Header list of 1x6a.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 17-MAY-05 1X6A
TITLE SOLUTION STRUCTURES OF THE SECOND LIM DOMAIN OF HUMAN LIM-KINASE 2
TITLE 2 (LIMK2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIM DOMAIN KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIM DOMAIN;
COMPND 5 SYNONYM: LIMK-2;
COMPND 6 EC: 2.7.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LIMK2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040921-12;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS LIM-KINASE 2, ZINC FINGER DOMAIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN
KEYWDS 4 BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.NAMEKI,A.SASAGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X6A 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1X6A 1 VERSN
REVDAT 1 17-NOV-05 1X6A 0
JRNL AUTH N.NAMEKI,A.SASAGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE SECOND LIM DOMAIN OF HUMAN
JRNL TITL 2 LIM-KINASE 2 (LIMK2)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, OPALP 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), KORADI, R.,BILLETER, M.,GUNTERT,
REMARK 3 P. (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X6A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024432.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3MM LIM DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3;
REMARK 210 0.05MM ZNCL2, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 7 CYS A 70 CB - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 17 CYS A 70 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 19 CYS A 21 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 19 CYS A 70 CB - CA - C ANGL. DEV. = 8.6 DEGREES
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 PHE A 14 -50.11 -138.32
REMARK 500 1 THR A 26 -37.36 -143.87
REMARK 500 1 ASP A 53 77.26 -67.27
REMARK 500 1 ALA A 56 103.42 -55.69
REMARK 500 1 SER A 76 13.67 55.16
REMARK 500 1 SER A 80 -78.62 -83.98
REMARK 500 2 SER A 2 78.38 40.21
REMARK 500 2 TYR A 10 50.57 -152.82
REMARK 500 2 GLU A 34 -0.96 82.21
REMARK 500 2 LYS A 48 -1.62 66.38
REMARK 500 2 SER A 79 -165.67 -121.38
REMARK 500 3 THR A 26 -56.54 -131.53
REMARK 500 3 GLU A 34 6.67 84.04
REMARK 500 3 ALA A 63 76.10 -67.66
REMARK 500 3 SER A 80 -56.56 -163.61
REMARK 500 4 HIS A 19 21.95 -64.50
REMARK 500 4 THR A 26 -70.68 -127.36
REMARK 500 4 GLU A 34 -1.83 76.52
REMARK 500 4 CYS A 47 -8.37 -142.43
REMARK 500 4 ASP A 53 3.81 -63.24
REMARK 500 4 HIS A 62 39.91 38.99
REMARK 500 4 ALA A 63 -16.55 -148.61
REMARK 500 4 SER A 76 49.06 -89.49
REMARK 500 5 SER A 5 34.56 -71.50
REMARK 500 5 SER A 6 14.36 59.75
REMARK 500 5 THR A 26 -50.25 -125.66
REMARK 500 5 PRO A 78 -166.29 -74.98
REMARK 500 6 ASP A 53 43.97 -75.44
REMARK 500 6 GLN A 61 48.66 38.27
REMARK 500 6 ALA A 63 -38.66 -147.43
REMARK 500 7 SER A 5 41.96 -148.81
REMARK 500 7 TYR A 10 -49.58 -163.61
REMARK 500 7 LYS A 13 151.01 174.72
REMARK 500 7 PHE A 14 -67.47 -120.81
REMARK 500 7 GLU A 34 13.13 53.57
REMARK 500 7 CYS A 41 40.99 -143.47
REMARK 500 7 GLN A 61 44.65 34.35
REMARK 500 7 HIS A 62 36.23 39.03
REMARK 500 7 ALA A 63 -11.92 -143.64
REMARK 500 7 SER A 76 0.69 -65.13
REMARK 500 8 SER A 3 -168.96 -165.00
REMARK 500 8 LYS A 8 59.73 -145.25
REMARK 500 8 TYR A 10 -23.38 -150.11
REMARK 500 8 SER A 22 -16.12 81.11
REMARK 500 8 GLU A 34 -9.48 87.43
REMARK 500 8 LYS A 48 -7.85 71.78
REMARK 500 8 GLN A 61 -6.83 -55.91
REMARK 500 8 ALA A 63 7.86 80.09
REMARK 500 9 HIS A 19 19.80 -64.83
REMARK 500 9 SER A 22 -3.35 67.33
REMARK 500
REMARK 500 THIS ENTRY HAS 115 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 TYR A 37 0.10 SIDE CHAIN
REMARK 500 3 TYR A 37 0.07 SIDE CHAIN
REMARK 500 3 TYR A 66 0.06 SIDE CHAIN
REMARK 500 6 TYR A 10 0.07 SIDE CHAIN
REMARK 500 16 TYR A 66 0.07 SIDE CHAIN
REMARK 500 17 TYR A 57 0.07 SIDE CHAIN
REMARK 500 18 TYR A 10 0.09 SIDE CHAIN
REMARK 500 20 TYR A 10 0.08 SIDE CHAIN
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 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 18 SG
REMARK 620 2 CYS A 21 SG 82.0
REMARK 620 3 HIS A 38 ND1 79.9 72.0
REMARK 620 4 CYS A 41 SG 92.6 152.2 134.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 44 SG
REMARK 620 2 CYS A 47 SG 83.9
REMARK 620 3 CYS A 67 SG 95.3 138.7
REMARK 620 4 CYS A 70 SG 122.8 145.2 66.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002010509.1 RELATED DB: TARGETDB
DBREF 1X6A A 8 75 UNP P53671 LIMK2_HUMAN 62 129
SEQADV 1X6A GLY A 1 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A SER A 2 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A SER A 3 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A GLY A 4 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A SER A 5 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A SER A 6 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A GLY A 7 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A SER A 76 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A GLY A 77 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A PRO A 78 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A SER A 79 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A SER A 80 UNP P53671 CLONING ARTIFACT
SEQADV 1X6A GLY A 81 UNP P53671 CLONING ARTIFACT
SEQRES 1 A 81 GLY SER SER GLY SER SER GLY LYS ASP TYR TRP GLY LYS
SEQRES 2 A 81 PHE GLY GLU PHE CYS HIS GLY CYS SER LEU LEU MET THR
SEQRES 3 A 81 GLY PRO PHE MET VAL ALA GLY GLU PHE LYS TYR HIS PRO
SEQRES 4 A 81 GLU CYS PHE ALA CYS MET SER CYS LYS VAL ILE ILE GLU
SEQRES 5 A 81 ASP GLY ASP ALA TYR ALA LEU VAL GLN HIS ALA THR LEU
SEQRES 6 A 81 TYR CYS GLY LYS CYS HIS ASN GLU VAL VAL SER GLY PRO
SEQRES 7 A 81 SER SER GLY
HET ZN A 201 1
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLY A 68 SER A 76 1 9
SHEET 1 A 2 TYR A 57 LEU A 59 0
SHEET 2 A 2 LEU A 65 CYS A 67 -1 O TYR A 66 N ALA A 58
LINK SG CYS A 18 ZN ZN A 201 1555 1555 3.29
LINK SG CYS A 21 ZN ZN A 201 1555 1555 3.18
LINK ND1 HIS A 38 ZN ZN A 201 1555 1555 2.52
LINK SG CYS A 41 ZN ZN A 201 1555 1555 3.13
LINK SG CYS A 44 ZN ZN A 401 1555 1555 3.17
LINK SG CYS A 47 ZN ZN A 401 1555 1555 3.03
LINK SG CYS A 67 ZN ZN A 401 1555 1555 3.05
LINK SG CYS A 70 ZN ZN A 401 1555 1555 3.16
SITE 1 AC1 4 CYS A 18 CYS A 21 HIS A 38 CYS A 41
SITE 1 AC2 4 CYS A 44 CYS A 47 CYS A 67 CYS A 70
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