Header list of 1ed7.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 27-JAN-00 1ED7
TITLE SOLUTION STRUCTURE OF THE CHITIN-BINDING DOMAIN OF BACILLUS CIRCULANS
TITLE 2 WL-12 CHITINASE A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITINASE A1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CHITIN-BINDING DOMAIN;
COMPND 5 SYNONYM: (CHBD-CHIA1);
COMPND 6 EC: 3.2.1.14;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CIRCULANS;
SOURCE 3 ORGANISM_TAXID: 1397;
SOURCE 4 STRAIN: WL-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS TWISTED BETA-SANDWICH, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR T.IKEGAMI,T.OKADA,M.HASHIMOTO,S.SEINO,T.WATANABE,M.SHIRAKAWA
REVDAT 3 16-FEB-22 1ED7 1 REMARK
REVDAT 2 24-FEB-09 1ED7 1 VERSN
REVDAT 1 24-MAY-00 1ED7 0
JRNL AUTH T.IKEGAMI,T.OKADA,M.HASHIMOTO,S.SEINO,T.WATANABE,M.SHIRAKAWA
JRNL TITL SOLUTION STRUCTURE OF THE CHITIN-BINDING DOMAIN OF BACILLUS
JRNL TITL 2 CIRCULANS WL-12 CHITINASE A1.
JRNL REF J.BIOL.CHEM. V. 275 13654 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10788483
JRNL DOI 10.1074/JBC.275.18.13654
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 493 NOE
REMARK 3 -BASED DISTANCE, 20 HYDROGEN BOND, AND 33 DIHEDRAL ANGLE
REMARK 3 CONSTRAINTS.
REMARK 4
REMARK 4 1ED7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010466.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 10; 100
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.0 MM 15N-LABELED CHBD-CHIA1 IN
REMARK 210 10 MM KH2PO4-K2HPO4 (PH 6.0) AND
REMARK 210 10 MM DEUTERATED DITHIOTHREITOL
REMARK 210 (DTT); 1.2 MM 15N-LABELED CHBD-
REMARK 210 CHIA1 IN 100 MM KH2PO4-K2HPO4
REMARK 210 (PH 6.0) AND 10 MM DEUTERATED DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, NMRPIPE 1.7, XWINNMR
REMARK 210 2.0, NMRPIPP 4.2.4, MOLMOL 2.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 26
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING A UNIFORMLY 15N
REMARK 210 -LABELED CHBD-CHIA1. STEREOSPECIFIC ASSIGNMENTS OF THE METHYL
REMARK 210 GROUPS OF THE LEUCINE AND VALINE RESIDUES WERE ACHIEVED WITH 15%
REMARK 210 FRACTIONALLY 13C-LABELED CHBD-CHIA1 DISSOLVED IN 99.8% D2O.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-30
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLN A 699 O
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 TYR A 670 -156.70 -97.72
REMARK 500 1 ASN A 671 90.87 -47.82
REMARK 500 1 ALA A 685 71.60 -63.40
REMARK 500 1 TRP A 687 36.27 -88.55
REMARK 500 2 ASN A 671 88.43 40.67
REMARK 500 2 ALA A 685 74.75 -64.29
REMARK 500 2 TRP A 687 33.38 -86.38
REMARK 500 2 VAL A 692 78.48 -116.87
REMARK 500 3 ALA A 664 108.06 -58.63
REMARK 500 3 ASN A 671 -35.87 -31.15
REMARK 500 3 PRO A 680 99.54 -61.61
REMARK 500 3 ALA A 685 78.66 -60.42
REMARK 500 3 TRP A 687 37.72 -89.46
REMARK 500 4 ASN A 671 -37.93 -32.09
REMARK 500 4 PRO A 680 102.31 -59.77
REMARK 500 4 ALA A 685 73.99 -62.45
REMARK 500 4 TRP A 687 38.82 -89.60
REMARK 500 5 VAL A 658 155.79 -48.04
REMARK 500 5 ASN A 671 -38.42 -29.60
REMARK 500 5 PRO A 680 99.36 -62.32
REMARK 500 5 ALA A 685 81.43 -58.26
REMARK 500 5 TRP A 687 30.48 -86.57
REMARK 500 5 SER A 690 59.41 71.06
REMARK 500 6 ASN A 671 -82.21 57.99
REMARK 500 6 ALA A 685 72.16 -63.69
REMARK 500 6 TRP A 687 39.34 -88.64
REMARK 500 6 SER A 690 62.04 69.90
REMARK 500 6 LEU A 698 -169.99 -104.32
REMARK 500 7 THR A 663 -167.47 -111.82
REMARK 500 7 TYR A 670 -159.45 -83.30
REMARK 500 7 ASN A 671 93.81 -46.30
REMARK 500 7 HIS A 681 -156.58 -155.42
REMARK 500 7 ALA A 685 74.91 -64.40
REMARK 500 7 TRP A 687 30.89 -85.68
REMARK 500 8 ASN A 671 82.62 42.76
REMARK 500 8 ALA A 685 77.38 -60.51
REMARK 500 8 TRP A 687 32.58 -87.97
REMARK 500 9 ASN A 671 -80.76 57.57
REMARK 500 9 PRO A 680 94.68 -61.58
REMARK 500 9 ALA A 685 84.70 -60.24
REMARK 500 9 TRP A 687 37.87 -88.91
REMARK 500 9 LEU A 695 10.33 -140.21
REMARK 500 10 ASN A 671 83.43 45.25
REMARK 500 10 PRO A 680 94.10 -63.68
REMARK 500 10 ALA A 685 81.80 -67.30
REMARK 500 10 TRP A 687 32.79 -86.70
REMARK 500 10 VAL A 692 76.76 -116.27
REMARK 500 11 ASN A 671 91.51 -47.81
REMARK 500 11 ALA A 685 74.15 -63.83
REMARK 500 11 TRP A 687 31.54 -85.65
REMARK 500
REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ED7 A 655 699 UNP P20533 CHIA1_BACCI 655 699
SEQRES 1 A 45 ALA TRP GLN VAL ASN THR ALA TYR THR ALA GLY GLN LEU
SEQRES 2 A 45 VAL THR TYR ASN GLY LYS THR TYR LYS CYS LEU GLN PRO
SEQRES 3 A 45 HIS THR SER LEU ALA GLY TRP GLU PRO SER ASN VAL PRO
SEQRES 4 A 45 ALA LEU TRP GLN LEU GLN
SHEET 1 A 2 THR A 660 TYR A 662 0
SHEET 2 A 2 HIS A 681 SER A 683 -1 O HIS A 681 N TYR A 662
SHEET 1 B 3 GLN A 666 TYR A 670 0
SHEET 2 B 3 LYS A 673 CYS A 677 -1 N LYS A 673 O TYR A 670
SHEET 3 B 3 TRP A 696 LEU A 698 -1 N GLN A 697 O LYS A 676
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 - b 16 2 Bytes