spacer
spacer

PDBsum entry 3l2l

Go to PDB code: 
Top Page protein ligands metals links
Hydrolase PDB id
3l2l
Jmol
Contents
Protein chain
496 a.a.
Ligands
GLC-GLC-GLC-GLC
GLC-GLC-GLC-GLC-
GLC-GLC
GLC
Metals
_CL
_CA
Waters ×607
HEADER    HYDROLASE                               15-DEC-09   3L2L
TITLE     X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PIG PANCREATIC ALPHA-AMYLASE WITH
TITLE    2 LIMIT DEXTRIN AND OLIGOSACCHARIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PANCREATIC ALPHA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 16-511;
COMPND   5 SYNONYM: PA, 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND   6 EC: 3.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 OTHER_DETAILS: PANCREAS
KEYWDS    CATALYTIC DOMAIN, CARBOHYDRATE BINDING MODULE, OLIGOSACCHARIDE, LIMIT
KEYWDS   2 DEXTRIN, GLUCOSE, CARBOHYDRATE METABOLISM, GLYCOPROTEIN,
KEYWDS   3 GLYCOSIDASE, METAL-BINDING, PYRROLIDONE CARBOXYLIC ACID, SECRETED,
KEYWDS   4 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.B.LARSON,J.S.DAY,A.MCPHERSON
REVDAT   3   13-JUL-11 3L2L    1       VERSN
REVDAT   2   21-APR-10 3L2L    1       JRNL
REVDAT   1   14-APR-10 3L2L    0
JRNL        AUTH   S.B.LARSON,J.S.DAY,A.MCPHERSON
JRNL        TITL   X-RAY CRYSTALLOGRAPHIC ANALYSES OF PIG PANCREATIC
JRNL        TITL 2 ALPHA-AMYLASE WITH LIMIT DEXTRIN, OLIGOSACCHARIDE, AND
JRNL        TITL 3 ALPHA-CYCLODEXTRIN.
JRNL        REF    BIOCHEMISTRY                  V.  49  3101 2010
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   20222716
JRNL        DOI    10.1021/BI902183W
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.B.LARSON,A.GREENWOOD,D.CASCIO,J.DAY,A.MCPHERSON
REMARK   1  TITL   REFINED MOLECULAR STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE
REMARK   1  TITL 2 AT 2.1 A RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 235  1560 1994
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   A.MCPHERSON,A.RICH
REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC ANALYSIS OF SWINE PANCREAS
REMARK   1  TITL 2 ALPHA-AMYLASE
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V. 285   493 1972
REMARK   1  REFN                   ISSN 0006-3002
REMARK   2
REMARK   2 RESOLUTION.    2.11 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0089
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.01
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0
REMARK   3   NUMBER OF REFLECTIONS             : 47147
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) : 0.119
REMARK   3   R VALUE            (WORKING SET) : 0.115
REMARK   3   FREE R VALUE                     : 0.157
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 4749
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) : 2.11
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 438
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 12.22
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230
REMARK   3   BIN FREE R VALUE SET COUNT          : 55
REMARK   3   BIN FREE R VALUE                    : 0.3140
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3909
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 126
REMARK   3   SOLVENT ATOMS            : 584
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : 23.25
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.36000
REMARK   3    B22 (A**2) : -1.27000
REMARK   3    B33 (A**2) : -0.09000
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): 0.126
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.718
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4593 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  4197 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6337 ; 1.487 ; 1.948
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9517 ; 0.813 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   597 ; 6.044 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   231 ;35.877 ;24.113
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   708 ;14.545 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;19.778 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   672 ; 0.112 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5308 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  1149 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   942 ; 0.217 ; 0.300
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4191 ; 0.187 ; 0.300
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2259 ; 0.191 ; 0.500
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2710 ; 0.094 ; 0.500
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   693 ; 0.210 ; 0.500
REMARK   3   H-BOND (X...Y) OTHERS             (A):   523 ; 0.189 ; 0.500
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.070 ; 0.500
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.143 ; 0.300
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.176 ; 0.300
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.183 ; 0.500
REMARK   3   SYMMETRY H-BOND OTHERS            (A):     9 ; 0.159 ; 0.500
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):  2699 ; 2.322 ; 4.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1107 ; 0.595 ; 4.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4405 ; 3.372 ; 8.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1894 ; 4.199 ; 8.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1910 ; 5.443 ;10.000
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  : 14
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A    99
REMARK   3    RESIDUE RANGE :   A   169        A   403
REMARK   3    ORIGIN FOR THE GROUP (A):  38.8690  33.4020  44.6410
REMARK   3    T TENSOR
REMARK   3      T11:   0.0003 T22:   0.0067
REMARK   3      T33:   0.0022 T12:   0.0010
REMARK   3      T13:  -0.0001 T23:   0.0010
REMARK   3    L TENSOR
REMARK   3      L11:   0.6708 L22:   1.2826
REMARK   3      L33:   0.7013 L12:   0.1325
REMARK   3      L13:   0.0256 L23:   0.1581
REMARK   3    S TENSOR
REMARK   3      S11:   0.0097 S12:   0.0089 S13:  -0.0117
REMARK   3      S21:   0.0008 S22:  -0.0106 S23:  -0.0505
REMARK   3      S31:  -0.0037 S32:   0.0104 S33:   0.0010
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   100        A   168
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0470  49.8490  62.0530
REMARK   3    T TENSOR
REMARK   3      T11:   0.0721 T22:   0.0473
REMARK   3      T33:   0.0180 T12:   0.0042
REMARK   3      T13:  -0.0049 T23:  -0.0121
REMARK   3    L TENSOR
REMARK   3      L11:   3.6942 L22:   1.2806
REMARK   3      L33:   1.1122 L12:   0.9278
REMARK   3      L13:  -0.3768 L23:   0.0953
REMARK   3    S TENSOR
REMARK   3      S11:   0.0850 S12:  -0.2797 S13:   0.1308
REMARK   3      S21:   0.1699 S22:  -0.0458 S23:   0.0398
REMARK   3      S31:  -0.0847 S32:  -0.0160 S33:  -0.0393
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 :   A   404        A   496
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4380   9.0210  28.8980
REMARK   3    T TENSOR
REMARK   3      T11:   0.0107 T22:   0.0110
REMARK   3      T33:   0.0170 T12:   0.0052
REMARK   3      T13:  -0.0017 T23:  -0.0126
REMARK   3    L TENSOR
REMARK   3      L11:   1.6513 L22:   1.8641
REMARK   3      L33:   2.3054 L12:   0.0461
REMARK   3      L13:  -0.3235 L23:   0.0102
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0207 S12:   0.0523 S13:  -0.0932
REMARK   3      S21:  -0.0790 S22:  -0.0054 S23:  -0.0292
REMARK   3      S31:   0.1056 S32:   0.0275 S33:   0.0261
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 :   A   601        A   601
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4650  29.8860  71.0930
REMARK   3    T TENSOR
REMARK   3      T11:   0.0617 T22:   0.1799
REMARK   3      T33:   0.1959 T12:  -0.0489
REMARK   3      T13:   0.0092 T23:   0.1047
REMARK   3    L TENSOR
REMARK   3      L11:  10.8944 L22:  65.6258
REMARK   3      L33:   0.3561 L12:   7.8608
REMARK   3      L13:   1.5422 L23:   0.0041
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1424 S12:   0.3525 S13:   0.3914
REMARK   3      S21:   0.5451 S22:  -0.1157 S23:  -0.0860
REMARK   3      S31:  -0.0493 S32:   0.1746 S33:   0.2581
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   602        A   602
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6260  33.7470  72.2300
REMARK   3    T TENSOR
REMARK   3      T11:   0.2418 T22:   0.4034
REMARK   3      T33:   0.3828 T12:  -0.1134
REMARK   3      T13:  -0.0560 T23:   0.0562
REMARK   3    L TENSOR
REMARK   3      L11:   5.5020 L22:  17.6753
REMARK   3      L33:   0.1577 L12:  -9.8564
REMARK   3      L13:   0.9077 L23:  -1.6140
REMARK   3    S TENSOR
REMARK   3      S11:   0.1037 S12:  -0.0516 S13:  -0.6245
REMARK   3      S21:  -0.1657 S22:   0.0451 S23:   1.0500
REMARK   3      S31:   0.0345 S32:  -0.0369 S33:  -0.1488
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   603        A   603
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3680  38.9880  73.1750
REMARK   3    T TENSOR
REMARK   3      T11:   0.1311 T22:   0.0503
REMARK   3      T33:   0.0573 T12:  -0.0085
REMARK   3      T13:   0.0268 T23:   0.0051
REMARK   3    L TENSOR
REMARK   3      L11:  16.6733 L22:   0.3362
REMARK   3      L33:   1.0692 L12:  -2.3677
REMARK   3      L13:   4.2221 L23:  -0.5996
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0374 S12:  -0.0981 S13:   0.0884
REMARK   3      S21:   0.0052 S22:   0.0142 S23:  -0.0124
REMARK   3      S31:  -0.0082 S32:  -0.0251 S33:   0.0233
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   604        A   604
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0030  42.8810  72.9330
REMARK   3    T TENSOR
REMARK   3      T11:   0.1971 T22:   0.3942
REMARK   3      T33:   0.2879 T12:   0.1550
REMARK   3      T13:   0.0143 T23:   0.0404
REMARK   3    L TENSOR
REMARK   3      L11:  17.5005 L22:  13.0692
REMARK   3      L33:  24.1837 L12:  15.1231
REMARK   3      L13:  20.5723 L23:  17.7778
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0785 S12:  -0.7603 S13:   0.6253
REMARK   3      S21:  -0.0729 S22:  -0.6672 S23:   0.5459
REMARK   3      S31:  -0.0903 S32:  -0.8912 S33:   0.7456
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   701        A   701
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7310  42.2410  70.0000
REMARK   3    T TENSOR
REMARK   3      T11:   0.6617 T22:   1.9174
REMARK   3      T33:   0.7859 T12:   0.1492
REMARK   3      T13:  -0.2509 T23:   0.3966
REMARK   3    L TENSOR
REMARK   3      L11:   0.0004 L22:   0.0002
REMARK   3      L33:   0.0020 L12:   0.0002
REMARK   3      L13:   0.0007 L23:   0.0006
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0006 S12:  -0.0101 S13:   0.0124
REMARK   3      S21:   0.0079 S22:  -0.0048 S23:   0.0023
REMARK   3      S31:   0.0134 S32:  -0.0397 S33:   0.0054
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   702        A   702
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2530  38.9420  68.6760
REMARK   3    T TENSOR
REMARK   3      T11:   0.1249 T22:   0.0828
REMARK   3      T33:   0.1353 T12:  -0.0400
REMARK   3      T13:   0.0236 T23:  -0.0317
REMARK   3    L TENSOR
REMARK   3      L11:   0.0281 L22:   0.3178
REMARK   3      L33:  41.5545 L12:   0.0840
REMARK   3      L13:  -0.8230 L23:  -3.5372
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0196 S12:   0.0302 S13:  -0.0098
REMARK   3      S21:   0.0147 S22:   0.0503 S23:  -0.0093
REMARK   3      S31:  -0.6131 S32:  -0.2245 S33:  -0.0308
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   703        A   703
REMARK   3    ORIGIN FOR THE GROUP (A):  38.9690  37.5810  64.7540
REMARK   3    T TENSOR
REMARK   3      T11:   0.1181 T22:   0.0743
REMARK   3      T33:   0.0749 T12:  -0.0034
REMARK   3      T13:   0.0316 T23:  -0.0104
REMARK   3    L TENSOR
REMARK   3      L11:  31.4752 L22:   0.3339
REMARK   3      L33:   3.2985 L12:  -3.2410
REMARK   3      L13:   8.8442 L23:  -0.9226
REMARK   3    S TENSOR
REMARK   3      S11:   0.0066 S12:  -0.3667 S13:   0.1215
REMARK   3      S21:  -0.0021 S22:   0.0350 S23:  -0.0104
REMARK   3      S31:   0.1828 S32:   0.0514 S33:  -0.0416
REMARK   3
REMARK   3   TLS GROUP : 11
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   704        A   704
REMARK   3    ORIGIN FOR THE GROUP (A):  38.3890  36.8360  59.8110
REMARK   3    T TENSOR
REMARK   3      T11:   0.1003 T22:   0.0600
REMARK   3      T33:   0.0596 T12:  -0.0090
REMARK   3      T13:  -0.0105 T23:  -0.0007
REMARK   3    L TENSOR
REMARK   3      L11:  41.7595 L22:   0.0542
REMARK   3      L33:   0.0634 L12:   1.5043
REMARK   3      L13:  -1.6265 L23:  -0.0586
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0114 S12:   0.3045 S13:   0.0249
REMARK   3      S21:  -0.0003 S22:   0.0122 S23:   0.0012
REMARK   3      S31:   0.0019 S32:  -0.0115 S33:  -0.0008
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   705        A   705
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7480  37.5510  56.1690
REMARK   3    T TENSOR
REMARK   3      T11:   0.1025 T22:   0.0886
REMARK   3      T33:   0.2057 T12:  -0.0367
REMARK   3      T13:  -0.1310 T23:   0.0386
REMARK   3    L TENSOR
REMARK   3      L11:  10.4216 L22:   3.2509
REMARK   3      L33:  28.1879 L12:   0.0000
REMARK   3      L13:   9.5727 L23:   0.0000
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0583 S12:  -0.1827 S13:   0.0197
REMARK   3      S21:   0.0338 S22:   0.1012 S23:  -0.0124
REMARK   3      S31:   0.1036 S32:   0.2982 S33:  -0.0430
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   706        A   706
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8110  41.2260  67.4590
REMARK   3    T TENSOR
REMARK   3      T11:   0.2107 T22:   0.1197
REMARK   3      T33:   0.0388 T12:   0.0463
REMARK   3      T13:  -0.0411 T23:  -0.0220
REMARK   3    L TENSOR
REMARK   3      L11:  41.3493 L22:   4.0134
REMARK   3      L33:   1.8216 L12:  12.8821
REMARK   3      L13:  -8.6785 L23:  -2.7038
REMARK   3    S TENSOR
REMARK   3      S11:   0.0232 S12:   0.1274 S13:   0.3002
REMARK   3      S21:   0.0079 S22:   0.0399 S23:   0.0934
REMARK   3      S31:  -0.0045 S32:  -0.0293 S33:  -0.0632
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   801        A   801
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6310  53.1520  52.4440
REMARK   3    T TENSOR
REMARK   3      T11:   0.2093 T22:   0.1929
REMARK   3      T33:   0.1240 T12:  -0.1547
REMARK   3      T13:  -0.0747 T23:   0.0545
REMARK   3    L TENSOR
REMARK   3      L11:   1.7935 L22:  17.7789
REMARK   3      L33:   0.3508 L12:  -5.3308
REMARK   3      L13:   0.5762 L23:  -2.2787
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1861 S12:   0.0952 S13:   0.1081
REMARK   3      S21:  -0.0033 S22:   0.2427 S23:  -0.0064
REMARK   3      S31:   0.1034 S32:  -0.1238 S33:  -0.0566
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   : 1.40
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 3L2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-10.
REMARK 100 THE RCSB ID CODE IS RCSB056753.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-SEP-92
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 6.75
REMARK 200  NUMBER OF CRYSTALS USED        : 9
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : SUPPER GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SDMS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS DETECTOR SYSTEM
REMARK 200  DATA SCALING SOFTWARE          : SDMS DETECTOR SYSTEM
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47147
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.010
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.05200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.22
REMARK 200  COMPLETENESS FOR SHELL     (%) : 28.8
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.910
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 71.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.010 M CACODYLATE, 0.002 M CALCIUM
REMARK 280  CHLORIDE, PH 6.75, EVAPORATION, 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       35.29500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.39000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.41000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.39000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.29500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.41000
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: 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: 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  HH22  ARG A   424     O    HOH A   711              1.48
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    ARG A 195   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 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    TYR A  31      -57.98   -138.74
REMARK 500    MET A 102     -147.46   -107.58
REMARK 500    VAL A 163       45.73     35.33
REMARK 500    ASP A 317       49.49   -106.37
REMARK 500    SER A 414     -102.47   -137.77
REMARK 500    ASP A 433       30.43    -90.96
REMARK 500    ASN A 460       47.32   -104.68
REMARK 500    PRO A 486       40.53    -83.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1038        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH A1050        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH A1085        DISTANCE =  5.28 ANGSTROMS
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 501  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 158   O
REMARK 620 2 ASN A 100   OD1 155.2
REMARK 620 3 HIS A 201   O    78.6  76.6
REMARK 620 4 HOH A 767   O    76.2 101.8  80.9
REMARK 620 5 ASP A 167   OD2  80.1 124.7 158.4  90.7
REMARK 620 6 HOH A 760   O   123.8  70.4 124.5 148.1  71.3
REMARK 620 7 ASP A 167   OD1 119.0  81.9 138.6  69.3  52.6  78.8
REMARK 620 8 HOH A 852   O    75.3 100.7  85.9 150.4  92.1  59.1 133.1
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L2M   RELATED DB: PDB
REMARK 900 X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PIG PANCREATIC ALPHA-
REMARK 900 AMYLASE WITH ALPHA-CYCLODEXTRIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUE AT POSITION 426 IS A VARIANT AS LISTED IN UNP ENTRY
REMARK 999 P00690. PCA IS A POST-TRANSLATIONAL MODIFICATION.
DBREF  3L2L A    1   496  UNP    P00690   AMYP_PIG        16    511
SEQADV 3L2L PCA A    1  UNP  P00690    GLN    16 SEE REMARK 999
SEQADV 3L2L ASP A  411  UNP  P00690    ALA   426 SEE REMARK 999
SEQRES   1 A  496  PCA TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR
SEQRES   5 A  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU
SEQRES   7 A  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES   9 A  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES  10 A  496  TYR CYS ASN PRO GLY ASN ARG GLU PHE PRO ALA VAL PRO
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE GLN SER SER GLU TYR
SEQRES  20 A  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES  21 A  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES  23 A  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES  24 A  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS VAL ALA VAL
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES  27 A  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY
SEQRES  28 A  496  GLN ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLN
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES  32 A  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES  34 A  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES  36 A  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES  37 A  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN
SEQRES  38 A  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES  39 A  496  LYS LEU
MODRES 3L2L PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1      13
HET    GLC  A 604      23
HET    GLC  A 603      21
HET    GLC  A 602      21
HET    GLC  A 601      21
HET    GLC  A 705      23
HET    GLC  A 704      21
HET    GLC  A 703      20
HET    GLC  A 702      21
HET    GLC  A 701      21
HET    GLC  A 706      21
HET    GLC  A 801      24
HET     CA  A 501       1
HET     CL  A 502       1
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
FORMUL   1  PCA    C5 H7 N O3
FORMUL   2  GLC    11(C6 H12 O6)
FORMUL   5   CA    CA 2+
FORMUL   6   CL    CL 1-
FORMUL   7  HOH   *584(H2 O)
HELIX    1   1 ARG A   20  TYR A   31  1                                  12
HELIX    2   2 PRO A   57  GLN A   63  5                                   7
HELIX    3   3 ASN A   75  VAL A   89  1                                  15
HELIX    4   4 ASN A  120  ARG A  124  5                                   5
HELIX    5   5 SER A  132  PHE A  136  5                                   5
HELIX    6   6 ASP A  153  CYS A  160  1                                   8
HELIX    7   7 GLN A  161  VAL A  163  5                                   3
HELIX    8   8 LYS A  172  GLY A  190  1                                  19
HELIX    9   9 ALA A  198  MET A  202  5                                   5
HELIX   10  10 TRP A  203  ASP A  212  1                                  10
HELIX   11  11 GLN A  243  PHE A  248  5                                   6
HELIX   12  12 PHE A  256  ARG A  267  1                                  12
HELIX   13  13 LYS A  273  TRP A  280  5                                   8
HELIX   14  14 GLY A  281  GLY A  285  5                                   5
HELIX   15  15 PRO A  288  ASP A  290  5                                   3
HELIX   16  16 ASP A  300  GLY A  304  5                                   5
HELIX   17  17 GLY A  308  ILE A  312  5                                   5
HELIX   18  18 THR A  314  TRP A  316  5                                   3
HELIX   19  19 ASP A  317  HIS A  331  1                                  15
HELIX   20  20 CYS A  384  ARG A  387  5                                   4
HELIX   21  21 TRP A  388  ASP A  402  1                                  15
HELIX   22  22 GLU A  493  LYS A  495  5                                   3
SHEET    1   A 9 SER A  12  LEU A  16  0
SHEET    2   A 9 GLY A  39  VAL A  42  1  O  GLN A  41   N  VAL A  14
SHEET    3   A 9 ARG A  92  ALA A  97  1  O  TYR A  94   N  VAL A  40
SHEET    4   A 9 GLY A 193  ILE A 196  1  O  ARG A 195   N  ALA A  97
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 231   N  ILE A 196
SHEET    6   A 9 ARG A 252  THR A 254  1  O  ARG A 252   N  ILE A 230
SHEET    7   A 9 ALA A 292  VAL A 294  1  O  LEU A 293   N  VAL A 253
SHEET    8   A 9 PHE A 335  SER A 340  1  O  PHE A 335   N  VAL A 294
SHEET    9   A 9 SER A  12  LEU A  16  1  N  ILE A  13   O  VAL A 338
SHEET    1   B 2 HIS A 101  GLY A 104  0
SHEET    2   B 2 LEU A 165  ASP A 167 -1  O  LEU A 166   N  MET A 102
SHEET    1   C 2 ASN A 362  ASN A 363  0
SHEET    2   C 2 VAL A 366  ILE A 367 -1  O  VAL A 366   N  ASN A 363
SHEET    1   D 4 PHE A 406  ASP A 411  0
SHEET    2   D 4 GLN A 416  ARG A 421 -1  O  GLY A 420   N  ALA A 407
SHEET    3   D 4 GLY A 425  ASN A 430 -1  O  PHE A 429   N  VAL A 417
SHEET    4   D 4 PHE A 487  HIS A 491 -1  O  ILE A 490   N  PHE A 426
SHEET    1   E 2 LEU A 436  GLN A 441  0
SHEET    2   E 2 THR A 474  ILE A 479 -1  O  ALA A 475   N  LEU A 440
SHEET    1   F 2 GLY A 447  CYS A 450  0
SHEET    2   F 2 LYS A 466  VAL A 469 -1  O  VAL A 469   N  GLY A 447
SHEET    1   G 2 LYS A 457  VAL A 458  0
SHEET    2   G 2 SER A 461  CYS A 462 -1  O  SER A 461   N  VAL A 458
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.02
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.04
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.04
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.04
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.34
LINK         O4 AGLC A 704                 C1 AGLC A 703     1555   1555  1.43
LINK         O4 AGLC A 703                 C1 AGLC A 702     1555   1555  1.44
LINK         O6 AGLC A 703                 C1 AGLC A 706     1555   1555  1.44
LINK         O4 AGLC A 705                 C1 AGLC A 704     1555   1555  1.45
LINK         O4 AGLC A 604                 C1 AGLC A 603     1555   1555  1.45
LINK         O4 AGLC A 702                 C1 AGLC A 701     1555   1555  1.45
LINK         O4 AGLC A 603                 C1 AGLC A 602     1555   1555  1.46
LINK         O4 AGLC A 602                 C1 AGLC A 601     1555   1555  1.48
LINK         O   ARG A 158                CA    CA A 501     1555   1555  2.32
LINK         OD1 ASN A 100                CA    CA A 501     1555   1555  2.40
LINK         O   HIS A 201                CA    CA A 501     1555   1555  2.42
LINK        CA    CA A 501                 O   HOH A 767     1555   1555  2.42
LINK         OD2 ASP A 167                CA    CA A 501     1555   1555  2.45
LINK        CA    CA A 501                 O   HOH A 760     1555   1555  2.47
LINK         OD1 ASP A 167                CA    CA A 501     1555   1555  2.52
LINK        CA    CA A 501                 O   HOH A 852     1555   1555  2.54
CISPEP   1 ASN A   53    PRO A   54          0        -5.34
CISPEP   2 VAL A  129    PRO A  130          0        -5.00
SITE     1 AC1  5 ALA A 108  HOH A 569  HOH A 570  GLC A 603
SITE     2 AC1  5 HOH A 606
SITE     1 AC2  7 THR A  52  ASN A  53  GLU A 272  ASN A 279
SITE     2 AC2  7 GLC A 602  GLC A 604  HOH A 696
SITE     1 AC3 11 THR A  52  ASN A  53  LYS A 261  TRP A 284
SITE     2 AC3 11 GLY A 285  HOH A 573  HOH A 574  GLC A 601
SITE     3 AC3 11 GLC A 603  HOH A 979  HOH A 998
SITE     1 AC4  9 ASN A  53  PRO A  54  HOH A 530  HOH A 571
SITE     2 AC4  9 HOH A 572  GLC A 602  HOH A 979  HOH A1034
SITE     3 AC4  9 HOH A1035
SITE     1 AC5 12 TYR A  62  HIS A 101  ASP A 197  ALA A 198
SITE     2 AC5 12 GLU A 233  ILE A 235  ASP A 300  HOH A 552
SITE     3 AC5 12 HOH A 582  HOH A 583  HOH A 584  GLC A 704
SITE     1 AC6 10 TRP A  58  TRP A  59  TYR A  62  GLN A  63
SITE     2 AC6 10 ASP A 300  HOH A 582  HOH A 584  GLC A 703
SITE     3 AC6 10 GLC A 705  HOH A1023
SITE     1 AC7  5 GLN A  63  VAL A 163  GLC A 702  GLC A 704
SITE     2 AC7  5 GLC A 706
SITE     1 AC8  3 HOH A 578  GLC A 701  GLC A 703
SITE     1 AC9  8 GLY A 147  HOH A 550  HOH A 551  HOH A 575
SITE     2 AC9  8 HOH A 576  HOH A 577  HOH A 622  GLC A 702
SITE     1 BC1 11 TRP A  59  GLN A  63  GLY A 104  SER A 105
SITE     2 BC1 11 GLY A 106  ALA A 107  HOH A 579  HOH A 580
SITE     3 BC1 11 HOH A 581  HOH A 679  GLC A 703
SITE     1 BC2  8 LYS A 140  GLU A 171  TRP A 203  ASP A 206
SITE     2 BC2  8 HOH A 778  HOH A 805  HOH A 949  HOH A1093
SITE     1 BC3  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 BC3  7 HOH A 760  HOH A 767  HOH A 852
SITE     1 BC4  3 ARG A 195  ASN A 298  ARG A 337
CRYST1   70.590  114.820  118.780  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      0.014166  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008709  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008419        0.00000
      
PROCHECK
Go to PROCHECK summary
 References