Header list of 1pb5.pdb file
Complete list - 23 20 Bytes
HEADER SIGNALING PROTEIN 14-MAY-03 1PB5
TITLE NMR STRUCTURE OF A PROTOTYPE LNR MODULE FROM HUMAN NOTCH1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST LNR MODULE;
COMPND 5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1;
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: BL21DE3PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMM
KEYWDS NOTCH SIGNALING, LIN12/NOTCH REPEAT, CALCIUM-BINDING DOMAIN, PROTEIN
KEYWDS 2 MODULE, DISULFIDE BOND, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
MDLTYP MINIMIZED AVERAGE
AUTHOR D.VARDAR,C.L.NORTH,C.SANCHEZ-IRIZARRY,J.C.ASTER,S.C.BLACKLOW
REVDAT 3 23-FEB-22 1PB5 1 REMARK LINK
REVDAT 2 24-FEB-09 1PB5 1 VERSN
REVDAT 1 17-JUN-03 1PB5 0
JRNL AUTH D.VARDAR,C.L.NORTH,C.SANCHEZ-IRIZARRY,J.C.ASTER,S.C.BLACKLOW
JRNL TITL NUCLEAR MAGNETIC RESONANCE STRUCTURE OF A PROTOTYPE
JRNL TITL 2 LIN12-NOTCH REPEAT MODULE FROM HUMAN NOTCH1
JRNL REF BIOCHEMISTRY V. 42 7061 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12795601
JRNL DOI 10.1021/BI034156Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PB5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019211.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 283
REMARK 210 PH : 6.5; 7.0
REMARK 210 IONIC STRENGTH : 10MM CA2+; 10MM CA2+, 50MM PIPES
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM LNRA U-15N, 10MM CA2+, 0.5MM
REMARK 210 DSS PH 6.5; 1MM LNRA U-15N,13C,
REMARK 210 10MM CA2+, 0.5MM DSS PH 6.5;
REMARK 210 1.5MM LNRA U-15N,13C, 10 MM CA2+,
REMARK 210 0.5MM DSS, 50 MM DEUTERATED
REMARK 210 PIPES PH 7.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HNCOCA, 13C HSQC; 3D_15N
REMARK 210 -SEPARATED TOCSY, 2D TOCSY, 15N-
REMARK 210 HSQC, 15N-HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 400 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0.4, CNS 1.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, TORSION ANGLE
REMARK 210 DYNAMICS, SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 H ASN A 15 OD2 ASP A 33 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 2 87.01 -69.93
REMARK 500 1 ALA A 3 16.78 -140.86
REMARK 500 1 CYS A 4 145.02 61.56
REMARK 500 1 VAL A 17 -139.35 -95.90
REMARK 500 1 CYS A 18 109.04 -162.39
REMARK 500 1 ASP A 30 28.14 46.43
REMARK 500 2 ALA A 3 16.18 -140.25
REMARK 500 2 CYS A 4 136.91 60.68
REMARK 500 2 VAL A 17 -141.53 -96.10
REMARK 500 2 CYS A 18 105.46 -162.06
REMARK 500 2 ASP A 30 27.33 47.06
REMARK 500 3 ALA A 3 16.86 -140.44
REMARK 500 3 CYS A 4 139.95 61.68
REMARK 500 3 VAL A 17 -141.98 -97.36
REMARK 500 3 ASP A 30 23.58 48.20
REMARK 500 4 GLU A 2 58.84 -102.05
REMARK 500 4 ALA A 3 17.62 -140.41
REMARK 500 4 CYS A 4 136.08 61.38
REMARK 500 4 VAL A 17 -141.48 -97.26
REMARK 500 4 CYS A 18 105.67 -161.03
REMARK 500 4 ASP A 30 23.30 48.80
REMARK 500 5 ALA A 3 16.78 -140.37
REMARK 500 5 CYS A 4 138.63 61.30
REMARK 500 5 VAL A 17 -141.65 -97.36
REMARK 500 5 ASP A 30 23.85 47.91
REMARK 500 6 ALA A 3 17.12 -140.68
REMARK 500 6 CYS A 4 145.64 62.02
REMARK 500 6 VAL A 17 -141.43 -95.94
REMARK 500 6 CYS A 18 105.72 -160.94
REMARK 500 6 ASP A 30 23.83 47.86
REMARK 500 7 ALA A 3 17.46 -140.41
REMARK 500 7 CYS A 4 138.08 61.66
REMARK 500 7 VAL A 17 -141.58 -95.74
REMARK 500 7 CYS A 18 105.46 -161.85
REMARK 500 7 ASP A 30 26.73 47.35
REMARK 500 8 GLU A 2 44.88 -95.29
REMARK 500 8 ALA A 3 18.67 -140.57
REMARK 500 8 CYS A 4 137.17 61.89
REMARK 500 8 VAL A 17 -139.79 -97.98
REMARK 500 8 CYS A 18 105.89 -163.18
REMARK 500 8 ASP A 30 28.12 46.11
REMARK 500 9 GLU A 2 56.74 -99.53
REMARK 500 9 ALA A 3 17.43 -140.67
REMARK 500 9 CYS A 4 144.14 62.27
REMARK 500 9 VAL A 17 -139.13 -97.95
REMARK 500 9 CYS A 18 106.25 -162.58
REMARK 500 9 ASP A 30 28.00 46.01
REMARK 500 10 ALA A 3 16.87 -140.31
REMARK 500 10 CYS A 4 138.59 61.07
REMARK 500 10 VAL A 17 -139.07 -98.28
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 12 O
REMARK 620 2 ASN A 15 OD1 70.8
REMARK 620 3 CYS A 18 N 146.1 104.0
REMARK 620 4 ASP A 30 OD1 62.9 129.3 125.9
REMARK 620 5 ASP A 30 OD2 105.2 170.9 83.9 44.1
REMARK 620 6 ASP A 33 OD2 71.1 65.0 138.7 80.9 106.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
DBREF 1PB5 A 1 35 UNP P46531 NOTC1_HUMAN 1447 1481
SEQRES 1 A 35 GLU GLU ALA CYS GLU LEU PRO GLU CYS GLN GLU ASP ALA
SEQRES 2 A 35 GLY ASN LYS VAL CYS SER LEU GLN CYS ASN ASN HIS ALA
SEQRES 3 A 35 CYS GLY TRP ASP GLY GLY ASP CYS SER
HET CA A 501 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 GLU A 8 ALA A 13 1 6
HELIX 2 2 GLY A 28 ASP A 33 5 6
SSBOND 1 CYS A 4 CYS A 27 1555 1555 2.03
SSBOND 2 CYS A 9 CYS A 22 1555 1555 2.03
SSBOND 3 CYS A 18 CYS A 34 1555 1555 2.03
LINK O ASP A 12 CA CA A 501 1555 1555 3.09
LINK OD1 ASN A 15 CA CA A 501 1555 1555 2.31
LINK N CYS A 18 CA CA A 501 1555 1555 3.23
LINK OD1 ASP A 30 CA CA A 501 1555 1555 2.90
LINK OD2 ASP A 30 CA CA A 501 1555 1555 2.95
LINK OD2 ASP A 33 CA CA A 501 1555 1555 2.16
SITE 1 AC1 6 ASP A 12 ASN A 15 VAL A 17 CYS A 18
SITE 2 AC1 6 ASP A 30 ASP A 33
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 - 23 20 Bytes