Header list of 1azj.pdb file
Complete list - 3 20 Bytes
HEADER CELLULASE 18-NOV-97 1AZJ
TITLE THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING
TITLE 2 DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 18
TITLE 3 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLOBIOHYDROLASE I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CELLULOSE-BINDING DOMAIN;
COMPND 5 SYNONYM: CBD;
COMPND 6 EC: 3.2.1.91;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HYPOCREA JECORINA;
SOURCE 3 ORGANISM_TAXID: 51453
KEYWDS CELLULASE, NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, PROTEIN-
KEYWDS 2 CARBOHYDRATE INTERACTION, CELLULOSE DEGRADATION, HYDROLASE,
KEYWDS 3 GLYCOSIDASE
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR M.-L.MATTINEN
REVDAT 3 03-NOV-21 1AZJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1AZJ 1 VERSN
REVDAT 1 29-APR-98 1AZJ 0
JRNL AUTH M.L.MATTINEN,M.KONTTELI,J.KEROVUO,M.LINDER,A.ANNILA,
JRNL AUTH 2 G.LINDEBERG,T.REINIKAINEN,T.DRAKENBERG
JRNL TITL THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED
JRNL TITL 2 CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM
JRNL TITL 3 TRICHODERMA REESEI.
JRNL REF PROTEIN SCI. V. 6 294 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9041630
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SA/MD
REMARK 3 AUTHORS : CLORE,NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AZJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171446.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 3.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; COSY; NOESY; RELAY-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : VARIAN UNITY 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BIOSYM TECHNOLOGIES
REMARK 210 TECHNOLOGIES, FELIX, INSIGHT II
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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: 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 HIS A 4 132.55 -38.59
REMARK 500 1 TYR A 5 -23.12 70.05
REMARK 500 1 ILE A 11 71.88 -59.77
REMARK 500 1 THR A 17 32.04 -71.76
REMARK 500 1 VAL A 27 50.75 -140.37
REMARK 500 2 TYR A 5 -12.06 69.83
REMARK 500 2 PRO A 16 88.89 -65.38
REMARK 500 2 THR A 17 31.88 -72.90
REMARK 500 2 ALA A 20 96.47 -67.23
REMARK 500 2 SER A 21 -13.71 -37.09
REMARK 500 2 PRO A 30 17.76 -65.82
REMARK 500 2 SER A 33 81.62 153.63
REMARK 500 2 CYS A 35 79.27 -62.92
REMARK 500 3 TYR A 5 -13.73 67.19
REMARK 500 3 ILE A 11 109.04 -54.19
REMARK 500 3 TYR A 13 -177.43 -65.97
REMARK 500 3 CYS A 25 82.33 -67.30
REMARK 500 3 GLN A 26 173.59 -54.23
REMARK 500 3 PRO A 30 -9.31 -58.26
REMARK 500 3 CYS A 35 84.13 -64.67
REMARK 500 4 TYR A 5 -15.49 67.53
REMARK 500 4 SER A 14 85.07 -157.98
REMARK 500 4 GLN A 26 93.30 -66.40
REMARK 500 4 VAL A 27 68.23 -61.59
REMARK 500 4 CYS A 35 78.79 -67.55
REMARK 500 5 TYR A 5 -21.25 65.37
REMARK 500 5 PRO A 16 75.10 -60.82
REMARK 500 5 THR A 17 32.96 -60.71
REMARK 500 5 SER A 21 114.29 -35.17
REMARK 500 5 CYS A 25 77.19 -63.23
REMARK 500 5 VAL A 27 59.30 -63.98
REMARK 500 5 TYR A 32 -158.02 -130.11
REMARK 500 5 SER A 33 76.98 136.53
REMARK 500 6 TYR A 5 -8.00 65.87
REMARK 500 6 PRO A 16 84.28 -61.61
REMARK 500 6 THR A 17 42.50 -68.51
REMARK 500 6 CYS A 25 74.12 -67.60
REMARK 500 6 CYS A 35 87.88 -68.66
REMARK 500 7 CYS A 8 -39.16 -31.09
REMARK 500 7 ILE A 11 27.30 -74.01
REMARK 500 7 PRO A 16 69.64 -65.54
REMARK 500 7 THR A 17 32.19 -60.95
REMARK 500 7 SER A 21 103.04 -34.04
REMARK 500 7 VAL A 27 63.08 30.49
REMARK 500 8 TYR A 5 -23.55 73.08
REMARK 500 8 SER A 14 4.82 -151.60
REMARK 500 8 CYS A 25 81.17 -58.08
REMARK 500 8 VAL A 27 76.50 -53.91
REMARK 500 9 ILE A 11 108.49 -53.23
REMARK 500 9 TYR A 13 -179.84 -62.01
REMARK 500
REMARK 500 THIS ENTRY HAS 96 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 ILE A 11 GLY A 12 2 -145.93
REMARK 500 ILE A 11 GLY A 12 5 -145.07
REMARK 500 GLY A 12 TYR A 13 5 137.60
REMARK 500 ILE A 11 GLY A 12 6 -147.00
REMARK 500 GLY A 12 TYR A 13 6 144.34
REMARK 500 GLY A 10 ILE A 11 7 -128.43
REMARK 500 ILE A 11 GLY A 12 7 138.23
REMARK 500 TYR A 32 SER A 33 7 146.08
REMARK 500 ILE A 11 GLY A 12 8 -142.11
REMARK 500 GLY A 12 TYR A 13 8 141.98
REMARK 500 TYR A 32 SER A 33 8 149.22
REMARK 500 TYR A 32 SER A 33 9 148.94
REMARK 500 THR A 1 GLN A 2 10 147.52
REMARK 500 GLY A 12 TYR A 13 11 140.11
REMARK 500 GLY A 12 TYR A 13 12 137.99
REMARK 500 TYR A 32 SER A 33 12 148.62
REMARK 500 ILE A 11 GLY A 12 13 -148.57
REMARK 500 GLY A 12 TYR A 13 13 145.55
REMARK 500 ILE A 11 GLY A 12 14 -149.66
REMARK 500 TYR A 32 SER A 33 14 145.01
REMARK 500 GLY A 9 GLY A 10 15 148.70
REMARK 500 GLY A 12 TYR A 13 15 145.89
REMARK 500 ILE A 11 GLY A 12 16 -147.75
REMARK 500 GLY A 12 TYR A 13 16 139.66
REMARK 500 GLY A 12 TYR A 13 17 139.57
REMARK 500 CYS A 25 GLN A 26 18 -149.23
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 3 TYR A 13 0.17 SIDE CHAIN
REMARK 500 3 TYR A 32 0.09 SIDE CHAIN
REMARK 500 4 TYR A 13 0.16 SIDE CHAIN
REMARK 500 4 TYR A 32 0.08 SIDE CHAIN
REMARK 500 5 TYR A 32 0.11 SIDE CHAIN
REMARK 500 6 TYR A 32 0.12 SIDE CHAIN
REMARK 500 8 TYR A 5 0.08 SIDE CHAIN
REMARK 500 8 TYR A 13 0.18 SIDE CHAIN
REMARK 500 8 TYR A 32 0.09 SIDE CHAIN
REMARK 500 9 TYR A 13 0.14 SIDE CHAIN
REMARK 500 9 TYR A 32 0.14 SIDE CHAIN
REMARK 500 10 TYR A 13 0.13 SIDE CHAIN
REMARK 500 11 TYR A 13 0.07 SIDE CHAIN
REMARK 500 11 TYR A 32 0.12 SIDE CHAIN
REMARK 500 14 TYR A 13 0.12 SIDE CHAIN
REMARK 500 14 TYR A 32 0.09 SIDE CHAIN
REMARK 500 15 TYR A 13 0.10 SIDE CHAIN
REMARK 500 16 TYR A 13 0.14 SIDE CHAIN
REMARK 500 16 TYR A 32 0.08 SIDE CHAIN
REMARK 500 17 TYR A 32 0.09 SIDE CHAIN
REMARK 500 18 TYR A 13 0.13 SIDE CHAIN
REMARK 500 18 TYR A 32 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AZJ A 1 36 UNP P62694 GUX1_TRIRE 478 513
SEQADV 1AZJ ALA A 31 UNP P62694 TYR 508 ENGINEERED MUTATION
SEQRES 1 A 36 THR GLN SER HIS TYR GLY GLN CYS GLY GLY ILE GLY TYR
SEQRES 2 A 36 SER GLY PRO THR VAL CYS ALA SER GLY THR THR CYS GLN
SEQRES 3 A 36 VAL LEU ASN PRO ALA TYR SER GLN CYS LEU
SHEET 1 A 2 GLN A 7 GLY A 10 0
SHEET 2 A 2 TYR A 32 GLN A 34 -1 N SER A 33 O CYS A 8
SSBOND 1 CYS A 8 CYS A 25 1555 1555 2.15
SSBOND 2 CYS A 19 CYS A 35 1555 1555 2.14
CISPEP 1 GLY A 6 GLN A 7 16 -6.53
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 - 3 20 Bytes