Header list of 1qp6.pdb file
Complete list - r 2 2 Bytes
HEADER DE NOVO PROTEIN 01-JUN-99 1QP6
TITLE SOLUTION STRUCTURE OF ALPHA2D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ALPHA2D);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 WAS DESIGNED TO FOLD INTO A HELIX-TURN-HELIX PEPTIDE THAT DIMERIZES
SOURCE 5 TO FORM A FOUR-HELIX BUNDLE.
KEYWDS DE NOVO DESIGN, PROTEIN DESIGN, PROTEIN FOLDING, BISECTING U MOTIF,
KEYWDS 2 FOUR-HELIX BUNDLE, HELIX-TURN-HELIX, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR R.B.HILL,W.F.DEGRADO
REVDAT 3 02-MAR-22 1QP6 1 REMARK
REVDAT 2 24-FEB-09 1QP6 1 VERSN
REVDAT 1 09-JUN-99 1QP6 0
JRNL AUTH R.B.HILL,W.F.DEGRADO
JRNL TITL SOLUTION STRUCTURE OF ALPHA2D, A NATIVELIKE DE NOVO DESIGNED
JRNL TITL 2 PROTEIN
JRNL REF J.AM.CHEM.SOC. V. 120 1138 1998
JRNL REFN ISSN 0002-7863
JRNL DOI 10.1021/JA9733649
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.P.RALEIGH,S.F.BETZ,W.F.DEGRADO
REMARK 1 TITL A DE NOVO DESIGNED PROTEIN MIMICS THE NATIVE STATE OF
REMARK 1 TITL 2 NATURAL PROTEINS
REMARK 1 REF J.AM.CHEM.SOC. V. 117 7558 1995
REMARK 1 REFN ISSN 0002-7863
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:
REMARK 3 STRUCTURE BASED ON 834 RESTRAINTS: 140 LONG-RANGE RESTRAINTS, 30
REMARK 3 PHI ANGLE
REMARK 3 RESTRAINTS, AND 14 CHI-1 ANGLE RESTRAINTS. 83 OF THE LONG-RANGE
REMARK 3 NOES (59%)
REMARK 3 WERE DETERMINED TO ARISE FROM INTER-MONOMER CORRELATIONS BY
REMARK 3 COMPUTATIONAL
REMARK 3 METHODS. THE OTHER NOES WERE TREATED USING A WEIGHTING FUNCTION
REMARK 3 DEVELOPED FOR
REMARK 3 SYMMMETRIC HOMODIMERS THAT ALLOWS EACH NOE TO ARISE FROM EITHER AN
REMARK 3 INTRA- OR
REMARK 3 INTER- MONOMER CORRELATIONS AS DESCRIBED BY NILGES, M. PROTEINS
REMARK 3 (1993) 17:297-
REMARK 3 309. SYMMETRY TERMS WERE EMPLOYED FOR C-ALPHA CARBONS ONLY. SEE
REMARK 3 JACS(1998)120:
REMARK 3 1138-1145 FOR MORE DETAILS.
REMARK 4
REMARK 4 1QP6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000009135.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 7.3
REMARK 210 IONIC STRENGTH : 52 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM ALPHA2D TRIS, PH 7.3, 25 C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING FOR 48 PS AT
REMARK 210 2000K FOLLOWED BY A SLOW COOL TO
REMARK 210 50K
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR TECHNIQUES.
REMARK 210 BECAUSE ALPHA2D
REMARK 210 EXISTS AS A SYMMETRIC HOMODIMER, THERE EXISTS A PROBLEM OF
REMARK 210 DETERMINING WHETHER
REMARK 210 AN OBSERVED NOE ARISES FROM AN INTER- OR INTRA- MONOMER
REMARK 210 CORRELATION. THIS
REMARK 210 PROBLEM WAS DEALT WITH AS DESCRIBED REMARK 3.
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: 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 -97.58 -133.01
REMARK 500 1 PRO A 17 -157.17 -78.60
REMARK 500 1 ARG A 18 -175.06 -53.32
REMARK 500 1 ARG A 19 -49.64 -147.60
REMARK 500 1 LYS A 34 -174.06 52.21
REMARK 500 1 GLU B 2 -97.62 -132.99
REMARK 500 1 PRO B 17 -157.16 -78.69
REMARK 500 1 ARG B 18 -174.97 -53.26
REMARK 500 1 ARG B 19 -49.61 -147.67
REMARK 500 1 LYS B 34 -174.17 52.11
REMARK 500 2 PRO A 17 -154.78 -76.43
REMARK 500 2 ARG A 18 -175.06 -53.74
REMARK 500 2 ARG A 19 -41.55 -149.92
REMARK 500 2 LYS A 34 95.38 53.18
REMARK 500 2 PRO B 17 -154.86 -76.29
REMARK 500 2 ARG B 18 -174.99 -53.65
REMARK 500 2 ARG B 19 -41.60 -150.06
REMARK 500 2 LYS B 34 95.46 53.23
REMARK 500 3 PRO A 17 -157.78 -77.31
REMARK 500 3 ARG A 18 177.15 -49.62
REMARK 500 3 ARG A 19 -39.38 -143.95
REMARK 500 3 LYS A 34 88.99 52.15
REMARK 500 3 PRO B 17 -157.82 -77.21
REMARK 500 3 ARG B 18 177.26 -49.60
REMARK 500 3 ARG B 19 -39.30 -144.05
REMARK 500 3 LYS B 34 88.95 52.12
REMARK 500 4 LYS A 15 74.55 -102.23
REMARK 500 4 PRO A 17 -159.13 -77.08
REMARK 500 4 ARG A 18 171.80 -47.91
REMARK 500 4 ARG A 19 -43.22 -139.06
REMARK 500 4 LYS A 34 74.83 54.12
REMARK 500 4 LYS B 15 74.61 -102.51
REMARK 500 4 PRO B 17 -159.08 -77.07
REMARK 500 4 ARG B 18 171.74 -47.82
REMARK 500 4 ARG B 19 -43.25 -139.11
REMARK 500 4 LYS B 34 74.63 54.42
REMARK 500 5 LYS A 15 76.44 -102.56
REMARK 500 5 PRO A 17 -158.21 -77.19
REMARK 500 5 ARG A 18 174.24 -48.82
REMARK 500 5 ARG A 19 -40.04 -139.43
REMARK 500 5 LYS B 15 76.44 -102.52
REMARK 500 5 PRO B 17 -158.16 -77.24
REMARK 500 5 ARG B 18 174.20 -48.88
REMARK 500 5 ARG B 19 -40.09 -139.41
REMARK 500 6 LYS A 15 61.82 -103.35
REMARK 500 6 PRO A 17 -90.47 -74.40
REMARK 500 6 LYS A 34 87.58 55.11
REMARK 500 6 LYS B 15 62.01 -103.26
REMARK 500 6 PRO B 17 -90.43 -74.36
REMARK 500 6 LYS B 34 87.45 55.08
REMARK 500
REMARK 500 THIS ENTRY HAS 138 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 18 0.10 SIDE CHAIN
REMARK 500 1 ARG A 19 0.31 SIDE CHAIN
REMARK 500 1 ARG B 18 0.10 SIDE CHAIN
REMARK 500 1 ARG B 19 0.31 SIDE CHAIN
REMARK 500 2 ARG A 18 0.24 SIDE CHAIN
REMARK 500 2 ARG A 19 0.31 SIDE CHAIN
REMARK 500 2 ARG B 18 0.24 SIDE CHAIN
REMARK 500 2 ARG B 19 0.31 SIDE CHAIN
REMARK 500 3 ARG A 18 0.27 SIDE CHAIN
REMARK 500 3 ARG A 19 0.31 SIDE CHAIN
REMARK 500 3 ARG B 18 0.27 SIDE CHAIN
REMARK 500 3 ARG B 19 0.31 SIDE CHAIN
REMARK 500 4 ARG A 18 0.17 SIDE CHAIN
REMARK 500 4 ARG A 19 0.32 SIDE CHAIN
REMARK 500 4 ARG B 18 0.17 SIDE CHAIN
REMARK 500 4 ARG B 19 0.32 SIDE CHAIN
REMARK 500 5 ARG A 18 0.26 SIDE CHAIN
REMARK 500 5 ARG A 19 0.30 SIDE CHAIN
REMARK 500 5 ARG B 18 0.26 SIDE CHAIN
REMARK 500 5 ARG B 19 0.30 SIDE CHAIN
REMARK 500 6 ARG A 18 0.23 SIDE CHAIN
REMARK 500 6 ARG A 19 0.30 SIDE CHAIN
REMARK 500 6 ARG B 18 0.23 SIDE CHAIN
REMARK 500 6 ARG B 19 0.30 SIDE CHAIN
REMARK 500 7 ARG A 18 0.25 SIDE CHAIN
REMARK 500 7 ARG A 19 0.15 SIDE CHAIN
REMARK 500 7 ARG B 18 0.25 SIDE CHAIN
REMARK 500 7 ARG B 19 0.15 SIDE CHAIN
REMARK 500 8 ARG A 18 0.24 SIDE CHAIN
REMARK 500 8 ARG A 19 0.30 SIDE CHAIN
REMARK 500 8 ARG B 18 0.24 SIDE CHAIN
REMARK 500 8 ARG B 19 0.30 SIDE CHAIN
REMARK 500 9 ARG A 18 0.26 SIDE CHAIN
REMARK 500 9 ARG A 19 0.26 SIDE CHAIN
REMARK 500 9 ARG B 18 0.26 SIDE CHAIN
REMARK 500 9 ARG B 19 0.26 SIDE CHAIN
REMARK 500 10 ARG A 18 0.26 SIDE CHAIN
REMARK 500 10 ARG A 19 0.30 SIDE CHAIN
REMARK 500 10 ARG B 18 0.26 SIDE CHAIN
REMARK 500 10 ARG B 19 0.30 SIDE CHAIN
REMARK 500 11 ARG A 18 0.19 SIDE CHAIN
REMARK 500 11 ARG A 19 0.22 SIDE CHAIN
REMARK 500 11 ARG B 18 0.19 SIDE CHAIN
REMARK 500 11 ARG B 19 0.22 SIDE CHAIN
REMARK 500 12 ARG A 18 0.32 SIDE CHAIN
REMARK 500 12 ARG A 19 0.22 SIDE CHAIN
REMARK 500 12 ARG B 18 0.32 SIDE CHAIN
REMARK 500 12 ARG B 19 0.22 SIDE CHAIN
REMARK 500 13 ARG A 18 0.14 SIDE CHAIN
REMARK 500 13 ARG A 19 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 64 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QP6 A 1 35 PDB 1QP6 1QP6 1 35
DBREF 1QP6 B 1 35 PDB 1QP6 1QP6 1 35
SEQRES 1 A 35 GLY GLU VAL GLU GLU LEU GLU LYS LYS PHE LYS GLU LEU
SEQRES 2 A 35 TRP LYS GLY PRO ARG ARG GLY GLU ILE GLU GLU LEU HIS
SEQRES 3 A 35 LYS LYS PHE HIS GLU LEU ILE LYS GLY
SEQRES 1 B 35 GLY GLU VAL GLU GLU LEU GLU LYS LYS PHE LYS GLU LEU
SEQRES 2 B 35 TRP LYS GLY PRO ARG ARG GLY GLU ILE GLU GLU LEU HIS
SEQRES 3 B 35 LYS LYS PHE HIS GLU LEU ILE LYS GLY
HELIX 1 1 VAL A 3 LYS A 15 1 13
HELIX 2 2 ARG A 19 LYS A 34 1 16
HELIX 3 3 VAL B 3 LYS B 15 1 13
HELIX 4 4 ARG B 19 LYS B 34 1 16
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 2 2 Bytes