Header list of 1dc2.pdb file
Complete list - b 16 2 Bytes
HEADER GENE REGULATION 04-NOV-99 1DC2
TITLE SOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 4 INHIBITOR A (P16INK4A);
COMPND 3 CHAIN: A;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTG
KEYWDS ANKYRIN REPEAT, HELIX-TURN-HELIX, HELIX BUNDLE, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR I.-J.L.BYEON,J.LI,C.YUAN,M.-D.TSAI
REVDAT 6 16-FEB-22 1DC2 1 REMARK
REVDAT 5 24-FEB-09 1DC2 1 VERSN
REVDAT 4 01-APR-03 1DC2 1 JRNL
REVDAT 3 11-DEC-00 1DC2 1 AUTHOR JRNL
REVDAT 2 18-AUG-00 1DC2 1 AUTHOR JRNL
REVDAT 1 23-DEC-99 1DC2 0
JRNL AUTH C.YUAN,T.L.SELBY,J.LI,I.J.BYEON,M.D.TSAI
JRNL TITL TUMOR SUPPRESSOR INK4: REFINEMENT OF P16INK4A STRUCTURE AND
JRNL TITL 2 DETERMINATION OF P15INK4B STRUCTURE BY COMPARATIVE MODELING
JRNL TITL 3 AND NMR DATA.
JRNL REF PROTEIN SCI. V. 9 1120 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 10892805
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.-J.BYEON,J.LI,K.ERICSON,T.L.SELBY,A.TEVELEV,H.J.KIM,
REMARK 1 AUTH 2 P.O'MAILLE,M.-D.TSAI
REMARK 1 TITL TUMOR SUPPRESSOR P16INK4A: DETERMINATION OF SOLUTION
REMARK 1 TITL 2 STRUCTURE AND ANALYSES OF ITS INTERACTION WITH
REMARK 1 TITL 3 CYCLIN-DEPENDENT KINASE 4
REMARK 1 REF MOL.CELL V. 1 421 1998
REMARK 1 REFN ISSN 1097-2765
REMARK 1 DOI 10.1016/S1097-2765(00)80042-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85, X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1439 RESTRAINTS, 1372 DISTANCE RESTRAINTS, 67 TORSION ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1DC2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009960.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.2-0.4 MM P16INK4A U-15N,13C; 4
REMARK 210 MM HEPES, 1 MM DTT, 5 UM EDTA;
REMARK 210 95% H2O, 5% D2O; 0.2-0.4 MM
REMARK 210 P16INK4A U-15N; 4 MM HEPES, 1 MM
REMARK 210 DTT, 5 UM EDTA; 95% H2O, 5% D2O;
REMARK 210 0.2-0.4 MM P16INK4A; 4 MM HEPES,
REMARK 210 1 MM DTT, 5 UM EDTA; 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 4D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, FELIX 95
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE CLOSEST TO MEAN STRUCTURE
REMARK 210 WHICH SHOWS GOOD AGREEMENT WITH
REMARK 210 THE EXPERIMENTAL RESTRAINTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 VAL A 28 H LEU A 32 1.54
REMARK 500 O HIS A 123 H ALA A 127 1.54
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 ALA A 5 -44.64 -145.26
REMARK 500 1 ASP A 14 20.14 -157.65
REMARK 500 1 ARG A 22 30.35 -90.79
REMARK 500 1 ARG A 47 -172.65 43.52
REMARK 500 1 MET A 52 35.08 -96.96
REMARK 500 1 MET A 53 -6.26 64.55
REMARK 500 1 MET A 54 26.79 44.53
REMARK 500 1 ALA A 68 -150.97 -80.02
REMARK 500 1 CYS A 72 155.52 -43.69
REMARK 500 1 ALA A 73 -142.26 -152.07
REMARK 500 1 THR A 77 10.18 -140.24
REMARK 500 1 LEU A 104 61.81 -68.95
REMARK 500 1 ASP A 105 29.15 -167.44
REMARK 500 1 VAL A 106 -169.86 -100.65
REMARK 500 1 ALA A 109 -83.62 52.96
REMARK 500 1 ARG A 112 -68.82 68.41
REMARK 500 1 LEU A 121 -81.03 -56.67
REMARK 500 1 THR A 137 34.52 35.56
REMARK 500 1 SER A 140 24.33 -164.61
REMARK 500 1 HIS A 142 -66.90 -123.22
REMARK 500 1 ILE A 145 67.41 -176.26
REMARK 500 1 ASP A 146 -175.68 50.39
REMARK 500 1 ALA A 147 97.49 -60.04
REMARK 500 1 ALA A 148 -179.37 -51.30
REMARK 500 2 SER A 7 -170.06 57.16
REMARK 500 2 SER A 8 41.73 -90.77
REMARK 500 2 SER A 12 -76.59 -85.56
REMARK 500 2 ALA A 13 91.63 61.81
REMARK 500 2 SER A 43 40.24 -90.53
REMARK 500 2 ARG A 47 -179.33 -60.07
REMARK 500 2 ILE A 49 -61.35 63.40
REMARK 500 2 MET A 53 -17.62 -48.83
REMARK 500 2 SER A 56 102.41 -161.20
REMARK 500 2 ALA A 68 -151.88 -68.43
REMARK 500 2 CYS A 72 154.85 -48.41
REMARK 500 2 ALA A 73 -157.52 -151.52
REMARK 500 2 THR A 79 92.13 -61.82
REMARK 500 2 ALA A 100 -106.31 -124.20
REMARK 500 2 LEU A 104 54.64 -100.45
REMARK 500 2 ASP A 105 54.02 -165.38
REMARK 500 2 ALA A 109 -83.37 55.57
REMARK 500 2 ARG A 112 149.84 -178.73
REMARK 500 2 LEU A 121 -94.22 -81.27
REMARK 500 2 HIS A 123 49.90 -88.08
REMARK 500 2 ALA A 134 45.22 -103.60
REMARK 500 2 ARG A 138 -157.95 -173.30
REMARK 500 2 SER A 140 -138.69 -173.65
REMARK 500 2 ALA A 148 168.80 59.13
REMARK 500 2 ASP A 153 106.06 54.28
REMARK 500 2 ILE A 154 77.69 -116.03
REMARK 500
REMARK 500 THIS ENTRY HAS 497 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 22 0.28 SIDE CHAIN
REMARK 500 1 ARG A 24 0.08 SIDE CHAIN
REMARK 500 1 ARG A 29 0.16 SIDE CHAIN
REMARK 500 1 ARG A 46 0.30 SIDE CHAIN
REMARK 500 1 ARG A 47 0.31 SIDE CHAIN
REMARK 500 1 ARG A 58 0.15 SIDE CHAIN
REMARK 500 1 ARG A 80 0.20 SIDE CHAIN
REMARK 500 1 ARG A 87 0.29 SIDE CHAIN
REMARK 500 1 ARG A 99 0.26 SIDE CHAIN
REMARK 500 1 ARG A 103 0.29 SIDE CHAIN
REMARK 500 1 ARG A 124 0.14 SIDE CHAIN
REMARK 500 1 ARG A 128 0.30 SIDE CHAIN
REMARK 500 1 ARG A 131 0.25 SIDE CHAIN
REMARK 500 1 ARG A 138 0.15 SIDE CHAIN
REMARK 500 1 ARG A 144 0.20 SIDE CHAIN
REMARK 500 2 ARG A 24 0.32 SIDE CHAIN
REMARK 500 2 ARG A 29 0.12 SIDE CHAIN
REMARK 500 2 ARG A 46 0.28 SIDE CHAIN
REMARK 500 2 ARG A 47 0.30 SIDE CHAIN
REMARK 500 2 ARG A 58 0.31 SIDE CHAIN
REMARK 500 2 ARG A 80 0.31 SIDE CHAIN
REMARK 500 2 ARG A 87 0.30 SIDE CHAIN
REMARK 500 2 ARG A 99 0.32 SIDE CHAIN
REMARK 500 2 ARG A 103 0.27 SIDE CHAIN
REMARK 500 2 ARG A 107 0.30 SIDE CHAIN
REMARK 500 2 ARG A 112 0.21 SIDE CHAIN
REMARK 500 2 ARG A 124 0.21 SIDE CHAIN
REMARK 500 2 ARG A 128 0.31 SIDE CHAIN
REMARK 500 2 ARG A 131 0.20 SIDE CHAIN
REMARK 500 2 ARG A 144 0.21 SIDE CHAIN
REMARK 500 3 ARG A 22 0.31 SIDE CHAIN
REMARK 500 3 ARG A 24 0.21 SIDE CHAIN
REMARK 500 3 ARG A 29 0.31 SIDE CHAIN
REMARK 500 3 ARG A 46 0.32 SIDE CHAIN
REMARK 500 3 ARG A 47 0.22 SIDE CHAIN
REMARK 500 3 ARG A 58 0.13 SIDE CHAIN
REMARK 500 3 ARG A 80 0.17 SIDE CHAIN
REMARK 500 3 ARG A 87 0.31 SIDE CHAIN
REMARK 500 3 ARG A 99 0.31 SIDE CHAIN
REMARK 500 3 ARG A 103 0.29 SIDE CHAIN
REMARK 500 3 ARG A 107 0.22 SIDE CHAIN
REMARK 500 3 ARG A 112 0.22 SIDE CHAIN
REMARK 500 3 ARG A 124 0.32 SIDE CHAIN
REMARK 500 3 ARG A 128 0.20 SIDE CHAIN
REMARK 500 3 ARG A 131 0.12 SIDE CHAIN
REMARK 500 3 ARG A 138 0.31 SIDE CHAIN
REMARK 500 3 ARG A 144 0.25 SIDE CHAIN
REMARK 500 4 ARG A 22 0.29 SIDE CHAIN
REMARK 500 4 ARG A 24 0.28 SIDE CHAIN
REMARK 500 4 ARG A 29 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 324 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A5E RELATED DB: PDB
REMARK 900 1A5E CONTAINS THE SAME PROTEIN STRUCTURES WITH LESS EXPERIMENTAL
REMARK 900 CONSTRAINTS
DBREF 1DC2 A 1 156 UNP P42771 CDN2A_HUMAN 1 156
SEQRES 1 A 156 MET GLU PRO ALA ALA GLY SER SER MET GLU PRO SER ALA
SEQRES 2 A 156 ASP TRP LEU ALA THR ALA ALA ALA ARG GLY ARG VAL GLU
SEQRES 3 A 156 GLU VAL ARG ALA LEU LEU GLU ALA GLY ALA LEU PRO ASN
SEQRES 4 A 156 ALA PRO ASN SER TYR GLY ARG ARG PRO ILE GLN VAL MET
SEQRES 5 A 156 MET MET GLY SER ALA ARG VAL ALA GLU LEU LEU LEU LEU
SEQRES 6 A 156 HIS GLY ALA GLU PRO ASN CYS ALA ASP PRO ALA THR LEU
SEQRES 7 A 156 THR ARG PRO VAL HIS ASP ALA ALA ARG GLU GLY PHE LEU
SEQRES 8 A 156 ASP THR LEU VAL VAL LEU HIS ARG ALA GLY ALA ARG LEU
SEQRES 9 A 156 ASP VAL ARG ASP ALA TRP GLY ARG LEU PRO VAL ASP LEU
SEQRES 10 A 156 ALA GLU GLU LEU GLY HIS ARG ASP VAL ALA ARG TYR LEU
SEQRES 11 A 156 ARG ALA ALA ALA GLY GLY THR ARG GLY SER ASN HIS ALA
SEQRES 12 A 156 ARG ILE ASP ALA ALA GLU GLY PRO SER ASP ILE PRO ASP
HELIX 1 1 ASP A 14 ARG A 22 1 9
HELIX 2 2 ARG A 24 GLY A 35 1 12
HELIX 3 3 SER A 56 GLY A 67 1 12
HELIX 4 4 ARG A 80 GLY A 89 1 10
HELIX 5 5 PHE A 90 ALA A 100 1 11
HELIX 6 6 LEU A 113 GLY A 122 1 10
HELIX 7 7 HIS A 123 GLY A 135 1 13
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 - b 16 2 Bytes