HEADER HYDROLASE 12-JAN-96 1KUL
TITLE GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN, NMR, 5 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOAMYLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BINDING DOMAIN, RESIDUES 509 - 616;
COMPND 5 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCOHYDROLASE;
COMPND 6 EC: 3.2.1.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: PH 5.2, 313 K
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 STRAIN: AB4.1;
SOURCE 5 GENE: A. NIGER GLAA;
SOURCE 6 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 5061;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PIGF;
SOURCE 9 EXPRESSION_SYSTEM_GENE: A. NIGER GLAA
KEYWDS HYDROLASE, STARCH BINDING DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR K.SORIMACHI,A.J.JACKS,M.-F.LE GAL-COEFFET,G.WILLIAMSON,D.B.ARCHER,
AUTHOR 2 M.P.WILLIAMSON
REVDAT 3 23-FEB-22 1KUL 1 REMARK
REVDAT 2 24-FEB-09 1KUL 1 VERSN
REVDAT 1 11-JUL-96 1KUL 0
JRNL AUTH K.SORIMACHI,A.J.JACKS,M.F.LE GAL-COEFFET,G.WILLIAMSON,
JRNL AUTH 2 D.B.ARCHER,M.P.WILLIAMSON
JRNL TITL SOLUTION STRUCTURE OF THE GRANULAR STARCH BINDING DOMAIN OF
JRNL TITL 2 GLUCOAMYLASE FROM ASPERGILLUS NIGER BY NUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE SPECTROSCOPY.
JRNL REF J.MOL.BIOL. V. 259 970 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8683599
JRNL DOI 10.1006/JMBI.1996.0374
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.J.JACKS,K.SORIMACHI,M.F.LE GAL-COEFFET,G.WILLIAMSON,
REMARK 1 AUTH 2 D.B.ARCHER,M.P.WILLIAMSON
REMARK 1 TITL 1H AND 15N ASSIGNMENTS AND SECONDARY STRUCTURE OF THE
REMARK 1 TITL 2 STARCH-BINDING DOMAIN OF GLUCOAMYLASE FROM ASPERGILLUS NIGER
REMARK 1 REF EUR.J.BIOCHEM. V. 233 568 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KUL 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_1000174496.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 THR A 511 -169.07 46.60
REMARK 500 1 THR A 513 83.41 -33.49
REMARK 500 1 LEU A 521 -177.19 -68.42
REMARK 500 1 ALA A 523 119.11 -161.45
REMARK 500 1 THR A 524 43.82 -88.98
REMARK 500 1 THR A 526 32.80 -143.23
REMARK 500 1 TYR A 527 45.64 -82.65
REMARK 500 1 LEU A 540 33.03 -89.63
REMARK 500 1 ASP A 542 -62.68 75.95
REMARK 500 1 TRP A 543 44.17 -175.78
REMARK 500 1 LEU A 551 -167.42 -103.08
REMARK 500 1 ALA A 553 56.85 -142.51
REMARK 500 1 THR A 557 -77.87 -143.34
REMARK 500 1 SER A 558 -44.91 -133.87
REMARK 500 1 SER A 559 -80.36 -69.56
REMARK 500 1 TRP A 563 -168.90 -74.10
REMARK 500 1 LEU A 569 78.61 -160.34
REMARK 500 1 ALA A 571 80.49 71.61
REMARK 500 1 GLU A 573 148.24 -178.04
REMARK 500 1 PHE A 575 160.88 -36.45
REMARK 500 1 GLU A 583 -172.03 -69.85
REMARK 500 1 ASP A 585 -167.42 -113.22
REMARK 500 1 GLU A 591 134.17 -25.91
REMARK 500 1 SER A 592 -134.79 -69.75
REMARK 500 1 ASP A 593 -65.30 -91.76
REMARK 500 1 ASN A 595 -150.35 -65.21
REMARK 500 1 CYS A 604 -150.64 179.40
REMARK 500 1 THR A 606 -143.40 -103.62
REMARK 500 1 ALA A 609 -167.26 -169.59
REMARK 500 1 VAL A 611 98.19 -171.65
REMARK 500 2 ALA A 523 109.19 -161.19
REMARK 500 2 THR A 524 43.43 -86.72
REMARK 500 2 LEU A 540 34.28 -94.05
REMARK 500 2 ASP A 542 -65.86 82.20
REMARK 500 2 TRP A 543 45.27 -175.29
REMARK 500 2 ALA A 553 58.96 -143.20
REMARK 500 2 THR A 557 -55.70 -154.11
REMARK 500 2 SER A 558 -51.76 -147.27
REMARK 500 2 SER A 559 -81.26 -69.44
REMARK 500 2 TRP A 563 -170.50 -69.51
REMARK 500 2 LEU A 569 76.77 -156.65
REMARK 500 2 GLU A 573 145.80 172.69
REMARK 500 2 PHE A 575 170.50 -39.02
REMARK 500 2 ASP A 585 -168.08 -112.63
REMARK 500 2 GLU A 591 141.65 -28.98
REMARK 500 2 SER A 592 -145.29 -68.39
REMARK 500 2 PRO A 601 -157.74 -76.34
REMARK 500 2 GLN A 602 55.29 -147.28
REMARK 500 2 CYS A 604 -72.64 -94.79
REMARK 500 2 VAL A 611 109.91 -177.20
REMARK 500
REMARK 500 THIS ENTRY HAS 112 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 ARG A 581 0.19 SIDE CHAIN
REMARK 500 1 ARG A 596 0.25 SIDE CHAIN
REMARK 500 1 ARG A 616 0.22 SIDE CHAIN
REMARK 500 2 ARG A 581 0.31 SIDE CHAIN
REMARK 500 2 ARG A 596 0.29 SIDE CHAIN
REMARK 500 2 ARG A 616 0.09 SIDE CHAIN
REMARK 500 3 ARG A 581 0.08 SIDE CHAIN
REMARK 500 3 ARG A 596 0.26 SIDE CHAIN
REMARK 500 3 ARG A 616 0.25 SIDE CHAIN
REMARK 500 4 ARG A 581 0.27 SIDE CHAIN
REMARK 500 4 ARG A 596 0.12 SIDE CHAIN
REMARK 500 4 ARG A 616 0.30 SIDE CHAIN
REMARK 500 5 ARG A 581 0.22 SIDE CHAIN
REMARK 500 5 ARG A 596 0.31 SIDE CHAIN
REMARK 500 5 ARG A 616 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KUM RELATED DB: PDB
DBREF 1KUL A 509 616 UNP P69328 AMYG_ASPNG 533 640
SEQRES 1 A 108 CYS THR THR PRO THR ALA VAL ALA VAL THR PHE ASP LEU
SEQRES 2 A 108 THR ALA THR THR THR TYR GLY GLU ASN ILE TYR LEU VAL
SEQRES 3 A 108 GLY SER ILE SER GLN LEU GLY ASP TRP GLU THR SER ASP
SEQRES 4 A 108 GLY ILE ALA LEU SER ALA ASP LYS TYR THR SER SER ASP
SEQRES 5 A 108 PRO LEU TRP TYR VAL THR VAL THR LEU PRO ALA GLY GLU
SEQRES 6 A 108 SER PHE GLU TYR LYS PHE ILE ARG ILE GLU SER ASP ASP
SEQRES 7 A 108 SER VAL GLU TRP GLU SER ASP PRO ASN ARG GLU TYR THR
SEQRES 8 A 108 VAL PRO GLN ALA CYS GLY THR SER THR ALA THR VAL THR
SEQRES 9 A 108 ASP THR TRP ARG
HELIX 1 1 SER A 538 LEU A 540 5 3
SHEET 1 A 7 SER A 607 TRP A 615 0
SHEET 2 A 7 THR A 513 ALA A 523 1 N THR A 518 O ALA A 609
SHEET 3 A 7 PRO A 561 ALA A 571 -1 N VAL A 567 O VAL A 517
SHEET 4 A 7 ILE A 549 SER A 552 -1 N SER A 552 O TYR A 564
SHEET 5 A 7 ASN A 530 SER A 536 -1 N LEU A 533 O ILE A 549
SHEET 6 A 7 GLU A 573 ILE A 582 -1 N LYS A 578 O VAL A 534
SHEET 7 A 7 GLU A 589 GLU A 591 -1 N GLU A 589 O ARG A 581
SHEET 1 B 7 SER A 607 TRP A 615 0
SHEET 2 B 7 THR A 513 ALA A 523 1 N THR A 518 O ALA A 609
SHEET 3 B 7 PRO A 561 ALA A 571 -1 N VAL A 567 O VAL A 517
SHEET 4 B 7 ILE A 549 SER A 552 -1 N SER A 552 O TYR A 564
SHEET 5 B 7 ASN A 530 SER A 536 -1 N LEU A 533 O ILE A 549
SHEET 6 B 7 GLU A 573 ILE A 582 -1 N LYS A 578 O VAL A 534
SHEET 7 B 7 ARG A 596 VAL A 600 -1 N TYR A 598 O PHE A 575
SSBOND 1 CYS A 509 CYS A 604 1555 1555 2.02
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
