Header list of 1ac0.pdb file
Complete list - 29 20 Bytes
HEADER HYDROLASE 10-FEB-97 1AC0
TITLE GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH
TITLE 2 CYCLODEXTRIN, NMR, MINIMIZED AVERAGE STRUCTURE
CAVEAT 1AC0 GLC B 2 HAS WRONG CHIRALITY AT ATOM C1 GLC B 5 HAS WRONG
CAVEAT 2 1AC0 CHIRALITY AT ATOM C1 GLC C 6 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 3 1AC0 GLC C 7 HAS WRONG CHIRALITY AT ATOM C1
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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 STRAIN: AB4.1;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5061;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PIGF;
SOURCE 8 EXPRESSION_SYSTEM_GENE: A. NIGER GLAA
KEYWDS HYDROLASE, STARCH BINDING DOMAIN
EXPDTA SOLUTION NMR
AUTHOR K.SORIMACHI,M.-F.LE GAL-COEFFET,G.WILLIAMSON,D.B.ARCHER,
AUTHOR 2 M.P.WILLIAMSON
REVDAT 4 29-JUL-20 1AC0 1 CAVEAT COMPND REMARK HET
REVDAT 4 2 1 HETNAM FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 19-MAY-09 1AC0 1 REMARK
REVDAT 2 24-FEB-09 1AC0 1 VERSN
REVDAT 1 07-JUL-97 1AC0 0
JRNL AUTH K.SORIMACHI,M.F.LE GAL-COEFFET,G.WILLIAMSON,D.B.ARCHER,
JRNL AUTH 2 M.P.WILLIAMSON
JRNL TITL SOLUTION STRUCTURE OF THE GRANULAR STARCH BINDING DOMAIN OF
JRNL TITL 2 ASPERGILLUS NIGER GLUCOAMYLASE BOUND TO BETA-CYCLODEXTRIN.
JRNL REF STRUCTURE V. 5 647 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9195884
JRNL DOI 10.1016/S0969-2126(97)00220-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.SORIMACHI,A.J.JACKS,M.F.LE GAL-COEFFET,G.WILLIAMSON,
REMARK 1 AUTH 2 D.B.ARCHER,M.P.WILLIAMSON
REMARK 1 TITL SOLUTION STRUCTURE OF THE GRANULAR STARCH BINDING DOMAIN OF
REMARK 1 TITL 2 GLUCOAMYLASE FROM ASPERGILLUS NIGER BY NUCLEAR MAGNETIC
REMARK 1 TITL 3 RESONANCE SPECTROSCOPY
REMARK 1 REF J.MOL.BIOL. V. 259 970 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE VALUES SHOWN IN THE TEMPERATURE
REMARK 3 FACTOR FIELD ARE ATOMIC RMSD VALUES OF 41 STRUCTURES TO THE
REMARK 3 UNMINIMIZED AVERAGE STRUCTURE.
REMARK 4
REMARK 4 1AC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170638.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : RANDOM FROM 81 GOOD STRUCTURES
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, B, C
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 C ILE A 531 H TYR A 532 1.17
REMARK 500 H ILE A 531 HE3 TRP A 563 1.30
REMARK 500 O GLY A 535 HB2 ASP A 542 1.32
REMARK 500 O GLY A 535 O LEU A 540 1.33
REMARK 500 C GLY A 535 HB2 ASP A 542 1.36
REMARK 500 HG2 PRO A 561 O2 GLC C 1 1.48
REMARK 500 O4 GLC B 4 O6 GLC B 5 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 556 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 564 CB - CG - CD1 ANGL. DEV. = -3.7 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 THR A 510 -62.74 -141.90
REMARK 500 THR A 511 -55.14 176.06
REMARK 500 ALA A 523 -133.03 -141.04
REMARK 500 THR A 524 102.88 177.76
REMARK 500 THR A 526 65.48 -108.76
REMARK 500 ASP A 542 -19.16 65.75
REMARK 500 GLU A 544 82.86 -170.01
REMARK 500 THR A 545 -13.26 -46.65
REMARK 500 SER A 558 -120.07 -75.92
REMARK 500 ASP A 560 54.60 176.20
REMARK 500 TRP A 563 93.58 19.21
REMARK 500 VAL A 565 154.80 174.15
REMARK 500 THR A 566 86.82 -157.56
REMARK 500 VAL A 567 -166.73 -116.46
REMARK 500 ALA A 571 -66.86 -162.46
REMARK 500 GLU A 573 -143.41 -162.23
REMARK 500 ASP A 585 -76.65 -98.77
REMARK 500 ASP A 586 -90.14 -65.47
REMARK 500 SER A 587 -129.60 -170.18
REMARK 500 GLU A 589 74.12 -154.06
REMARK 500 TRP A 590 86.26 -51.07
REMARK 500 GLU A 591 87.86 -62.94
REMARK 500 ASP A 593 -66.72 -90.06
REMARK 500 GLU A 597 88.33 -160.03
REMARK 500 ALA A 603 -172.21 -59.63
REMARK 500 THR A 606 63.80 -158.35
REMARK 500 ALA A 609 -147.50 -135.45
REMARK 500 VAL A 611 78.72 -160.06
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 ARG A 581 0.26 SIDE CHAIN
REMARK 500 ARG A 596 0.31 SIDE CHAIN
REMARK 500 ARG A 616 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AC0 A 509 616 UNP P04064 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
HET GLC B 1 21
HET GLC B 2 21
HET GLC B 3 21
HET GLC B 4 21
HET GLC B 5 21
HET GLC B 6 21
HET GLC B 7 21
HET GLC C 1 21
HET GLC C 2 21
HET GLC C 3 21
HET GLC C 4 21
HET GLC C 5 21
HET GLC C 6 21
HET GLC C 7 21
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
FORMUL 2 GLC 14(C6 H12 O6)
HELIX 1 1 THR A 545 ASP A 547 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
SSBOND 1 CYS A 509 CYS A 604 1555 1555 2.02
LINK O4 GLC B 1 C1 GLC B 2 1555 1555 1.40
LINK C1 GLC B 1 O4 GLC B 7 1555 1555 1.40
LINK O4 GLC B 2 C1 GLC B 3 1555 1555 1.40
LINK O4 GLC B 3 C1 GLC B 4 1555 1555 1.40
LINK O4 GLC B 4 C1 GLC B 5 1555 1555 1.40
LINK O4 GLC B 5 C1 GLC B 6 1555 1555 1.41
LINK O4 GLC B 6 C1 GLC B 7 1555 1555 1.40
LINK O4 GLC C 1 C1 GLC C 2 1555 1555 1.41
LINK C1 GLC C 1 O4 GLC C 7 1555 1555 1.40
LINK O4 GLC C 2 C1 GLC C 3 1555 1555 1.40
LINK O4 GLC C 3 C1 GLC C 4 1555 1555 1.40
LINK O4 GLC C 4 C1 GLC C 5 1555 1555 1.40
LINK O4 GLC C 5 C1 GLC C 6 1555 1555 1.40
LINK O4 GLC C 6 C1 GLC C 7 1555 1555 1.40
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
Complete list - 29 20 Bytes