HEADER HYDROLASE 02-MAY-06 2GUY
TITLE ORTHORHOMBIC CRYSTAL STRUCTURE (SPACE GROUP P21212) OF ASPERGILLUS
TITLE 2 NIGER ALPHA-AMYLASE AT 1.6 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TAKA-AMYLASE A, TAA, 1,4- ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND 5 EC: 3.2.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE 3 ORGANISM_TAXID: 5062
KEYWDS (BETA-ALPHA) 8 BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VUJICIC ZAGAR
REVDAT 6 30-AUG-23 2GUY 1 HETSYN
REVDAT 5 29-JUL-20 2GUY 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 18-OCT-17 2GUY 1 REMARK
REVDAT 3 13-JUL-11 2GUY 1 VERSN
REVDAT 2 24-FEB-09 2GUY 1 VERSN
REVDAT 1 15-AUG-06 2GUY 0
JRNL AUTH A.VUJICIC-ZAGAR,B.W.DIJKSTRA
JRNL TITL MONOCLINIC CRYSTAL FORM OF ASPERGILLUS NIGER ALPHA-AMYLASE
JRNL TITL 2 IN COMPLEX WITH MALTOSE AT 1.8 ANGSTROMS RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 62 716 2006
JRNL REFN ESSN 1744-3091
JRNL PMID 16880540
JRNL DOI 10.1107/S1744309106024729
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 60711
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3245
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3418
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 183
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3686
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 564
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.79000
REMARK 3 B22 (A**2) : 1.08000
REMARK 3 B33 (A**2) : -0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.205
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3828 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5234 ; 1.483 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 475 ; 5.772 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;35.711 ;25.115
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 567 ;13.725 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;10.104 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 579 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2950 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1903 ; 0.217 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2703 ; 0.324 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 815 ; 0.172 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.030 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.235 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 98 ; 0.279 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2394 ; 1.158 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3805 ; 1.726 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1659 ; 1.482 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1429 ; 2.129 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 476
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5739 6.5953 18.7641
REMARK 3 T TENSOR
REMARK 3 T11: -0.0168 T22: -0.0169
REMARK 3 T33: -0.0373 T12: 0.0354
REMARK 3 T13: 0.0160 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.0247 L22: 0.8174
REMARK 3 L33: 0.6026 L12: -0.3997
REMARK 3 L13: 0.0484 L23: -0.2453
REMARK 3 S TENSOR
REMARK 3 S11: 0.1099 S12: 0.1992 S13: 0.0083
REMARK 3 S21: -0.0613 S22: -0.1166 S23: -0.0204
REMARK 3 S31: -0.0035 S32: -0.0366 S33: 0.0068
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2GUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91835
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PRODC
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65130
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 7TAA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.2M NA-ACETATE, 0.1M NA
REMARK 280 -CACODYLATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 51.39950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.61400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.39950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.61400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1252 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 477
REMARK 465 SER A 478
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 NZ LYS A 412 CE1 TYR A 419 2.02
REMARK 500 O HOH A 1147 O HOH A 1521 2.09
REMARK 500 O HOH A 1177 O HOH A 1443 2.12
REMARK 500 O HOH A 1311 O HOH A 1375 2.12
REMARK 500 OE1 GLU A 109 O HOH A 1452 2.13
REMARK 500 O HOH A 1112 O HOH A 1446 2.17
REMARK 500 OG SER A 422 ND2 ASN A 450 2.17
REMARK 500 O HOH A 1134 O HOH A 1566 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1227 O HOH A 1302 2555 2.03
REMARK 500 O HOH A 1428 O HOH A 1441 3556 2.13
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 ALA A 78 45.81 -79.57
REMARK 500 TRP A 83 61.50 -119.95
REMARK 500 GLN A 85 -34.80 -130.64
REMARK 500 ALA A 329 121.60 -36.03
REMARK 500 ASP A 340 126.94 -33.64
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 CA A 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 121 OD1
REMARK 620 2 GLU A 162 O 152.1
REMARK 620 3 ASP A 175 OD2 124.0 78.1
REMARK 620 4 ASP A 175 OD1 75.8 115.7 51.7
REMARK 620 5 HIS A 210 O 73.8 81.7 159.0 136.1
REMARK 620 6 HOH A1026 O 116.4 72.5 96.4 139.5 83.0
REMARK 620 7 HOH A1050 O 88.7 73.9 88.7 68.3 80.1 144.2
REMARK 620 8 HOH A1194 O 73.4 132.4 77.4 77.8 121.4 70.4 144.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7TAA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FAMILY 13 ALPHA AMYLASE FROM ASPERGILLUS
REMARK 900 ORYZAE IN COMPLEX WITH ACARBOSE
REMARK 900 RELATED ID: 6TAA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN A DIFFERENT CRYSTAL FORM
REMARK 900 RELATED ID: 2TAA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN A DIFFERENT CRYSTAL FORM
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CURRENTLY THERE IS NO AMINOACID SEQUENCE DATABASE REFERENCE
REMARK 999 AVAILABLE FOR THE PROTEIN
DBREF 2GUY A 1 478 UNP P0C1B3 AMYA1_ASPOR 22 499
SEQRES 1 A 478 ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE
SEQRES 2 A 478 LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR
SEQRES 3 A 478 THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY
SEQRES 4 A 478 GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE
SEQRES 5 A 478 GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL
SEQRES 6 A 478 THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA
SEQRES 7 A 478 TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN
SEQRES 8 A 478 GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER
SEQRES 9 A 478 SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP
SEQRES 10 A 478 VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER
SEQRES 11 A 478 SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN
SEQRES 12 A 478 ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU
SEQRES 13 A 478 ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN
SEQRES 14 A 478 THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL
SEQRES 15 A 478 VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL
SEQRES 16 A 478 SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL
SEQRES 17 A 478 LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS
SEQRES 18 A 478 ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY
SEQRES 19 A 478 ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP
SEQRES 20 A 478 GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN
SEQRES 21 A 478 ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR
SEQRES 22 A 478 ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER
SEQRES 23 A 478 THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO
SEQRES 24 A 478 ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS
SEQRES 25 A 478 ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO
SEQRES 26 A 478 ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY
SEQRES 27 A 478 ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY
SEQRES 28 A 478 TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER
SEQRES 29 A 478 ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR
SEQRES 30 A 478 GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP
SEQRES 31 A 478 ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER
SEQRES 32 A 478 GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY
SEQRES 33 A 478 ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR
SEQRES 34 A 478 ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR
SEQRES 35 A 478 VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET
SEQRES 36 A 478 ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS
SEQRES 37 A 478 LEU ALA GLY SER LYS ILE CYS SER SER SER
MODRES 2GUY ASN A 197 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET CA A 601 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 3 CA CA 2+
FORMUL 4 HOH *564(H2 O)
HELIX 1 1 THR A 2 ARG A 7 1 6
HELIX 2 2 LEU A 15 ALA A 20 1 6
HELIX 3 3 ASN A 31 GLN A 35 5 5
HELIX 4 4 THR A 41 LYS A 48 1 8
HELIX 5 5 LYS A 48 GLY A 54 1 7
HELIX 6 6 THR A 96 ARG A 110 1 15
HELIX 7 7 ALA A 128 VAL A 132 5 5
HELIX 8 8 ASP A 133 PHE A 137 5 5
HELIX 9 9 SER A 142 PHE A 146 5 5
HELIX 10 10 ASP A 157 CYS A 164 1 8
HELIX 11 11 LYS A 180 SER A 199 1 20
HELIX 12 12 THR A 207 VAL A 211 5 5
HELIX 13 13 GLN A 212 ASP A 214 5 3
HELIX 14 14 PHE A 215 GLY A 224 1 10
HELIX 15 15 ASP A 235 CYS A 240 1 6
HELIX 16 16 PRO A 241 VAL A 245 5 5
HELIX 17 17 ASN A 251 LYS A 263 1 13
HELIX 18 18 SER A 268 CYS A 283 1 16
HELIX 19 19 ASP A 285 LEU A 288 5 4
HELIX 20 20 ARG A 300 TYR A 304 5 5
HELIX 21 21 ASP A 307 ASN A 321 1 15
HELIX 22 22 GLY A 330 HIS A 334 5 5
HELIX 23 23 ALA A 346 GLY A 351 5 6
HELIX 24 24 SER A 356 ASP A 376 1 21
HELIX 25 25 GLU A 467 ALA A 470 5 4
SHEET 1 A 8 GLY A 248 VAL A 249 0
SHEET 2 A 8 TYR A 226 GLY A 229 1 N GLY A 229 O GLY A 248
SHEET 3 A 8 GLY A 202 ILE A 205 1 N ILE A 205 O ILE A 228
SHEET 4 A 8 TYR A 113 VAL A 118 1 N VAL A 118 O ARG A 204
SHEET 5 A 8 ALA A 59 ILE A 62 1 N ILE A 60 O MET A 115
SHEET 6 A 8 ILE A 11 LEU A 14 1 N LEU A 14 O TRP A 61
SHEET 7 A 8 ILE A 324 TYR A 328 1 O PRO A 325 N ILE A 11
SHEET 8 A 8 GLY A 290 THR A 291 1 N THR A 291 O ILE A 326
SHEET 1 B 2 THR A 66 GLN A 68 0
SHEET 2 B 2 GLN A 84 LEU A 90 -1 O GLN A 85 N ALA A 67
SHEET 1 C 3 TYR A 125 ASP A 126 0
SHEET 2 C 3 VAL A 171 LEU A 173 -1 O SER A 172 N TYR A 125
SHEET 3 C 3 LEU A 166 GLY A 167 -1 N LEU A 166 O LEU A 173
SHEET 1 D 6 TRP A 385 ASP A 390 0
SHEET 2 D 6 THR A 393 LYS A 398 -1 O ALA A 395 N TYR A 388
SHEET 3 D 6 ILE A 405 SER A 410 -1 O LEU A 409 N ILE A 394
SHEET 4 D 6 ARG A 461 PRO A 465 -1 O LEU A 463 N VAL A 406
SHEET 5 D 6 GLN A 433 GLU A 436 -1 N THR A 435 O TYR A 464
SHEET 6 D 6 THR A 441 THR A 444 -1 O VAL A 443 N LEU A 434
SHEET 1 E 2 TYR A 419 LEU A 423 0
SHEET 2 E 2 VAL A 451 MET A 455 -1 O MET A 455 N TYR A 419
SSBOND 1 CYS A 30 CYS A 38 1555 1555 2.13
SSBOND 2 CYS A 150 CYS A 164 1555 1555 2.49
SSBOND 3 CYS A 240 CYS A 283 1555 1555 2.04
SSBOND 4 CYS A 440 CYS A 475 1555 1555 2.05
LINK ND2 ASN A 197 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.46
LINK OD1 ASN A 121 CA CA A 601 1555 1555 2.38
LINK O GLU A 162 CA CA A 601 1555 1555 2.44
LINK OD2 ASP A 175 CA CA A 601 1555 1555 2.50
LINK OD1 ASP A 175 CA CA A 601 1555 1555 2.61
LINK O HIS A 210 CA CA A 601 1555 1555 2.41
LINK CA CA A 601 O HOH A1026 1555 1555 2.48
LINK CA CA A 601 O HOH A1050 1555 1555 2.51
LINK CA CA A 601 O HOH A1194 1555 1555 2.43
CISPEP 1 LYS A 138 PRO A 139 0 4.88
CISPEP 2 ASP A 340 PRO A 341 0 5.20
CRYST1 102.799 63.228 74.456 90.00 90.00 90.00 P 21 21 2 4
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 0.009728 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015816 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013431 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
