Header list of 1z1m.pdb file
Complete list - r 2 2 Bytes
HEADER LIGASE 04-MAR-05 1Z1M
TITLE NMR STRUCTURE OF UNLIGANDED MDM2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-PROTEIN LIGASE E3 MDM2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: P53-BINDING PROTEIN MDM2, ONCOPROTEIN MDM2, DOUBLE MINUTE 2
COMPND 6 PROTEIN, HDM2;
COMPND 7 EC: 6.3.2.-;
COMPND 8 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: ROSETTA (DE3) PLYSS
KEYWDS PEPTIDE-BINDING GROOVE, PSUDOSYMMETRY, ALPHA-BETA DOMAINS, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR S.UHRINOVA,D.UHRIN,H.POWERS,K.WATT,D.ZHELEVA,P.FISCHER,C.MCINNES,
AUTHOR 2 P.N.BARLOW
REVDAT 4 02-MAR-22 1Z1M 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1Z1M 1 VERSN
REVDAT 2 29-NOV-05 1Z1M 1 TITLE
REVDAT 1 28-JUN-05 1Z1M 0
JRNL AUTH S.UHRINOVA,D.UHRIN,H.POWERS,K.WATT,D.ZHELEVA,P.FISCHER,
JRNL AUTH 2 C.MCINNES,P.N.BARLOW
JRNL TITL STRUCTURE OF FREE MDM2 N-TERMINAL DOMAIN REVEALS
JRNL TITL 2 CONFORMATIONAL ADJUSTMENTS THAT ACCOMPANY P53-BINDING
JRNL REF J.MOL.BIOL. V. 350 587 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15953616
JRNL DOI 10.1016/J.JMB.2005.05.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AZARA, CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z1M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032183.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : 7.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.5MM HDM2(1-118), 60MM
REMARK 210 DEUTERATED SODIUM ACETATE, 60MM
REMARK 210 PHOSPHATE BUFFER; 0.5MM HDM2(1-
REMARK 210 118), 60MM DEUTERATED SODIUM
REMARK 210 ACETATE, 60MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG, CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 110
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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
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 CYS A 2 -16.93 -146.71
REMARK 500 1 MET A 6 11.19 -145.82
REMARK 500 1 SER A 7 176.25 61.51
REMARK 500 1 PRO A 9 24.69 -79.90
REMARK 500 1 ALA A 13 -173.21 58.68
REMARK 500 1 GLN A 18 -56.32 -162.87
REMARK 500 1 PRO A 20 96.20 -66.16
REMARK 500 1 ALA A 21 18.60 -163.51
REMARK 500 1 SER A 22 -53.79 -176.70
REMARK 500 1 GLU A 25 -79.97 -78.04
REMARK 500 1 THR A 26 126.26 85.00
REMARK 500 1 PRO A 32 97.93 -43.43
REMARK 500 1 LEU A 33 -42.10 -172.75
REMARK 500 1 GLN A 44 77.33 -173.33
REMARK 500 1 LEU A 54 -72.20 -53.19
REMARK 500 1 ASP A 68 -151.99 -52.57
REMARK 500 1 GLU A 69 20.84 -150.92
REMARK 500 1 LYS A 70 -62.32 -102.94
REMARK 500 1 HIS A 73 -10.94 -140.24
REMARK 500 1 ILE A 74 76.68 -105.14
REMARK 500 1 PHE A 86 -71.05 -115.76
REMARK 500 1 ARG A 105 -72.06 -68.19
REMARK 500 1 ASN A 106 -81.95 -79.51
REMARK 500 1 LEU A 107 146.71 -172.42
REMARK 500 1 VAL A 108 111.78 -176.15
REMARK 500 1 ASN A 111 -70.01 -87.40
REMARK 500 1 GLN A 112 93.35 57.42
REMARK 500 1 SER A 116 40.20 -87.56
REMARK 500 1 ASP A 117 -83.69 61.93
REMARK 500 2 PRO A 9 -178.27 -62.42
REMARK 500 2 THR A 10 129.12 66.23
REMARK 500 2 ALA A 13 -173.38 59.18
REMARK 500 2 VAL A 14 -72.49 -100.77
REMARK 500 2 SER A 17 173.45 61.97
REMARK 500 2 GLN A 18 -41.50 -150.41
REMARK 500 2 GLU A 23 -76.58 -85.20
REMARK 500 2 THR A 26 -39.11 84.51
REMARK 500 2 LEU A 27 83.33 52.19
REMARK 500 2 PRO A 32 95.21 -45.19
REMARK 500 2 LEU A 33 -30.00 -169.68
REMARK 500 2 LEU A 35 -44.62 -134.69
REMARK 500 2 GLN A 44 68.10 -150.57
REMARK 500 2 LEU A 54 -71.33 -48.82
REMARK 500 2 GLN A 59 -70.88 -51.83
REMARK 500 2 MET A 62 1.49 -69.59
REMARK 500 2 ARG A 65 80.32 55.32
REMARK 500 2 GLU A 69 -20.48 73.03
REMARK 500 2 HIS A 73 -67.96 -96.14
REMARK 500 2 SER A 78 89.35 52.40
REMARK 500 2 LEU A 85 -76.50 -55.00
REMARK 500
REMARK 500 THIS ENTRY HAS 668 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 18 ILE A 19 1 -148.82
REMARK 500 THR A 26 LEU A 27 5 143.60
REMARK 500 THR A 26 LEU A 27 6 140.76
REMARK 500 THR A 26 LEU A 27 7 144.92
REMARK 500 LEU A 35 LYS A 36 10 146.43
REMARK 500 THR A 26 LEU A 27 11 148.25
REMARK 500 LEU A 35 LYS A 36 11 147.07
REMARK 500 LEU A 38 LYS A 39 13 145.46
REMARK 500 GLN A 18 ILE A 19 14 -148.87
REMARK 500 GLN A 18 ILE A 19 15 142.87
REMARK 500 GLU A 25 THR A 26 15 -147.03
REMARK 500 GLU A 25 THR A 26 16 -145.03
REMARK 500 THR A 26 LEU A 27 16 -136.32
REMARK 500 THR A 26 LEU A 27 17 143.80
REMARK 500 LEU A 35 LYS A 36 17 -149.69
REMARK 500 THR A 26 LEU A 27 18 144.27
REMARK 500 ASP A 84 LEU A 85 20 -146.30
REMARK 500 THR A 26 LEU A 27 21 142.92
REMARK 500 LYS A 45 ASP A 46 22 -148.56
REMARK 500 GLN A 18 ILE A 19 23 -149.99
REMARK 500 THR A 26 LEU A 27 23 148.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z1M A 1 118 UNP Q00987 MDM2_HUMAN 1 118
SEQADV 1Z1M SER A 119 UNP Q00987 CLONING ARTIFACT
SEQRES 1 A 119 MET CYS ASN THR ASN MET SER VAL PRO THR ASP GLY ALA
SEQRES 2 A 119 VAL THR THR SER GLN ILE PRO ALA SER GLU GLN GLU THR
SEQRES 3 A 119 LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS
SEQRES 4 A 119 SER VAL GLY ALA GLN LYS ASP THR TYR THR MET LYS GLU
SEQRES 5 A 119 VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR LYS ARG
SEQRES 6 A 119 LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL TYR CYS SER
SEQRES 7 A 119 ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO SER PHE
SEQRES 8 A 119 SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET ILE TYR
SEQRES 9 A 119 ARG ASN LEU VAL VAL VAL ASN GLN GLN GLU SER SER ASP
SEQRES 10 A 119 SER SER
HELIX 1 1 LEU A 34 GLY A 42 1 9
HELIX 2 2 LYS A 51 THR A 63 1 13
HELIX 3 3 ASP A 80 PHE A 86 1 7
HELIX 4 4 GLU A 95 TYR A 104 1 10
SHEET 1 A 2 ILE A 74 VAL A 75 0
SHEET 2 A 2 PHE A 91 SER A 92 -1 O PHE A 91 N VAL A 75
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