Header list of 1q02.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 15-JUL-03 1Q02
TITLE NMR STRUCTURE OF THE UBA DOMAIN OF P62 (SQSTM1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEQUESTOSOME 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBA DOMAIN;
COMPND 5 SYNONYM: UBIQUITIN-BINDING PROTEIN P62, SQSTM1;
COMPND 6 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_STRAIN: XL-10 GOLD;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS HELICAL BUNDLE, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR B.CIANI,R.LAYFIELD,J.R.CAVEY,P.W.SHEPPARD,M.S.SEARLE
REVDAT 3 02-MAR-22 1Q02 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q02 1 VERSN
REVDAT 1 30-SEP-03 1Q02 0
JRNL AUTH B.CIANI,R.LAYFIELD,J.R.CAVEY,P.W.SHEPPARD,M.S.SEARLE
JRNL TITL STRUCTURE OF THE UBIQUITIN-ASSOCIATED DOMAIN OF P62 (SQSTM1)
JRNL TITL 2 AND IMPLICATIONS FOR MUTATIONS THAT CAUSE PAGET'S DISEASE OF
JRNL TITL 3 BONE
JRNL REF J.BIOL.CHEM. V. 278 37409 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12857745
JRNL DOI 10.1074/JBC.M307416200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, AT (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Q02 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019746.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 308
REMARK 210 PH : 5.8; 5.8
REMARK 210 IONIC STRENGTH : 50MM POTASSIUM PHOSPHATE; 50MM
REMARK 210 POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM UBA, PHOSPHATE BUFFER PH
REMARK 210 5.8, 10% D2O, 90% H2O; 2MM UBA,
REMARK 210 PHOSPHATE BUFFER PH 5.8, 90% D2O,
REMARK 210 10% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1, ANSIG 3.3
REMARK 210 METHOD USED : RESTRAINED SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
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: 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 LEU A 32 H LYS A 36 1.42
REMARK 500 O ASP A 39 H ALA A 43 1.43
REMARK 500 O LYS A 36 H ASP A 39 1.49
REMARK 500 O LEU A 33 H TYR A 38 1.50
REMARK 500 O ALA A 43 H ILE A 47 1.52
REMARK 500 O TRP A 28 H LEU A 32 1.55
REMARK 500 OD1 ASP A 24 H LEU A 29 1.58
REMARK 500 O LEU A 44 H GLN A 48 1.58
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 2 75.99 -165.68
REMARK 500 1 MET A 20 -63.80 -103.68
REMARK 500 1 SER A 23 -158.24 -105.82
REMARK 500 1 ASP A 24 38.54 -175.80
REMARK 500 1 GLU A 25 -70.82 -39.00
REMARK 500 1 LYS A 36 40.77 -87.63
REMARK 500 1 ASN A 37 50.32 34.04
REMARK 500 1 ASP A 39 39.20 -84.13
REMARK 500 1 TYR A 49 86.29 37.42
REMARK 500 2 GLU A 5 49.89 -106.98
REMARK 500 2 ALA A 6 -78.42 -179.04
REMARK 500 2 ASP A 7 78.99 42.11
REMARK 500 2 SER A 23 -142.07 -62.45
REMARK 500 2 ASP A 24 30.40 -169.25
REMARK 500 2 ASN A 37 64.40 38.01
REMARK 500 2 TYR A 49 27.73 40.13
REMARK 500 2 SER A 50 70.07 41.77
REMARK 500 3 SER A 2 85.78 -166.76
REMARK 500 3 ALA A 6 -49.01 -163.34
REMARK 500 3 MET A 20 -47.14 -135.82
REMARK 500 3 SER A 23 -139.18 -58.33
REMARK 500 3 ASP A 24 29.20 -173.78
REMARK 500 3 LYS A 36 32.59 -148.59
REMARK 500 3 TYR A 49 -167.37 41.73
REMARK 500 3 SER A 50 -74.27 169.71
REMARK 500 3 LYS A 51 74.69 53.67
REMARK 500 4 MET A 20 -62.65 -133.67
REMARK 500 4 SER A 23 -154.13 -111.72
REMARK 500 4 ASP A 24 36.25 -155.48
REMARK 500 4 ASN A 37 71.23 50.31
REMARK 500 4 TYR A 38 46.94 27.29
REMARK 500 4 ILE A 40 -74.46 -47.80
REMARK 500 4 TYR A 49 38.47 35.90
REMARK 500 5 MET A 20 -53.93 -133.39
REMARK 500 5 SER A 23 -151.04 -96.08
REMARK 500 5 ASP A 24 22.22 -156.28
REMARK 500 5 GLU A 25 98.72 -49.45
REMARK 500 5 LYS A 36 47.08 -142.02
REMARK 500 5 ASN A 37 72.42 49.03
REMARK 500 5 ASP A 39 32.64 -96.11
REMARK 500 5 ILE A 40 -80.29 -45.32
REMARK 500 5 TYR A 49 71.91 62.02
REMARK 500 6 SER A 2 70.13 53.60
REMARK 500 6 GLU A 5 66.88 -150.26
REMARK 500 6 MET A 20 -63.28 -105.51
REMARK 500 6 SER A 23 -150.50 -108.12
REMARK 500 6 ASP A 24 38.18 -160.79
REMARK 500 6 TYR A 38 53.95 31.28
REMARK 500 6 TYR A 49 75.47 35.54
REMARK 500 7 SER A 2 -58.48 174.97
REMARK 500
REMARK 500 THIS ENTRY HAS 257 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 9 0.25 SIDE CHAIN
REMARK 500 1 ARG A 31 0.30 SIDE CHAIN
REMARK 500 2 ARG A 9 0.32 SIDE CHAIN
REMARK 500 2 ARG A 31 0.28 SIDE CHAIN
REMARK 500 3 ARG A 9 0.15 SIDE CHAIN
REMARK 500 3 ARG A 31 0.23 SIDE CHAIN
REMARK 500 4 ARG A 9 0.20 SIDE CHAIN
REMARK 500 4 ARG A 31 0.32 SIDE CHAIN
REMARK 500 5 ARG A 9 0.30 SIDE CHAIN
REMARK 500 5 ARG A 31 0.14 SIDE CHAIN
REMARK 500 6 ARG A 9 0.23 SIDE CHAIN
REMARK 500 6 ARG A 31 0.28 SIDE CHAIN
REMARK 500 7 ARG A 9 0.28 SIDE CHAIN
REMARK 500 7 ARG A 31 0.31 SIDE CHAIN
REMARK 500 8 ARG A 9 0.27 SIDE CHAIN
REMARK 500 8 ARG A 31 0.27 SIDE CHAIN
REMARK 500 9 ARG A 9 0.23 SIDE CHAIN
REMARK 500 9 ARG A 31 0.20 SIDE CHAIN
REMARK 500 10 ARG A 9 0.30 SIDE CHAIN
REMARK 500 10 ARG A 31 0.32 SIDE CHAIN
REMARK 500 11 ARG A 9 0.19 SIDE CHAIN
REMARK 500 11 ARG A 31 0.26 SIDE CHAIN
REMARK 500 12 ARG A 9 0.31 SIDE CHAIN
REMARK 500 12 ARG A 31 0.30 SIDE CHAIN
REMARK 500 13 ARG A 9 0.22 SIDE CHAIN
REMARK 500 13 ARG A 31 0.25 SIDE CHAIN
REMARK 500 14 ARG A 9 0.31 SIDE CHAIN
REMARK 500 14 ARG A 31 0.32 SIDE CHAIN
REMARK 500 15 ARG A 9 0.27 SIDE CHAIN
REMARK 500 15 ARG A 31 0.31 SIDE CHAIN
REMARK 500 16 ARG A 9 0.24 SIDE CHAIN
REMARK 500 16 ARG A 31 0.32 SIDE CHAIN
REMARK 500 17 ARG A 31 0.27 SIDE CHAIN
REMARK 500 18 ARG A 9 0.30 SIDE CHAIN
REMARK 500 18 ARG A 31 0.29 SIDE CHAIN
REMARK 500 19 ARG A 9 0.30 SIDE CHAIN
REMARK 500 19 ARG A 31 0.21 SIDE CHAIN
REMARK 500 20 ARG A 9 0.20 SIDE CHAIN
REMARK 500 20 ARG A 31 0.31 SIDE CHAIN
REMARK 500 21 ARG A 9 0.27 SIDE CHAIN
REMARK 500 21 ARG A 31 0.26 SIDE CHAIN
REMARK 500 22 ARG A 9 0.15 SIDE CHAIN
REMARK 500 22 ARG A 31 0.27 SIDE CHAIN
REMARK 500 23 ARG A 9 0.27 SIDE CHAIN
REMARK 500 23 ARG A 31 0.31 SIDE CHAIN
REMARK 500 24 ARG A 9 0.27 SIDE CHAIN
REMARK 500 24 ARG A 31 0.29 SIDE CHAIN
REMARK 500 25 ARG A 9 0.28 SIDE CHAIN
REMARK 500 25 ARG A 31 0.32 SIDE CHAIN
REMARK 500 26 ARG A 9 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 53 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Q02 A 3 52 UNP Q13501 SQSTM_HUMAN 387 436
SEQADV 1Q02 GLY A 1 UNP Q13501 CLONING ARTIFACT
SEQADV 1Q02 SER A 2 UNP Q13501 CLONING ARTIFACT
SEQRES 1 A 52 GLY SER PRO PRO GLU ALA ASP PRO ARG LEU ILE GLU SER
SEQRES 2 A 52 LEU SER GLN MET LEU SER MET GLY PHE SER ASP GLU GLY
SEQRES 3 A 52 GLY TRP LEU THR ARG LEU LEU GLN THR LYS ASN TYR ASP
SEQRES 4 A 52 ILE GLY ALA ALA LEU ASP THR ILE GLN TYR SER LYS HIS
HELIX 1 1 ASP A 7 SER A 19 1 13
HELIX 2 2 GLY A 27 LYS A 36 1 10
HELIX 3 3 ASP A 39 GLN A 48 1 10
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