Header list of 1a5e.pdb file
Complete list - b 16 2 Bytes
HEADER ANTI-ONCOGENE 13-FEB-98 1A5E
TITLE SOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, 18 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR SUPPRESSOR P16INK4A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: TUMOR SUPPRESSOR P16INK4A
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)
KEYWDS CELL CYCLE, ANTI-ONCOGENE, ANK REPEAT
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR I.-J.L.BYEON,J.LI,K.ERICSON,T.L.SELBY,A.TEVELEV,H.-J.KIM,P.O'MAILLE,
AUTHOR 2 M.-D.TSAI
REVDAT 5 16-FEB-22 1A5E 1 REMARK
REVDAT 4 19-MAY-09 1A5E 1 REMARK
REVDAT 3 24-FEB-09 1A5E 1 VERSN
REVDAT 2 01-APR-03 1A5E 1 JRNL
REVDAT 1 13-AUG-99 1A5E 0
JRNL AUTH I.J.BYEON,J.LI,K.ERICSON,T.L.SELBY,A.TEVELEV,H.J.KIM,
JRNL AUTH 2 P.O'MAILLE,M.D.TSAI
JRNL TITL TUMOR SUPPRESSOR P16INK4A: DETERMINATION OF SOLUTION
JRNL TITL 2 STRUCTURE AND ANALYSES OF ITS INTERACTION WITH
JRNL TITL 3 CYCLIN-DEPENDENT KINASE 4.
JRNL REF MOL.CELL V. 1 421 1998
JRNL REFN ISSN 1097-2765
JRNL PMID 9660926
JRNL 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 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE 18 STRUCTURES WERE SUPERIMPOSED IN
REMARK 3 ORDER TO HAVE BEST FITTING FOR THE BACKBONE ATOMS (N, CA, C) OF
REMARK 3 RESIDUES 14-134. THE EXPERIMENTAL RESTRAINTS ARE PRESENTED IN
REMARK 3 ENTRY 1INK.MR. RESIDUES 1-13 AND 135-156 ARE POORLY DEFINED BY
REMARK 3 THE EXPERIMENTAL DATA. THUS, NO MEANING SHOULD BE GIVEN TO THOSE
REMARK 3 RESIDUES' COORDINATES.
REMARK 4
REMARK 4 1A5E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170413.
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 : CA. 0
REMARK 210 PRESSURE : NO
REMARK 210 SAMPLE CONTENTS : H2O AND D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NMR EXPERIMENTS FOR THE
REMARK 210 ASSIGNMENTS AND STRUCTURE
REMARK 210 CALCULATIONS : HNCACB; CBCA(CO)
REMARK 210 HN; HN(CO)CA; HCCH-TOCSY; HNHA;
REMARK 210 3D 15N-EDITED NOESY AND TOCSY;
REMARK 210 2D NOESY AND TOCSY; 3D 13C-
REMARK 210 EDITED NOESY; 3D 15N/13C
REMARK 210 SIMULTANEOUSLY EDITED NOESY; 4D
REMARK 210 15N/13C-EDITED NOESY; 4D 13C/13C-
REMARK 210 EDITED NOESY.
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 90
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : CLOSEST TO MEAN STRUCTURE WHICH
REMARK 210 SHOWS GOOD AGREEMENT WITH THE
REMARK 210 CONSTRAINTS. NONE OF THE
REMARK 210 CONSTRAINTS SHOW NOE VIOLATION
REMARK 210 BIGGER THAN 0.5 A AND DIHEDRAL
REMARK 210 ANGLE VIOLATION BIGGER THAN 5
REMARK 210 DEGREE.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE SOLUTION STRUCTURE OF THE TUMOR SUPPRESSOR P16INK4A
REMARK 210 HAS BEEN DETERMINED BY MULTI-DIMENSIONAL HERERONUCLEAR NMR. THE
REMARK 210 STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING
REMARK 210 PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING
REMARK 210 THE PROGRAM X-PLOR 3.1 (BRUNGER). THE CALCULATION IS BASED ON
REMARK 210 1437 EXPERIMENTAL NMR RESTRAINTS (1370 DISTANCE AND 67 TORSION
REMARK 210 ANGLE RESTRAINTS).
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 GLU A 61 H LEU A 65 1.54
REMARK 500 O ALA A 60 H LEU A 64 1.56
REMARK 500 O LEU A 130 H ALA A 134 1.60
REMARK 500 O HIS A 83 H ARG A 87 1.60
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 10 72.77 59.52
REMARK 500 1 ALA A 13 -62.84 -155.75
REMARK 500 1 ARG A 46 -161.09 -114.18
REMARK 500 1 SER A 56 81.24 -161.39
REMARK 500 1 ALA A 68 -156.57 -78.05
REMARK 500 1 GLU A 69 64.42 -114.92
REMARK 500 1 CYS A 72 150.27 -48.32
REMARK 500 1 ALA A 73 -139.49 -136.54
REMARK 500 1 LEU A 78 23.25 46.92
REMARK 500 1 THR A 79 94.16 -61.54
REMARK 500 1 ALA A 102 108.86 -160.41
REMARK 500 1 TRP A 110 -79.71 -59.57
REMARK 500 1 ARG A 112 -165.04 -107.42
REMARK 500 1 LEU A 121 -81.89 -57.07
REMARK 500 1 ALA A 134 54.57 -97.42
REMARK 500 1 ARG A 138 63.55 -151.77
REMARK 500 1 HIS A 142 -161.71 -117.37
REMARK 500 1 ALA A 143 115.36 -176.88
REMARK 500 1 ARG A 144 -175.28 -56.05
REMARK 500 1 ASP A 146 98.48 -44.98
REMARK 500 1 ASP A 153 137.31 65.29
REMARK 500 2 ALA A 4 92.30 49.35
REMARK 500 2 SER A 7 175.16 -55.47
REMARK 500 2 MET A 9 174.86 65.72
REMARK 500 2 GLU A 10 72.28 58.78
REMARK 500 2 ALA A 13 -37.72 -179.97
REMARK 500 2 ARG A 22 32.25 -90.99
REMARK 500 2 MET A 53 96.60 -61.10
REMARK 500 2 LEU A 62 -70.95 -49.62
REMARK 500 2 ALA A 68 -158.81 -76.05
REMARK 500 2 GLU A 69 74.63 -114.55
REMARK 500 2 ASN A 71 -60.92 -139.53
REMARK 500 2 CYS A 72 152.81 -45.43
REMARK 500 2 LEU A 78 21.73 47.76
REMARK 500 2 THR A 79 102.81 -59.08
REMARK 500 2 ALA A 100 70.83 -118.98
REMARK 500 2 ASP A 105 56.65 -101.68
REMARK 500 2 VAL A 106 -164.21 -114.99
REMARK 500 2 ASP A 108 63.75 -68.73
REMARK 500 2 ALA A 109 -77.17 57.06
REMARK 500 2 TRP A 110 -70.70 -45.94
REMARK 500 2 LEU A 121 -92.72 -59.77
REMARK 500 2 SER A 140 39.13 -162.41
REMARK 500 2 HIS A 142 74.72 -108.85
REMARK 500 2 ALA A 143 -43.96 -135.86
REMARK 500 2 ILE A 145 67.74 -177.52
REMARK 500 2 ALA A 147 93.48 55.08
REMARK 500 2 SER A 152 -157.12 -79.24
REMARK 500 2 ILE A 154 93.83 -178.90
REMARK 500 3 ALA A 5 72.40 47.73
REMARK 500
REMARK 500 THIS ENTRY HAS 464 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 29 0.27 SIDE CHAIN
REMARK 500 1 ARG A 46 0.24 SIDE CHAIN
REMARK 500 1 ARG A 47 0.26 SIDE CHAIN
REMARK 500 1 ARG A 58 0.26 SIDE CHAIN
REMARK 500 1 ARG A 80 0.14 SIDE CHAIN
REMARK 500 1 ARG A 87 0.26 SIDE CHAIN
REMARK 500 1 ARG A 99 0.32 SIDE CHAIN
REMARK 500 1 ARG A 103 0.31 SIDE CHAIN
REMARK 500 1 ARG A 107 0.27 SIDE CHAIN
REMARK 500 1 ARG A 112 0.31 SIDE CHAIN
REMARK 500 1 ARG A 124 0.31 SIDE CHAIN
REMARK 500 1 ARG A 128 0.23 SIDE CHAIN
REMARK 500 1 ARG A 131 0.26 SIDE CHAIN
REMARK 500 1 ARG A 138 0.14 SIDE CHAIN
REMARK 500 1 ARG A 144 0.32 SIDE CHAIN
REMARK 500 2 ARG A 22 0.18 SIDE CHAIN
REMARK 500 2 ARG A 24 0.31 SIDE CHAIN
REMARK 500 2 ARG A 29 0.23 SIDE CHAIN
REMARK 500 2 ARG A 46 0.24 SIDE CHAIN
REMARK 500 2 ARG A 47 0.26 SIDE CHAIN
REMARK 500 2 ARG A 58 0.32 SIDE CHAIN
REMARK 500 2 ARG A 80 0.31 SIDE CHAIN
REMARK 500 2 ARG A 87 0.31 SIDE CHAIN
REMARK 500 2 ARG A 99 0.31 SIDE CHAIN
REMARK 500 2 ARG A 103 0.30 SIDE CHAIN
REMARK 500 2 ARG A 107 0.26 SIDE CHAIN
REMARK 500 2 ARG A 112 0.23 SIDE CHAIN
REMARK 500 2 ARG A 124 0.29 SIDE CHAIN
REMARK 500 2 ARG A 128 0.32 SIDE CHAIN
REMARK 500 2 ARG A 138 0.18 SIDE CHAIN
REMARK 500 2 ARG A 144 0.29 SIDE CHAIN
REMARK 500 3 ARG A 22 0.29 SIDE CHAIN
REMARK 500 3 ARG A 24 0.29 SIDE CHAIN
REMARK 500 3 ARG A 29 0.27 SIDE CHAIN
REMARK 500 3 ARG A 46 0.23 SIDE CHAIN
REMARK 500 3 ARG A 47 0.18 SIDE CHAIN
REMARK 500 3 ARG A 58 0.29 SIDE CHAIN
REMARK 500 3 ARG A 80 0.08 SIDE CHAIN
REMARK 500 3 ARG A 87 0.18 SIDE CHAIN
REMARK 500 3 ARG A 99 0.20 SIDE CHAIN
REMARK 500 3 ARG A 103 0.30 SIDE CHAIN
REMARK 500 3 ARG A 107 0.31 SIDE CHAIN
REMARK 500 3 ARG A 112 0.29 SIDE CHAIN
REMARK 500 3 ARG A 124 0.24 SIDE CHAIN
REMARK 500 3 ARG A 128 0.23 SIDE CHAIN
REMARK 500 3 ARG A 131 0.18 SIDE CHAIN
REMARK 500 3 ARG A 138 0.30 SIDE CHAIN
REMARK 500 3 ARG A 144 0.28 SIDE CHAIN
REMARK 500 4 ARG A 22 0.32 SIDE CHAIN
REMARK 500 4 ARG A 29 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 292 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A5E 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 IA ASP A 14 ARG A 22 1 9
HELIX 2 IB VAL A 25 GLY A 35 1 11
HELIX 3 IIA ARG A 47 VAL A 51 1 5
HELIX 4 IIB ALA A 57 HIS A 66 1 10
HELIX 5 3A PRO A 81 GLU A 88 1 8
HELIX 6 3B LEU A 91 ALA A 100 1 10
HELIX 7 IVA PRO A 114 LEU A 121 1 8
HELIX 8 IVB ARG A 124 ALA A 134 1 11
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