HEADER HYDROLASE 11-DEC-07 3BLP
TITLE ROLE OF AROMATIC RESIDUES IN HUMAN SALIVARY ALPHA-AMYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE 1;
COMPND 3 CHAIN: X;
COMPND 4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE 1, SALIVARY ALPHA-
COMPND 5 AMYLASE;
COMPND 6 EC: 3.2.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AMY1A, AMY1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS TIM BARREL, GREEK KEY BARREL, CARBOHYDRATE METABOLISM, CHLORIDE,
KEYWDS 2 GLYCOPROTEIN, GLYCOSIDASE, HYDROLASE, METAL-BINDING, PYRROLIDONE
KEYWDS 3 CARBOXYLIC ACID, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR N.RAMASUBBU
REVDAT 7 30-AUG-23 3BLP 1 REMARK
REVDAT 6 20-OCT-21 3BLP 1 SEQADV HETSYN LINK
REVDAT 5 29-JUL-20 3BLP 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 25-DEC-19 3BLP 1 SEQADV SEQRES LINK
REVDAT 3 13-JUL-11 3BLP 1 VERSN
REVDAT 2 24-FEB-09 3BLP 1 VERSN
REVDAT 1 18-NOV-08 3BLP 0
JRNL AUTH C.RAGUNATH,C.KASINATHAN,S.G.A.MANUEL,N.RAMASUBBU
JRNL TITL STRUCTURE-FUNCTION RELATIONSHIPS IN HUMAN SALIVARY
JRNL TITL 2 ALPHA-AMYLASE: ROLE OF AROMATIC RESIDUES IN A SECONDARY
JRNL TITL 3 BINDING SITE
JRNL REF BIOLOGIA V. 63 1028 2008
JRNL REFN ISSN 0006-3088
JRNL DOI 10.2478/S11756-008-0163-3
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 64253
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3405
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4500
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 238
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3937
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 32.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.24000
REMARK 3 B22 (A**2) : 0.42000
REMARK 3 B33 (A**2) : -0.66000
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): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.545
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4113 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5589 ; 1.352 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 495 ; 5.960 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;36.695 ;23.762
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 622 ;12.279 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.977 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 575 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3230 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1816 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2813 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 270 ; 0.121 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.057 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 34 ; 0.152 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.158 ; 0.200
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): 2500 ; 0.822 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3940 ; 1.290 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1865 ; 1.981 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1649 ; 2.917 ; 4.500
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 99
REMARK 3 RESIDUE RANGE : X 170 X 400
REMARK 3 RESIDUE RANGE : X 498 X 498
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0210 58.0340 17.7490
REMARK 3 T TENSOR
REMARK 3 T11: -0.0477 T22: -0.0758
REMARK 3 T33: 0.0946 T12: -0.0019
REMARK 3 T13: -0.0022 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.3949 L22: 0.3922
REMARK 3 L33: 0.2966 L12: 0.0689
REMARK 3 L13: 0.0787 L23: 0.0365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.0262 S13: -0.0014
REMARK 3 S21: -0.0163 S22: -0.0029 S23: 0.0071
REMARK 3 S31: 0.0096 S32: -0.0190 S33: -0.0149
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 100 X 169
REMARK 3 RESIDUE RANGE : X 497 X 497
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4060 34.9550 13.0480
REMARK 3 T TENSOR
REMARK 3 T11: -0.0207 T22: -0.1108
REMARK 3 T33: 0.1387 T12: -0.0259
REMARK 3 T13: -0.0403 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 2.3755 L22: 0.4962
REMARK 3 L33: 0.5653 L12: 0.0327
REMARK 3 L13: 0.0154 L23: -0.0503
REMARK 3 S TENSOR
REMARK 3 S11: 0.1177 S12: -0.0926 S13: -0.2753
REMARK 3 S21: -0.0585 S22: -0.0307 S23: 0.0321
REMARK 3 S31: 0.1879 S32: -0.0359 S33: -0.0870
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 401 X 496
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8090 80.9770 27.0730
REMARK 3 T TENSOR
REMARK 3 T11: -0.0484 T22: -0.0944
REMARK 3 T33: 0.0993 T12: -0.0139
REMARK 3 T13: 0.0002 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 1.4519 L22: 0.7931
REMARK 3 L33: 1.2288 L12: -0.1416
REMARK 3 L13: 0.1786 L23: -0.0020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: -0.0727 S13: 0.1228
REMARK 3 S21: -0.0104 S22: -0.0080 S23: -0.0841
REMARK 3 S31: -0.0983 S32: 0.0103 S33: -0.0241
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 502 X 506
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3590 43.6610 21.8000
REMARK 3 T TENSOR
REMARK 3 T11: -0.0137 T22: 0.0137
REMARK 3 T33: 0.0267 T12: -0.0308
REMARK 3 T13: -0.0329 T23: -0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 18.3024 L22: 6.5390
REMARK 3 L33: 1.8283 L12: 2.0703
REMARK 3 L13: -4.8090 L23: -2.4309
REMARK 3 S TENSOR
REMARK 3 S11: 0.3484 S12: -0.3295 S13: -0.0275
REMARK 3 S21: 0.2115 S22: -0.2094 S23: 0.0438
REMARK 3 S31: 0.2271 S32: 0.4871 S33: -0.1390
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 3BLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000045673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9777
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64253
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
REMARK 200 R SYM FOR SHELL (I) : 0.43900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1SMD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% MPD, 0.1M TRIS.HCL, 10 MM CALCIUM
REMARK 280 CHLORIDE, PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.04250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.34500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.43650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.34500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.04250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.43650
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, 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 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 CB CYS X 450 O HOH X 665 2.09
REMARK 500 O HOH X 568 O HOH X 740 2.11
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 TYR X 31 -54.70 -140.22
REMARK 500 MET X 102 -142.46 -100.12
REMARK 500 ASP X 317 64.45 -109.22
REMARK 500 SER X 414 -107.53 -134.18
REMARK 500 ASP X 433 32.37 -84.98
REMARK 500 ASN X 459 49.54 37.35
REMARK 500 PRO X 486 49.56 -86.52
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 X 497 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN X 100 OD1
REMARK 620 2 ARG X 158 O 157.5
REMARK 620 3 ASP X 167 OD1 80.1 117.0
REMARK 620 4 ASP X 167 OD2 125.2 77.0 52.0
REMARK 620 5 HIS X 201 O 76.2 81.3 138.8 157.8
REMARK 620 6 HOH X 518 O 71.4 124.9 75.8 72.2 125.7
REMARK 620 7 HOH X 525 O 101.1 73.9 70.1 87.5 81.8 145.9
REMARK 620 8 HOH X 542 O 104.4 73.6 137.0 96.3 82.0 65.9 145.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SMD RELATED DB: PDB
REMARK 900 RELATED ID: 1MFV RELATED DB: PDB
REMARK 900 RELATED ID: 1MFU RELATED DB: PDB
REMARK 900 RELATED ID: 3BLK RELATED DB: PDB
DBREF 3BLP X 1 496 UNP P04745 AMY1_HUMAN 16 511
SEQADV 3BLP ALA X 388 UNP P04745 TRP 403 ENGINEERED MUTATION
SEQRES 1 X 496 PCA TYR SER SER ASN THR GLN GLN GLY ARG THR SER ILE
SEQRES 2 X 496 VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES 3 X 496 GLU CYS GLU ARG TYR LEU ALA PRO LYS GLY PHE GLY GLY
SEQRES 4 X 496 VAL GLN VAL SER PRO PRO ASN GLU ASN VAL ALA ILE HIS
SEQRES 5 X 496 ASN PRO PHE ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES 6 X 496 SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASP GLU
SEQRES 7 X 496 PHE ARG ASN MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES 8 X 496 ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES 9 X 496 ASN ALA VAL SER ALA GLY THR SER SER THR CYS GLY SER
SEQRES 10 X 496 TYR PHE ASN PRO GLY SER ARG ASP PHE PRO ALA VAL PRO
SEQRES 11 X 496 TYR SER GLY TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 X 496 GLY SER GLY ASP ILE GLU ASN TYR ASN ASP ALA THR GLN
SEQRES 13 X 496 VAL ARG ASP CYS ARG LEU SER GLY LEU LEU ASP LEU ALA
SEQRES 14 X 496 LEU GLY LYS ASP TYR VAL ARG SER LYS ILE ALA GLU TYR
SEQRES 15 X 496 MET ASN HIS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES 16 X 496 ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES 17 X 496 ALA ILE LEU ASP LYS LEU HIS ASN LEU ASN SER ASN TRP
SEQRES 18 X 496 PHE PRO GLU GLY SER LYS PRO PHE ILE TYR GLN GLU VAL
SEQRES 19 X 496 ILE ASP LEU GLY GLY GLU PRO ILE LYS SER SER ASP TYR
SEQRES 20 X 496 PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES 21 X 496 LYS LEU GLY THR VAL ILE ARG LYS TRP ASN GLY GLU LYS
SEQRES 22 X 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 X 496 MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 X 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE
SEQRES 25 X 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS MET ALA VAL
SEQRES 26 X 496 GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES 27 X 496 MET SER SER TYR ARG TRP PRO ARG TYR PHE GLU ASN GLY
SEQRES 28 X 496 LYS ASP VAL ASN ASP TRP VAL GLY PRO PRO ASN ASP ASN
SEQRES 29 X 496 GLY VAL THR LYS GLU VAL THR ILE ASN PRO ASP THR THR
SEQRES 30 X 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG ALA ARG GLN
SEQRES 31 X 496 ILE ARG ASN MET VAL ASN PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 X 496 GLN PRO PHE THR ASN TRP TYR ASP ASN GLY SER ASN GLN
SEQRES 33 X 496 VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES 34 X 496 ASN ASN ASP ASP TRP THR PHE SER LEU THR LEU GLN THR
SEQRES 35 X 496 GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 X 496 ASP LYS ILE ASN GLY ASN CYS THR GLY ILE LYS ILE TYR
SEQRES 37 X 496 VAL SER ASP ASP GLY LYS ALA HIS PHE SER ILE SER ASN
SEQRES 38 X 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 X 496 LYS LEU
MODRES 3BLP PCA X 1 GLN PYROGLUTAMIC ACID
HET PCA X 1 8
HET GLC A 1 11
HET AGL A 2 10
HET GLC B 1 12
HET AGL B 2 10
HET CA X 497 1
HET CL X 498 1
HET HMC X 504 11
HETNAM PCA PYROGLUTAMIC ACID
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM AGL 4-AMINO-4,6-DIDEOXY-ALPHA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM HMC 5-HYDROXYMETHYL-CHONDURITOL
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN AGL 4,6-DIDEOXY-4-AMINO-ALPHA-D-GLUCOSE; 4-AMINO-4-DEOXY-
HETSYN 2 AGL ALPHA-D-QUINOVOPYRANOSE; 4-AMINO-4,6-DIDEOXY-ALPHA-D-
HETSYN 3 AGL GLUCOSE; 4-AMINO-4,6-DIDEOXY-D-GLUCOSE; 4-AMINO-4,6-
HETSYN 4 AGL DIDEOXY-GLUCOSE
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 GLC 2(C6 H12 O6)
FORMUL 2 AGL 2(C6 H13 N O4)
FORMUL 4 CA CA 2+
FORMUL 5 CL CL 1-
FORMUL 6 HMC C7 H12 O5
FORMUL 7 HOH *323(H2 O)
HELIX 1 1 ARG X 20 TYR X 31 1 12
HELIX 2 2 PRO X 57 GLN X 63 5 7
HELIX 3 3 ASN X 75 VAL X 89 1 15
HELIX 4 4 ASN X 120 ARG X 124 5 5
HELIX 5 5 SER X 132 PHE X 136 5 5
HELIX 6 6 ASP X 153 CYS X 160 1 8
HELIX 7 7 ARG X 161 SER X 163 5 3
HELIX 8 8 LYS X 172 GLY X 190 1 19
HELIX 9 9 ALA X 198 MET X 202 5 5
HELIX 10 10 TRP X 203 ASP X 212 1 10
HELIX 11 11 LYS X 243 PHE X 248 5 6
HELIX 12 12 PHE X 256 LYS X 268 1 13
HELIX 13 13 LYS X 273 TRP X 280 5 8
HELIX 14 14 GLY X 281 GLY X 285 5 5
HELIX 15 15 ASP X 300 GLY X 304 5 5
HELIX 16 16 THR X 314 TRP X 316 5 3
HELIX 17 17 ASP X 317 HIS X 331 1 15
HELIX 18 18 CYS X 384 ARG X 387 5 4
HELIX 19 19 ALA X 388 VAL X 401 1 14
HELIX 20 20 GLU X 493 LYS X 495 5 3
SHEET 1 A 9 SER X 12 LEU X 16 0
SHEET 2 A 9 GLY X 39 VAL X 42 1 O GLN X 41 N VAL X 14
SHEET 3 A 9 ARG X 92 ALA X 97 1 O TYR X 94 N VAL X 40
SHEET 4 A 9 GLY X 193 ILE X 196 1 O ARG X 195 N ALA X 97
SHEET 5 A 9 PHE X 229 GLN X 232 1 O PHE X 229 N PHE X 194
SHEET 6 A 9 ARG X 252 THR X 254 1 O ARG X 252 N ILE X 230
SHEET 7 A 9 ALA X 292 VAL X 294 1 O LEU X 293 N VAL X 253
SHEET 8 A 9 PHE X 335 SER X 340 1 O PHE X 335 N VAL X 294
SHEET 9 A 9 SER X 12 LEU X 16 1 N HIS X 15 O VAL X 338
SHEET 1 B 2 HIS X 101 GLY X 104 0
SHEET 2 B 2 LEU X 165 ASP X 167 -1 O LEU X 166 N CYS X 103
SHEET 1 C 2 PHE X 348 GLU X 349 0
SHEET 2 C 2 LYS X 352 ASP X 353 -1 O LYS X 352 N GLU X 349
SHEET 1 D 2 ASN X 362 ASP X 363 0
SHEET 2 D 2 VAL X 366 THR X 367 -1 O VAL X 366 N ASP X 363
SHEET 1 E 4 PHE X 406 ASP X 411 0
SHEET 2 E 4 GLN X 416 ARG X 421 -1 O GLY X 420 N THR X 407
SHEET 3 E 4 GLY X 425 ASN X 430 -1 O PHE X 429 N VAL X 417
SHEET 4 E 4 PHE X 487 HIS X 491 -1 O ILE X 488 N VAL X 428
SHEET 1 F 2 PHE X 436 GLN X 441 0
SHEET 2 F 2 LYS X 474 ILE X 479 -1 O ALA X 475 N LEU X 440
SHEET 1 G 2 GLY X 447 CYS X 450 0
SHEET 2 G 2 LYS X 466 VAL X 469 -1 O ILE X 467 N TYR X 449
SHEET 1 H 2 LYS X 457 ILE X 458 0
SHEET 2 H 2 ASN X 461 CYS X 462 -1 O ASN X 461 N ILE X 458
SSBOND 1 CYS X 28 CYS X 86 1555 1555 2.07
SSBOND 2 CYS X 70 CYS X 115 1555 1555 2.08
SSBOND 3 CYS X 141 CYS X 160 1555 1555 2.08
SSBOND 4 CYS X 378 CYS X 384 1555 1555 2.02
SSBOND 5 CYS X 450 CYS X 462 1555 1555 2.06
LINK C PCA X 1 N TYR X 2 1555 1555 1.34
LINK O4 HMC X 504 C1 GLC A 1 1555 1555 1.34
LINK C1 HMC X 504 N4 AGL B 2 1555 1555 1.31
LINK O4 GLC A 1 C1 AGL A 2 1555 1555 1.44
LINK O4 GLC B 1 C1 AGL B 2 1555 1555 1.45
LINK OD1 ASN X 100 CA CA X 497 1555 1555 2.39
LINK O ARG X 158 CA CA X 497 1555 1555 2.35
LINK OD1 ASP X 167 CA CA X 497 1555 1555 2.54
LINK OD2 ASP X 167 CA CA X 497 1555 1555 2.47
LINK O HIS X 201 CA CA X 497 1555 1555 2.36
LINK CA CA X 497 O HOH X 518 1555 1555 2.55
LINK CA CA X 497 O HOH X 525 1555 1555 2.44
LINK CA CA X 497 O HOH X 542 1555 1555 2.49
CISPEP 1 ASN X 53 PRO X 54 0 -3.50
CISPEP 2 VAL X 129 PRO X 130 0 -6.46
CRYST1 52.085 74.873 134.690 90.00 90.00 90.00 P 21 21 21 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 0.019199 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013356 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007424 0.00000
HETATM 1 N PCA X 1 12.458 58.662 0.631 1.00 22.57 N
HETATM 2 CA PCA X 1 11.912 58.194 1.915 1.00 22.26 C
HETATM 3 CB PCA X 1 12.130 56.683 2.024 1.00 21.97 C
HETATM 4 CG PCA X 1 13.376 56.410 1.198 1.00 23.48 C
HETATM 5 CD PCA X 1 13.273 57.527 0.205 1.00 22.99 C
HETATM 6 OE PCA X 1 13.820 57.486 -0.906 1.00 26.29 O
HETATM 7 C PCA X 1 12.566 58.843 3.115 1.00 22.22 C
HETATM 8 O PCA X 1 12.136 58.618 4.239 1.00 22.16 O
(ATOM LINES ARE NOT SHOWN.)
END