Header list of 3sak.pdb file
Complete list - v 3 2 Bytes
HEADER APOPTOSIS/CELL CYCLE/GENE REGULATION 30-APR-99 3SAK
TITLE HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN
TITLE 2 OF P53 BY MULTI-DIMENSIONAL NMR (SAC STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TUMOR SUPPRESSOR P53);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: OLIGOMERIZATION DOMAIN, RESIDUES 319 - 360
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ANTI-ONCOGENE, P53 DOMAIN, APOPTOSIS-CELL CYCLE-GENE REGULATION
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR G.M.CLORE
REVDAT 5 03-NOV-21 3SAK 1 REMARK
REVDAT 4 24-FEB-09 3SAK 1 VERSN
REVDAT 3 27-SEP-00 3SAK 1 HEADER DBREF
REVDAT 2 30-JUN-99 3SAK 1 HEADER
REVDAT 1 25-JUN-99 3SAK 0
JRNL AUTH J.KUSZEWSKI,A.M.GRONENBORN,G.M.CLORE
JRNL TITL IMPROVING THE PACKING AND ACCURACY OF NMR STRUCTURE WITH A
JRNL TITL 2 PSEUDOPOTENTIAL FOR THE RADIUS OF GYRATION
JRNL REF J.AM.CHEM.SOC. V. 121 2337 1999
JRNL REFN ISSN 0002-7863
JRNL DOI 10.1021/JA9843730
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.M.CLORE,J.ERNST,R.CLUBB,J.G.OMICHINSKI,
REMARK 1 AUTH 2 W.M.POINDEXTER KENNEDY,K.SAKAGUCHI,E.APPELLA,A.M.GRONENBORN
REMARK 1 TITL REFINED SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF
REMARK 1 TITL 2 THE TUMOUR SUPPRESSOR P53
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 321 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.M.CLORE,J.G.OMICHINSKI,K.SAKAGUCHI,N.ZAMBRANO,H.SAKAMOTO,
REMARK 1 AUTH 2 E.APPELLA,A.M.GRONENBORN
REMARK 1 TITL INTERHELICAL ANGLES IN THE SOLUTION STRUCTURE OF THE
REMARK 1 TITL 2 OLIGOMERIZATION DOMAIN OF P53: CORRECTION
REMARK 1 REF SCIENCE V. 267 1515 1995
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.M.CLORE,J.G.OMICHINSKI,K.SAKAGUCHI,N.ZAMBRANO,H.SAKAMOTO,
REMARK 1 AUTH 2 E.APPELLA,A.M.GRONENBORN
REMARK 1 TITL HIGH-RESOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF
REMARK 1 TITL 2 P53 BY MULTIDIMENSIONAL NMR
REMARK 1 REF SCIENCE V. 265 386 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR/CNS
REMARK 3 AUTHORS : BRUNGER, A., CLORE, G.M. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 TERMS IN THE TARGET FUNCTION USED FOR SIMULATED ANNEALING
REMARK 3 NOE (SUM AVERAGING) AND TORSION ANGLE RESTRAINTS
REMARK 3 3JHNALPHA COUPLING CONSTANT RESTRAINTS (GARRETT ET AL
REMARK 3 J. MAGN. RESON. B104, 99-103 (1994).
REMARK 3 TERM FOR THE RADIUS OF GYRATION (KUSZEWSKI J, GRONENB
REMARK 3 CLORE, GM J AM CHEM SOC 121, 2337-2338 (1999))
REMARK 3 TORSION ANGLE DATABASE POTENTIAL (KUSZEWSKI J, GRONEN
REMARK 3 CLORE GM. PROTEIN SCI 5, 1067-1080 (1996); J. MAGN
REMARK 3 125, 171-177 (1997).
REMARK 3 COVALENT GEOMETRY RESTRAINTS (BONDS, ANGLES, IMPROPER
REMARK 3 QUARTIC VAN DER WAALS REPULSION TERM (NILGES. M,
REMARK 3 GRONENBORN, A.M., BRUNGER, A.T., CLORE, G.M. (1988)
REMARK 3 PROTEIN ENG. 2, 27-38).
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE OLIGOMERIZATION DOMAIN (RESIDUES
REMARK 3 319 - 360) OF P53 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED
REMARK 3 AND -FILTERED NMR IS BASED ON 4472 EXPERIMENTAL RESTRAINTS
REMARK 3 COMPRISING THE FOLLOWING INTRA- AND INTER-SUBUNIT
REMARK 3 RESTRAINTS:
REMARK 3
REMARK 3 (A) INTRASUBUNIT: 852 SEQUENTIAL (|I-J|=1), 712 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 76 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUES AND 740 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS, 136 DISTANCE RESTRAINTS FOR 68
REMARK 3 HYDROGEN BONDS, 284 TORSION ANGLE (144 PHI, 104 CHI1, AND
REMARK 3 36 CHI2) RESTRAINTS, AND 144 THREE-BOND HN-HA COUPLING
REMARK 3 CONSTANT RESTRAINTS.
REMARK 3
REMARK 3 (B) INTERSUBUNIT: 244 A-B/C-D, 876 A-C/B-D, 40 A-D/B-C
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS, 40 DISTANCE
REMARK 3 RESTRAINTS FOR 20 HYDROGEN BONDS INVOLVING THE A-C/B-D
REMARK 3 SUBUNITS, AND 36 DISTANCE RESTRAINTS FOR 4 WATER MOLECULES.
REMARK 3 IN ADDITION, THERE ARE A TOTAL OF 38 CALPHA AND 35 CB
REMARK 3 CHEMICAL SHIFT RESTRAINTS PER SUBUNIT THAT HAVE BEEN
REMARK 3 INCORPORATED INTO THE REFINEMENT [J. KUSZWESKI, J. QIN,
REMARK 3 A.M. GRONENBORN AND G.M. CLORE, J. MAGN RESON. SER B 106,
REMARK 3 92-96 (1995)].
REMARK 3
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. &
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT. 229, 317-324. ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE SOURCE REFERENCE.
REMARK 3
REMARK 3 THIS ENTRY CONTAINS THE RESTRAINED MINIMIZED AVERAGE
REMARK 3 STRUCTURE, FOLLOWED BY THE 22 INDIVIDUAL SIMULATED ANNEALING
REMARK 3 STRUCTURES. THE RESTRAINED MINIMIZED MEAN STRUCTURE IS OBTAI
REMARK 3 BY FIRST AVERAGING
REMARK 3 COORDINATES OF THE INDIVIDUAL 22 DYNAMICAL SIMULATED
REMARK 3 ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES 326 - 354
REMARK 3 OF ALL FOUR SUBUNITS, AND SUBJECTING THE RESULTING
REMARK 3 COORDINATES TO RESTRAINED MINIMIZATION. THE QUANTITY
REMARK 3 PRESENTED IN COLUMNS 61 - 66 OF THE RESTRAINED MINIMIZED MEA
REMARK 3 STRUCTURE
REMARK 3 (THE B-FACTOR COLUMN IN X-RAY STRUCTURES) GIVES THE
REMARK 3 AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES
REMARK 3 AND THE MEAN STRUCTURE. THE NUMBERS IN COLUMNS 61 - 66 OF
REMARK 3 THE INDIVIDUAL STRUCTURES HAVE NO MEANING. NOTE THAT
REMARK 3 RESIDUES 319 - 323 AT THE N-TERMINUS AND RESIDUES 357 - 360
REMARK 3 AT THE C-TERMINUS ARE COMPLETELY DISORDERED.
REMARK 3
REMARK 3
REMARK 3 TERMS IN THE TARGET FUNCTION USED FOR SIMULATED ANNEALING:
REMARK 3 NOE (SUM AVERAGING) AND TORSION ANGLE RESTRAINTS
REMARK 3 3JHNALPHA COUPLING CONSTANT RESTRAINTS (GARRETT ET AL
REMARK 3 J. MAGN. RESON. B104, 99-103 (1994).
REMARK 3 TERM FOR THE RADIUS OF GYRATION (KUSZEWSKI J, GRONENB
REMARK 3 CLORE, GM J AM CHEM SOC 121, 2337-2338 (1999))
REMARK 3 TORSION ANGLE DATABASE POTENTIAL (KUSZEWSKI J, GRONEN
REMARK 3 CLORE GM. PROTEIN SCI 5, 1067-1080 (1996); J. MAGN
REMARK 3 125, 171-177 (1997).
REMARK 3 COVALENT GEOMETRY RESTRAINTS (BONDS, ANGLES, IMPROPER
REMARK 3 QUARTIC VAN DER WAALS REPULSION TERM (NILGES. M,
REMARK 3 GRONENBORN, A.M., BRUNGER, A.T., CLORE, G.M. (1988)
REMARK 3 PROTEIN ENG. 2, 27-38).
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE OLIGOMERIZATION DOMAIN (RESIDUES
REMARK 3 319 - 360) OF P53 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED
REMARK 3 AND -FILTERED NMR IS BASED ON 4472 EXPERIMENTAL RESTRAINTS
REMARK 3 COMPRISING THE FOLLOWING INTRA- AND INTER-SUBUNIT
REMARK 3 RESTRAINTS:
REMARK 3
REMARK 3 (A) INTRASUBUNIT: 852 SEQUENTIAL (|I-J|=1), 712 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 76 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUES AND 740 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS, 136 DISTANCE RESTRAINTS FOR 68
REMARK 3 HYDROGEN BONDS, 284 TORSION ANGLE (144 PHI, 104 CHI1, AND
REMARK 3 36 CHI2) RESTRAINTS, AND 144 THREE-BOND HN-HA COUPLING
REMARK 3 CONSTANT RESTRAINTS.
REMARK 3
REMARK 3 (B) INTERSUBUNIT: 244 A-B/C-D, 876 A-C/B-D, 40 A-D/B-C
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS, 40 DISTANCE
REMARK 3 RESTRAINTS FOR 20 HYDROGEN BONDS INVOLVING THE A-C/B-D
REMARK 3 SUBUNITS, AND 36 DISTANCE RESTRAINTS FOR 4 WATER MOLECULES.
REMARK 3 IN ADDITION, THERE ARE A TOTAL OF 38 CALPHA AND 35 CB
REMARK 3 CHEMICAL SHIFT RESTRAINTS PER SUBUNIT THAT HAVE BEEN
REMARK 3 INCORPORATED INTO THE REFINEMENT [J. KUSZWESKI, J. QIN,
REMARK 3 A.M. GRONENBORN AND G.M. CLORE, J. MAGN RESON. SER B 106,
REMARK 3 92-96 (1995)].
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. &
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT. 229, 317-324. ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE SOURCE REFERENCE.
REMARK 3
REMARK 3 THIS ENTRY CONTAINS THE RESTRAINED MINIMIZED AVERAGE
REMARK 3 STRUCTURE, FOLLOWED BY THE 22 INDIVIDUAL SIMULATED ANNEALING
REMARK 3 STRUCTURES. THE RESTRAINED MINIMIZED MEAN STRUCTURE IS OBTAI
REMARK 3 BY FIRST AVERAGING
REMARK 3 COORDINATES OF THE INDIVIDUAL 22 DYNAMICAL SIMULATED
REMARK 3 ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES 326 - 354
REMARK 3 OF ALL FOUR SUBUNITS, AND SUBJECTING THE RESULTING
REMARK 3 COORDINATES TO RESTRAINED MINIMIZATION. THE QUANTITY
REMARK 3 PRESENTED IN COLUMNS 61 - 66 OF THE RESTRAINED MINIMIZED MEA
REMARK 3 STRUCTURE
REMARK 3 (THE B-FACTOR COLUMN IN X-RAY STRUCTURES) GIVES THE
REMARK 3 AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES
REMARK 3 AND THE MEAN STRUCTURE. THE NUMBERS IN COLUMNS 61 - 66 OF
REMARK 3 THE INDIVIDUAL STRUCTURES HAVE NO MEANING. NOTE THAT
REMARK 3 RESIDUES 319 - 323 AT THE N-TERMINUS AND RESIDUES 357 - 360
REMARK 3 AT THE C-TERMINUS ARE COMPLETELY DISORDERED.
REMARK 4
REMARK 4 3SAK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000000972.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D AND 4D TRIPLE AND DOUBLE
REMARK 210 RESONANCE HETERONUCLEAR
REMARK 210 EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR/CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 23
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : SIMULATED ANNEALING
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 H3 LYS B 1 HZ2 LYS B 2 1.20
REMARK 500 H3 LYS C 1 HZ2 LYS C 2 1.20
REMARK 500 H3 LYS A 1 HZ2 LYS A 2 1.20
REMARK 500 H3 LYS D 1 HZ2 LYS D 2 1.20
REMARK 500 O LYS B 1 H LYS B 3 1.31
REMARK 500 O LYS D 1 H LYS D 3 1.31
REMARK 500 O LYS C 1 H LYS C 3 1.31
REMARK 500 O LYS A 1 H LYS A 3 1.31
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 LYS A 2 -39.39 58.21
REMARK 500 1 LYS A 3 151.50 54.83
REMARK 500 1 LYS B 2 -39.45 58.27
REMARK 500 1 LYS B 3 151.54 54.85
REMARK 500 1 LYS C 2 -39.31 58.14
REMARK 500 1 LYS C 3 151.53 54.77
REMARK 500 1 LYS D 2 -39.35 58.19
REMARK 500 1 LYS D 3 151.54 54.76
REMARK 500 2 LYS A 3 72.32 51.19
REMARK 500 2 PRO A 4 -80.56 -60.40
REMARK 500 2 PRO A 41 174.75 -55.95
REMARK 500 2 LYS B 3 71.44 52.03
REMARK 500 2 PRO B 4 -81.04 -58.77
REMARK 500 2 PRO B 41 174.35 -55.18
REMARK 500 2 LYS C 3 73.07 51.23
REMARK 500 2 PRO C 4 -79.79 -60.79
REMARK 500 2 PRO C 41 170.95 -55.49
REMARK 500 2 LYS D 3 72.93 51.38
REMARK 500 2 PRO D 4 -80.31 -60.56
REMARK 500 2 PRO D 41 173.29 -56.19
REMARK 500 3 LYS A 2 90.91 50.86
REMARK 500 3 LYS B 2 90.98 50.70
REMARK 500 3 LYS C 2 90.81 50.97
REMARK 500 3 LYS D 2 90.88 51.20
REMARK 500 4 LYS A 2 -50.37 63.41
REMARK 500 4 LYS A 3 149.13 59.85
REMARK 500 4 PRO A 4 -83.25 -58.57
REMARK 500 4 PRO A 41 3.92 -60.00
REMARK 500 4 LYS B 2 -50.07 63.15
REMARK 500 4 LYS B 3 149.83 60.11
REMARK 500 4 PRO B 4 -83.53 -58.96
REMARK 500 4 PRO B 41 3.43 -59.81
REMARK 500 4 LYS C 2 -49.90 63.01
REMARK 500 4 LYS C 3 149.69 59.81
REMARK 500 4 PRO C 4 -84.41 -58.93
REMARK 500 4 PRO C 41 3.86 -60.15
REMARK 500 4 LYS D 2 -49.67 62.65
REMARK 500 4 LYS D 3 149.54 59.78
REMARK 500 4 PRO D 4 -84.64 -58.76
REMARK 500 4 PRO D 41 3.73 -59.38
REMARK 500 5 LYS A 2 -168.92 47.44
REMARK 500 5 LYS A 3 149.66 60.14
REMARK 500 5 PRO A 4 -163.80 -54.36
REMARK 500 5 LYS B 2 -168.20 47.43
REMARK 500 5 LYS B 3 149.93 59.81
REMARK 500 5 PRO B 4 -163.18 -54.59
REMARK 500 5 LYS C 2 -169.25 47.83
REMARK 500 5 LYS C 3 149.75 60.44
REMARK 500 5 PRO C 4 -164.07 -54.41
REMARK 500 5 LYS D 2 -168.26 47.50
REMARK 500
REMARK 500 THIS ENTRY HAS 211 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3SAK A 1 42 UNP P04637 P53_HUMAN 319 360
DBREF 3SAK B 1 42 UNP P04637 P53_HUMAN 319 360
DBREF 3SAK C 1 42 UNP P04637 P53_HUMAN 319 360
DBREF 3SAK D 1 42 UNP P04637 P53_HUMAN 319 360
SEQRES 1 A 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 A 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 A 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 A 42 GLU PRO GLY
SEQRES 1 B 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 B 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 B 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 B 42 GLU PRO GLY
SEQRES 1 C 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 C 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 C 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 C 42 GLU PRO GLY
SEQRES 1 D 42 LYS LYS LYS PRO LEU ASP GLY GLU TYR PHE THR LEU GLN
SEQRES 2 D 42 ILE ARG GLY ARG GLU ARG PHE GLU MET PHE ARG GLU LEU
SEQRES 3 D 42 ASN GLU ALA LEU GLU LEU LYS ASP ALA GLN ALA GLY LYS
SEQRES 4 D 42 GLU PRO GLY
FORMUL 5 HOH *4(H2 O)
HELIX 1 1 GLY A 16 GLY A 38 1 23
HELIX 2 2 GLY B 16 GLY B 38 1 23
HELIX 3 3 GLY C 16 GLY C 38 1 23
HELIX 4 4 GLY D 16 GLY D 38 1 23
SHEET 1 A 2 TYR A 9 ARG A 15 0
SHEET 2 A 2 TYR C 9 ARG C 15 -1 O PHE C 10 N ILE A 14
SHEET 1 B 2 TYR B 9 ARG B 15 0
SHEET 2 B 2 TYR D 9 ARG D 15 -1 O PHE D 10 N ILE B 14
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 - v 3 2 Bytes