : SEE PAPER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PAPER
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY+
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THREE-DIMENSIONAL STRUCTURE IN AQUEOUS SOLUTION
REMARK 210 REPRESENTED BY 20 CONFORMERS DETERMINED BY NUCLEAR
REMARK 210 MAGNETIC RESONANCE, TORSION ANGLE DYNAMICS AND RESTRAINED
REMARK 210 ENERGY REFINEMENT. DATA WERE COLLECTED AT 28 DEGREES CELSIUS
REMARK 210 AND AT PH 6.0. THEY CONSIST OF 1005 UPPER LIMITS ON DISTANCES
REMARK 210 OBTAINED FROM NOE MEASUREMENTS AND 584 ANGLE CONSTRAINTS
REMARK 210 OBTAINED FROM NOE MEASUREMENTS AND COUPLING CONSTANT
REMARK 210 MEASUREMENTS. THESE INPUT DATA ARE ALSO AVAILABLE FROM THE
REMARK 210 PROTEIN DATA BANK. SEE JNRK ARTICLE FOR DETAILS
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 400
REMARK 400 COMPOUND
REMARK 400 DEPOSITED COORDINATES ARE THOSE OF CONFORMERS 1 - 20 IN THE
REMARK 400 PAPER CITED ON *JRNL* RECORDS ABOVE. NO VIOLATIONS OF
REMARK 400 DISTANCE CONSTRAINTS FROM NOES EXCEED 0.11 ANGSTROMS, AND
REMARK 400 NO VIOLATIONS OF ANGLE CONSTRAINTS EXCEED 4.5 DEGREES.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 5 PHE A 27 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 6 PHE A 7 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 10 ASP A 5 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
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 SER A 4 -82.59 -95.20
REMARK 500 1 GLU A 23 58.19 -161.97
REMARK 500 1 PRO A 43 78.10 -66.95
REMARK 500 1 LYS A 46 -176.46 -61.13
REMARK 500 1 LYS A 55 -50.16 -137.07
REMARK 500 1 SER A 60 147.63 -171.14
REMARK 500 1 MET A 75 -101.22 -139.88
REMARK 500 1 ALA A 76 159.06 174.08
REMARK 500 1 ASN A 89 99.40 -36.89
REMARK 500 1 GLN A 91 71.12 -166.64
REMARK 500 1 ALA A 93 -87.88 -51.93
REMARK 500 1 PHE A 94 -135.14 33.89
REMARK 500 1 ASN A 104 -172.34 174.88
REMARK 500 1 MET A 105 -166.79 -65.69
REMARK 500 1 ALA A 108 -73.65 -73.58
REMARK 500 1 MET A 109 48.21 -159.19
REMARK 500 1 LEU A 111 -164.92 -165.06
REMARK 500 1 GLN A 115 44.74 -150.13
REMARK 500 1 LEU A 116 159.72 50.22
REMARK 500 2 SER A 2 112.84 -165.89
REMARK 500 2 ALA A 3 49.38 -166.84
REMARK 500 2 GLU A 23 55.16 -154.76
REMARK 500 2 PRO A 43 86.61 -68.01
REMARK 500 2 VAL A 54 50.13 -144.50
REMARK 500 2 LYS A 55 -40.50 -157.01
REMARK 500 2 SER A 60 144.60 -171.28
REMARK 500 2 LYS A 68 -169.91 -74.61
REMARK 500 2 MET A 75 -50.01 -153.59
REMARK 500 2 ALA A 76 161.41 97.08
REMARK 500 2 LEU A 83 -72.54 -70.68
REMARK 500 2 THR A 85 -17.45 -155.76
REMARK 500 2 MET A 88 98.77 66.24
REMARK 500 2 PRO A 90 77.12 -68.77
REMARK 500 2 LEU A 99 84.79 54.49
REMARK 500 2 ASN A 104 -95.31 -164.53
REMARK 500 2 MET A 105 -105.48 -150.95
REMARK 500 2 LYS A 110 42.54 -76.11
REMARK 500 2 GLN A 112 -80.77 -35.53
REMARK 500 2 LEU A 116 156.53 46.68
REMARK 500 2 ASN A 120 88.15 60.08
REMARK 500 2 LYS A 122 108.19 -162.30
REMARK 500 3 ALA A 3 57.39 34.44
REMARK 500 3 SER A 4 -156.65 -143.36
REMARK 500 3 ASP A 5 22.44 45.34
REMARK 500 3 GLU A 23 64.70 -165.35
REMARK 500 3 ASP A 41 60.02 60.24
REMARK 500 3 LYS A 46 -175.13 -65.84
REMARK 500 3 LYS A 55 -54.50 -129.25
REMARK 500 3 ASN A 64 29.37 45.39
REMARK 500 3 LYS A 68 -176.97 -63.16
REMARK 500
REMARK 500 THIS ENTRY HAS 416 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 48 THR A 49 1 147.23
REMARK 500 MET A 75 ALA A 76 3 -146.30
REMARK 500 ALA A 121 LYS A 122 5 145.57
REMARK 500 GLY A 33 ILE A 34 8 144.91
REMARK 500 LYS A 40 ASP A 41 10 148.82
REMARK 500 ALA A 48 THR A 49 10 147.65
REMARK 500 ALA A 69 ASP A 70 11 148.55
REMARK 500 LYS A 122 LEU A 123 12 146.73
REMARK 500 GLY A 33 ILE A 34 16 149.07
REMARK 500 MET A 88 ASN A 89 16 -136.37
REMARK 500 SER A 4 ASP A 5 17 129.43
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 PHE A 37 0.08 SIDE CHAIN
REMARK 500 2 TRP A 50 0.11 SIDE CHAIN
REMARK 500 5 PHE A 27 0.08 SIDE CHAIN
REMARK 500 9 PHE A 7 0.08 SIDE CHAIN
REMARK 500 9 TRP A 50 0.10 SIDE CHAIN
REMARK 500 16 PHE A 37 0.09 SIDE CHAIN
REMARK 500 16 TRP A 50 0.08 SIDE CHAIN
REMARK 500 20 PHE A 80 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4438 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS
DBREF 1QND A 1 123 UNP P22307 NLTP_HUMAN 425 547
SEQRES 1 A 123 SER SER ALA SER ASP GLY PHE LYS ALA ASN LEU VAL PHE
SEQRES 2 A 123 LYS GLU ILE GLU LYS LYS LEU GLU GLU GLU GLY GLU GLN
SEQRES 3 A 123 PHE VAL LYS LYS ILE GLY GLY ILE PHE ALA PHE LYS VAL
SEQRES 4 A 123 LYS ASP GLY PRO GLY GLY LYS GLU ALA THR TRP VAL VAL
SEQRES 5 A 123 ASP VAL LYS ASN GLY LYS GLY SER VAL LEU PRO ASN SER
SEQRES 6 A 123 ASP LYS LYS ALA ASP CYS THR ILE THR MET ALA ASP SER
SEQRES 7 A 123 ASP PHE LEU ALA LEU MET THR GLY LYS MET ASN PRO GLN
SEQRES 8 A 123 SER ALA PHE PHE GLN GLY LYS LEU LYS ILE THR GLY ASN
SEQRES 9 A 123 MET GLY LEU ALA MET LYS LEU GLN ASN LEU GLN LEU GLN
SEQRES 10 A 123 PRO GLY ASN ALA LYS LEU
HELIX 1 A LYS A 8 GLU A 22 1 15
HELIX 2 B GLY A 24 ILE A 31 1 8
HELIX 3 C ASP A 77 MET A 84 1 8
HELIX 4 D GLN A 112 GLN A 115 5 4
SHEET 1 A 4 CYS A 71 MET A 75 0
SHEET 2 A 4 GLY A 33 LYS A 40 1 N ALA A 36 O CYS A 71
SHEET 3 A 4 GLU A 47 VAL A 54 -1 N TRP A 50 O PHE A 37
SHEET 4 A 4 SER A 60 LEU A 62 -1 N SER A 60 O ASP A 53
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 - r 25 2 Bytes