HEADER CALCIUM-BINDING PROTEIN 30-MAR-04 1SW8
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN N60D CALMODULIN
TITLE 2 REFINED WITH PARAMAGNETISM BASED STRATEGY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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
KEYWDS CALCIUM, CALMODULIN, EF-HAND, LANTHANIDE, STRUCTURAL PROTEOMICS IN
KEYWDS 2 EUROPE, SPINE, STRUCTURAL GENOMICS, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.BERTINI,C.DEL BIANCO,I.GELIS,N.KATSAROS,C.LUCHINAT,G.PARIGI,
AUTHOR 2 M.PEANA,A.PROVENZANI,M.A.ZORODDU,STRUCTURAL PROTEOMICS IN EUROPE
AUTHOR 3 (SPINE)
REVDAT 4 27-OCT-21 1SW8 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1SW8 1 VERSN
REVDAT 2 11-MAY-04 1SW8 1 JRNL
REVDAT 1 06-APR-04 1SW8 0
JRNL AUTH I.BERTINI,C.DEL BIANCO,I.GELIS,N.KATSAROS,C.LUCHINAT,
JRNL AUTH 2 G.PARIGI,M.PEANA,A.PROVENZANI,M.A.ZORODDU
JRNL TITL EXPERIMENTALLY EXPLORING THE CONFORMATIONAL SPACE SAMPLED BY
JRNL TITL 2 DOMAIN REORIENTATION IN CALMODULIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 6841 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15100408
JRNL DOI 10.1073/PNAS.0308641101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1 3.1, DYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WITH PSEUDOCONTACT SHIFTS
REMARK 4
REMARK 4 1SW8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022048.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 400 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM CALMODULIN U-15N, 20 MM
REMARK 210 MES, 400 MM KCL, 90% H20, 10%
REMARK 210 D20; 1 MM CALMODULIN U-15N-13C,
REMARK 210 20 MM MES, 400 MM KCL, 90% H20,
REMARK 210 10% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1 3.1, XEASY 1.3,
REMARK 210 DYANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS CALCULATED USING DIMAGNETIC, DIHEDRAL
REMARK 210 ANGLE RESTRAINTS AND PSEUDOCONTACT SHIFTS
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 OD1 ASP A 22 CA CA A 80 0.99
REMARK 500 O GLN A 8 H PHE A 12 1.54
REMARK 500 O GLU A 11 H ALA A 15 1.57
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 ASP A 2 -39.16 88.45
REMARK 500 1 GLN A 3 33.20 -140.69
REMARK 500 1 LEU A 4 28.38 40.43
REMARK 500 1 PHE A 16 -39.18 -37.60
REMARK 500 1 GLN A 41 178.14 -49.95
REMARK 500 1 ASN A 42 64.83 -154.39
REMARK 500 1 ASP A 56 108.35 -43.88
REMARK 500 1 ASP A 58 -35.78 -39.50
REMARK 500 1 ASP A 60 -49.56 176.88
REMARK 500 2 LEU A 4 -38.86 -175.61
REMARK 500 2 THR A 5 -32.45 -37.47
REMARK 500 2 GLN A 41 -174.25 -52.59
REMARK 500 2 ASN A 42 60.60 -163.65
REMARK 500 2 ASP A 56 109.79 -53.12
REMARK 500 2 ASP A 60 -50.66 176.26
REMARK 500 3 GLN A 3 -57.42 -125.69
REMARK 500 3 LEU A 4 -34.21 -176.68
REMARK 500 3 THR A 5 -31.65 -37.58
REMARK 500 3 LEU A 39 -70.78 -81.89
REMARK 500 3 ASN A 42 61.67 -166.39
REMARK 500 3 ASP A 56 109.28 -49.74
REMARK 500 3 ASP A 60 -60.81 168.30
REMARK 500 4 GLN A 3 -72.71 -140.06
REMARK 500 4 LEU A 4 32.13 -173.35
REMARK 500 4 ILE A 9 -39.25 -39.42
REMARK 500 4 GLN A 41 -172.21 -61.06
REMARK 500 4 ASN A 42 60.71 -167.51
REMARK 500 4 ASP A 56 107.94 -51.79
REMARK 500 4 ASP A 60 -67.18 176.22
REMARK 500 5 ASP A 2 19.88 55.05
REMARK 500 5 PHE A 16 -32.18 -36.55
REMARK 500 5 ASP A 20 39.65 -96.59
REMARK 500 5 ILE A 27 77.84 -104.25
REMARK 500 5 ASP A 56 108.19 -50.48
REMARK 500 5 ASP A 58 -35.00 -39.86
REMARK 500 5 ASP A 60 -50.72 -167.64
REMARK 500 6 GLN A 3 20.64 -141.59
REMARK 500 6 LEU A 4 -61.95 69.69
REMARK 500 6 THR A 28 150.76 -46.06
REMARK 500 6 ASN A 42 62.31 -156.41
REMARK 500 6 ASP A 56 106.38 -54.07
REMARK 500 6 ASP A 58 -33.51 -38.93
REMARK 500 6 ASP A 60 -55.43 -164.20
REMARK 500 7 LEU A 4 -60.45 -127.45
REMARK 500 7 ASP A 22 -75.56 -43.59
REMARK 500 7 THR A 28 153.88 -47.57
REMARK 500 7 LEU A 39 35.51 -89.79
REMARK 500 7 GLN A 41 178.31 -49.05
REMARK 500 7 ASN A 42 57.09 -165.08
REMARK 500 7 ASP A 56 108.84 -50.22
REMARK 500
REMARK 500 THIS ENTRY HAS 127 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 80 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD2 163.9
REMARK 620 3 GLY A 23 N 99.2 90.8
REMARK 620 4 ASP A 24 OD1 109.5 54.4 123.4
REMARK 620 5 ASP A 24 N 98.9 75.6 58.6 69.3
REMARK 620 6 THR A 26 O 73.8 97.0 171.7 64.1 126.2
REMARK 620 7 GLU A 31 OE1 71.0 120.0 99.1 135.8 154.5 74.5
REMARK 620 8 GLU A 31 OE2 107.7 77.3 120.2 96.2 152.9 59.3 46.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 81 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 55.5
REMARK 620 3 ASP A 60 OD1 80.0 106.3
REMARK 620 4 ASP A 60 OD2 66.0 60.8 47.5
REMARK 620 5 THR A 62 N 77.3 131.5 49.2 92.0
REMARK 620 6 THR A 62 O 88.4 125.3 105.7 144.0 56.5
REMARK 620 7 GLU A 67 OE1 106.0 91.4 161.3 151.1 114.0 57.7
REMARK 620 8 GLU A 67 OE2 71.2 48.6 149.6 109.2 129.5 83.7 44.5
REMARK 620 N 1 2 3 4 5 6 7
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 80
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 81
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CIRMMP35 RELATED DB: TARGETDB
DBREF 1SW8 A 1 79 UNP P62158 CALM_HUMAN 2 80
SEQADV 1SW8 ASP A 60 UNP P62158 ASN 61 ENGINEERED MUTATION
SEQRES 1 A 79 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 79 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 79 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 79 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 79 ASN GLU VAL ASP ALA ASP GLY ASP GLY THR ILE ASP PHE
SEQRES 6 A 79 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 79 THR
HET CA A 80 1
HET CA A 81 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 LEU A 4 ASP A 20 1 17
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 THR A 79 1 15
SHEET 1 A 2 THR A 26 ILE A 27 0
SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
LINK OD1 ASP A 20 CA CA A 80 1555 1555 2.30
LINK OD2 ASP A 22 CA CA A 80 1555 1555 2.29
LINK N GLY A 23 CA CA A 80 1555 1555 2.80
LINK OD1 ASP A 24 CA CA A 80 1555 1555 2.79
LINK N ASP A 24 CA CA A 80 1555 1555 2.87
LINK O THR A 26 CA CA A 80 1555 1555 2.37
LINK OE1 GLU A 31 CA CA A 80 1555 1555 2.85
LINK OE2 GLU A 31 CA CA A 80 1555 1555 2.76
LINK OD1 ASP A 56 CA CA A 81 1555 1555 2.19
LINK OD1 ASP A 58 CA CA A 81 1555 1555 2.81
LINK OD1 ASP A 60 CA CA A 81 1555 1555 3.02
LINK OD2 ASP A 60 CA CA A 81 1555 1555 2.19
LINK N THR A 62 CA CA A 81 1555 1555 3.18
LINK O THR A 62 CA CA A 81 1555 1555 2.24
LINK OE1 GLU A 67 CA CA A 81 1555 1555 2.86
LINK OE2 GLU A 67 CA CA A 81 1555 1555 3.01
SITE 1 AC1 6 ASP A 20 ASP A 22 GLY A 23 ASP A 24
SITE 2 AC1 6 THR A 26 GLU A 31
SITE 1 AC2 6 ASP A 56 ASP A 58 ASP A 60 THR A 62
SITE 2 AC2 6 ASP A 64 GLU A 67
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
(ATOM LINES ARE NOT SHOWN.)
END