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PDBsum entry 3tnx

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Hydrolase PDB id
3tnx
Jmol
Contents
Protein chains
310 a.a.
Metals
_CL
Waters ×133
HEADER    HYDROLASE                               02-SEP-11   3TNX
TITLE     STRUCTURE OF THE PRECURSOR OF A THERMOSTABLE VARIANT OF PAPAIN AT 2.6
TITLE    2 ANGSTROEM RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PAPAIN;
COMPND   3 CHAIN: A, C;
COMPND   4 FRAGMENT: UNP RESIDUES 27-345;
COMPND   5 SYNONYM: PAPAYA PROTEINASE I, PPI;
COMPND   6 EC: 3.4.22.2;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CARICA PAPAYA;
SOURCE   3 ORGANISM_COMMON: MAMON;
SOURCE   4 ORGANISM_TAXID: 3649;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET30 EK/LIC
KEYWDS    HYDROLASE, CYTOPLASM FOR RECOMBINANT EXPRESSION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.ROY,D.CHOUDHURY,J.K.DATTAGUPTA,S.BISWAS
REVDAT   3   28-NOV-12 3TNX    1       JRNL
REVDAT   2   19-SEP-12 3TNX    1       JRNL
REVDAT   1   12-SEP-12 3TNX    0
JRNL        AUTH   S.ROY,D.CHOUDHURY,P.AICH,J.K.DATTAGUPTA,S.BISWAS
JRNL        TITL   THE STRUCTURE OF A THERMOSTABLE MUTANT OF PRO-PAPAIN REVEALS
JRNL        TITL 2 ITS ACTIVATION MECHANISM
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68  1591 2012
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   23151624
JRNL        DOI    10.1107/S0907444912038607
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.ROY,D.CHOUDHURY,C.CHAKRABARTI,S.BISWAS,J.K.DATTAGUPTA
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK   1  TITL 2 THE PRECURSOR PROTEIN OF A THERMOSTABLE VARIANT OF PAPAIN
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  67   634 2011
REMARK   1  REFN                   ESSN 1744-3091
REMARK   1  PMID   21543879
REMARK   1  DOI    10.1107/S1744309111010888
REMARK   2
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 2.62
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.92
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5
REMARK   3   NUMBER OF REFLECTIONS             : 20562
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) : 0.186
REMARK   3   R VALUE            (WORKING SET) : 0.183
REMARK   3   FREE R VALUE                     : 0.236
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1110
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) : 2.62
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1421
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.66
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860
REMARK   3   BIN FREE R VALUE SET COUNT          : 64
REMARK   3   BIN FREE R VALUE                    : 0.3440
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4945
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 133
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.18
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.38000
REMARK   3    B22 (A**2) : -1.19000
REMARK   3    B33 (A**2) : 0.82000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.15000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.316
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.256
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.261
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5071 ; 0.017 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6878 ; 1.643 ; 1.936
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   618 ; 6.157 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   257 ;36.607 ;24.241
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   823 ;21.601 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;23.040 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   706 ; 0.114 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3968 ; 0.007 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  3058 ; 0.741 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4903 ; 1.464 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2013 ; 2.306 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1975 ; 3.833 ; 4.500
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 : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    10        A    84
REMARK   3    RESIDUE RANGE :   A    85        A   107
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5720  -4.3530  12.8220
REMARK   3    T TENSOR
REMARK   3      T11:   0.1322 T22:   0.4267
REMARK   3      T33:   0.1086 T12:   0.0000
REMARK   3      T13:   0.0538 T23:  -0.0364
REMARK   3    L TENSOR
REMARK   3      L11:   2.3446 L22:   3.0061
REMARK   3      L33:   5.1055 L12:   0.3189
REMARK   3      L13:  -0.4320 L23:   0.3969
REMARK   3    S TENSOR
REMARK   3      S11:   0.0805 S12:  -0.0865 S13:  -0.0534
REMARK   3      S21:   0.0630 S22:  -0.0941 S23:   0.1261
REMARK   3      S31:   0.0059 S32:   0.2719 S33:   0.0137
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   108        A   319
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0900   2.0130  -2.7840
REMARK   3    T TENSOR
REMARK   3      T11:   0.0334 T22:   0.3406
REMARK   3      T33:   0.0330 T12:   0.0269
REMARK   3      T13:  -0.0172 T23:   0.0115
REMARK   3    L TENSOR
REMARK   3      L11:   2.8067 L22:   2.4551
REMARK   3      L33:   1.2169 L12:   0.6143
REMARK   3      L13:  -0.2709 L23:  -0.2387
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0001 S12:   0.2085 S13:   0.0765
REMARK   3      S21:  -0.0958 S22:   0.0034 S23:  -0.0424
REMARK   3      S31:  -0.0041 S32:   0.0146 S33:  -0.0033
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C    10        C    84
REMARK   3    RESIDUE RANGE :   C    85        C   107
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0720  -9.4650 -69.5410
REMARK   3    T TENSOR
REMARK   3      T11:   0.3937 T22:   0.6548
REMARK   3      T33:   0.1128 T12:   0.0506
REMARK   3      T13:   0.0062 T23:  -0.0549
REMARK   3    L TENSOR
REMARK   3      L11:   5.4621 L22:   1.9239
REMARK   3      L33:   5.6990 L12:   0.5089
REMARK   3      L13:  -2.6596 L23:  -0.7142
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0161 S12:  -0.2766 S13:  -0.1613
REMARK   3      S21:  -0.1344 S22:  -0.0748 S23:   0.2986
REMARK   3      S31:   0.1990 S32:   0.1448 S33:   0.0910
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 :   C   108        C   319
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3720 -15.9490 -50.5410
REMARK   3    T TENSOR
REMARK   3      T11:   0.3149 T22:   0.6703
REMARK   3      T33:   0.1303 T12:  -0.0666
REMARK   3      T13:   0.0618 T23:  -0.0140
REMARK   3    L TENSOR
REMARK   3      L11:   2.3996 L22:   6.5192
REMARK   3      L33:   3.4888 L12:   0.0277
REMARK   3      L13:  -0.0372 L23:  -2.4371
REMARK   3    S TENSOR
REMARK   3      S11:   0.1441 S12:  -0.3043 S13:  -0.0566
REMARK   3      S21:   0.7377 S22:  -0.1796 S23:   0.0573
REMARK   3      S31:  -0.2364 S32:   0.0156 S33:   0.0355
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : 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 3TNX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB067704.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : BM14
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9785
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21658
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6
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         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1PCI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8.0% PEG 3350, 0.1M NA-ACETATE PH 4.6,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       37.38750
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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     MET A   -43
REMARK 465     HIS A   -42
REMARK 465     HIS A   -41
REMARK 465     HIS A   -40
REMARK 465     HIS A   -39
REMARK 465     HIS A   -38
REMARK 465     HIS A   -37
REMARK 465     SER A   -36
REMARK 465     SER A   -35
REMARK 465     GLY A   -34
REMARK 465     LEU A   -33
REMARK 465     VAL A   -32
REMARK 465     PRO A   -31
REMARK 465     ARG A   -30
REMARK 465     GLY A   -29
REMARK 465     SER A   -28
REMARK 465     GLY A   -27
REMARK 465     MET A   -26
REMARK 465     LYS A   -25
REMARK 465     GLU A   -24
REMARK 465     THR A   -23
REMARK 465     ALA A   -22
REMARK 465     ALA A   -21
REMARK 465     ALA A   -20
REMARK 465     LYS A   -19
REMARK 465     PHE A   -18
REMARK 465     GLU A   -17
REMARK 465     ARG A   -16
REMARK 465     GLN A   -15
REMARK 465     HIS A   -14
REMARK 465     MET A   -13
REMARK 465     ASP A   -12
REMARK 465     SER A   -11
REMARK 465     PRO A   -10
REMARK 465     ASP A    -9
REMARK 465     LEU A    -8
REMARK 465     GLY A    -7
REMARK 465     THR A    -6
REMARK 465     ASP A    -5
REMARK 465     ASP A    -4
REMARK 465     ASP A    -3
REMARK 465     ASP A    -2
REMARK 465     LYS A    -1
REMARK 465     MET A     0
REMARK 465     ASP A     1
REMARK 465     PHE A     2
REMARK 465     SER A     3
REMARK 465     ILE A     4
REMARK 465     VAL A     5
REMARK 465     GLY A     6
REMARK 465     TYR A     7
REMARK 465     SER A     8
REMARK 465     GLN A     9
REMARK 465     MET C   -43
REMARK 465     HIS C   -42
REMARK 465     HIS C   -41
REMARK 465     HIS C   -40
REMARK 465     HIS C   -39
REMARK 465     HIS C   -38
REMARK 465     HIS C   -37
REMARK 465     SER C   -36
REMARK 465     SER C   -35
REMARK 465     GLY C   -34
REMARK 465     LEU C   -33
REMARK 465     VAL C   -32
REMARK 465     PRO C   -31
REMARK 465     ARG C   -30
REMARK 465     GLY C   -29
REMARK 465     SER C   -28
REMARK 465     GLY C   -27
REMARK 465     MET C   -26
REMARK 465     LYS C   -25
REMARK 465     GLU C   -24
REMARK 465     THR C   -23
REMARK 465     ALA C   -22
REMARK 465     ALA C   -21
REMARK 465     ALA C   -20
REMARK 465     LYS C   -19
REMARK 465     PHE C   -18
REMARK 465     GLU C   -17
REMARK 465     ARG C   -16
REMARK 465     GLN C   -15
REMARK 465     HIS C   -14
REMARK 465     MET C   -13
REMARK 465     ASP C   -12
REMARK 465     SER C   -11
REMARK 465     PRO C   -10
REMARK 465     ASP C    -9
REMARK 465     LEU C    -8
REMARK 465     GLY C    -7
REMARK 465     THR C    -6
REMARK 465     ASP C    -5
REMARK 465     ASP C    -4
REMARK 465     ASP C    -3
REMARK 465     ASP C    -2
REMARK 465     LYS C    -1
REMARK 465     MET C     0
REMARK 465     ASP C     1
REMARK 465     PHE C     2
REMARK 465     SER C     3
REMARK 465     ILE C     4
REMARK 465     VAL C     5
REMARK 465     GLY C     6
REMARK 465     TYR C     7
REMARK 465     SER C     8
REMARK 465     GLN C     9
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     TYR A  97    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     TYR C  97    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ASN C 102    CG   OD1  ND2
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 C    31     O    HOH C   346              2.09
REMARK 500   O    THR A   121     NH2  ARG A   281              2.09
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   OE2  GLU A    44     OE2  GLU C    44     1456     2.13
REMARK 500   OD1  ASP A    11     OE2  GLU A    98     2545     2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 225   CD    GLU A 225   OE2     0.095
REMARK 500    GLU A 242   CD    GLU A 242   OE2     0.079
REMARK 500    GLU C 154   CD    GLU C 154   OE2     0.086
REMARK 500    GLU C 225   CD    GLU C 225   OE2     0.085
REMARK 500    GLU C 242   CD    GLU C 242   OE2     0.085
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    VAL A  69   CB  -  CA  -  C   ANGL. DEV. = -11.5 DEGREES
REMARK 500    ARG A 281   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG A 281   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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    ASP A  11      152.20    146.38
REMARK 500    SER A  14      132.72   -170.39
REMARK 500    ASN A  60       57.46     78.13
REMARK 500    ALA A  87      -87.03     -5.77
REMARK 500    ASN A  89      116.14   -164.84
REMARK 500    THR A  91     -109.76    -28.64
REMARK 500    THR A  92       22.68   -179.68
REMARK 500    THR A  93       90.45     64.92
REMARK 500    GLU A  94     -175.72     62.20
REMARK 500    SER A  96       34.62     74.82
REMARK 500    GLU A  98       98.49     10.75
REMARK 500    GLU A  99      -70.10   -161.42
REMARK 500    VAL A 100      151.61    -48.07
REMARK 500    ASN A 102     -148.71    105.68
REMARK 500    ASP A 103     -162.52   -162.39
REMARK 500    ASP A 105       54.56    179.06
REMARK 500    ASP A 265       10.67   -155.47
REMARK 500    ASP C  11     -132.07   -124.89
REMARK 500    LEU C  12       74.56   -109.32
REMARK 500    GLU C  55      -92.47    -46.06
REMARK 500    ASN C  68     -158.21    -82.42
REMARK 500    ILE C  86      -63.11   -108.81
REMARK 500    ALA C  87      162.70     93.09
REMARK 500    ASN C  89      -88.63    -78.50
REMARK 500    TYR C  90        6.08     32.75
REMARK 500    THR C  91     -142.36     40.67
REMARK 500    THR C  93     -173.16     60.40
REMARK 500    GLU C  94     -143.20     57.22
REMARK 500    LEU C  95      -74.79   -102.32
REMARK 500    SER C  96       38.51    176.22
REMARK 500    TYR C  97      -72.65   -130.46
REMARK 500    LEU C 101     -145.20     43.24
REMARK 500    ASN C 102      142.82    162.12
REMARK 500    ASN C 107       66.25     16.41
REMARK 500    THR C 121     -176.51    -63.34
REMARK 500    HIS C 188     -165.52   -102.14
REMARK 500    TYR C 193       58.14   -166.97
REMARK 500    ARG C 200     -147.14    -77.65
REMARK 500    CYS C 202       91.92    -61.68
REMARK 500    GLN C 221      115.60    -31.06
REMARK 500    VAL C 257      -26.75   -142.25
REMARK 500    ASP C 265       17.94   -154.70
REMARK 500    LEU C 309      -36.05    -25.62
REMARK 500    SER C 312      117.69   -161.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLU C   94     LEU C   95                  146.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    THR A  93        23.9      L          L   OUTSIDE RANGE
REMARK 500    THR C  56        24.9      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 320
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 9PAP   RELATED DB: PDB
REMARK 900 MATURE DOMAIN OF PAPAIN
DBREF  3TNX A    1   319  UNP    P00784   PAPA1_CARPA     27    345
DBREF  3TNX C    1   319  UNP    P00784   PAPA1_CARPA     27    345
SEQADV 3TNX MET A  -43  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS A  -42  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS A  -41  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS A  -40  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS A  -39  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS A  -38  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS A  -37  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER A  -36  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER A  -35  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY A  -34  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LEU A  -33  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX VAL A  -32  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX PRO A  -31  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ARG A  -30  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY A  -29  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER A  -28  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY A  -27  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX MET A  -26  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LYS A  -25  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLU A  -24  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX THR A  -23  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA A  -22  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA A  -21  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA A  -20  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LYS A  -19  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX PHE A  -18  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLU A  -17  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ARG A  -16  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLN A  -15  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS A  -14  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX MET A  -13  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP A  -12  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER A  -11  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX PRO A  -10  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP A   -9  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LEU A   -8  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY A   -7  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX THR A   -6  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP A   -5  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP A   -4  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP A   -3  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP A   -2  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LYS A   -1  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX MET A    0  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA A  132  UNP  P00784    CYS   158 ENGINEERED MUTATION
SEQADV 3TNX SER A  139  UNP  P00784    VAL   165 ENGINEERED MUTATION
SEQADV 3TNX SER A  143  UNP  P00784    GLY   169 ENGINEERED MUTATION
SEQADV 3TNX ARG A  281  UNP  P00784    LYS   307 ENGINEERED MUTATION
SEQADV 3TNX MET C  -43  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS C  -42  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS C  -41  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS C  -40  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS C  -39  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS C  -38  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS C  -37  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER C  -36  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER C  -35  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY C  -34  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LEU C  -33  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX VAL C  -32  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX PRO C  -31  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ARG C  -30  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY C  -29  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER C  -28  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY C  -27  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX MET C  -26  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LYS C  -25  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLU C  -24  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX THR C  -23  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA C  -22  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA C  -21  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA C  -20  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LYS C  -19  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX PHE C  -18  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLU C  -17  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ARG C  -16  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLN C  -15  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX HIS C  -14  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX MET C  -13  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP C  -12  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX SER C  -11  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX PRO C  -10  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP C   -9  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LEU C   -8  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX GLY C   -7  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX THR C   -6  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP C   -5  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP C   -4  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP C   -3  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ASP C   -2  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX LYS C   -1  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX MET C    0  UNP  P00784              EXPRESSION TAG
SEQADV 3TNX ALA C  132  UNP  P00784    CYS   158 ENGINEERED MUTATION
SEQADV 3TNX SER C  139  UNP  P00784    VAL   165 ENGINEERED MUTATION
SEQADV 3TNX SER C  143  UNP  P00784    GLY   169 ENGINEERED MUTATION
SEQADV 3TNX ARG C  281  UNP  P00784    LYS   307 ENGINEERED MUTATION
SEQRES   1 A  363  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES   2 A  363  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE
SEQRES   3 A  363  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES   4 A  363  ASP ASP ASP LYS MET ASP PHE SER ILE VAL GLY TYR SER
SEQRES   5 A  363  GLN ASN ASP LEU THR SER THR GLU ARG LEU ILE GLN LEU
SEQRES   6 A  363  PHE GLU SER TRP MET LEU LYS HIS ASN LYS ILE TYR LYS
SEQRES   7 A  363  ASN ILE ASP GLU LYS ILE TYR ARG PHE GLU ILE PHE LYS
SEQRES   8 A  363  ASP ASN LEU LYS TYR ILE ASP GLU THR ASN LYS LYS ASN
SEQRES   9 A  363  ASN SER TYR TRP LEU GLY LEU ASN VAL PHE ALA ASP MET
SEQRES  10 A  363  SER ASN ASP GLU PHE LYS GLU LYS TYR THR GLY SER ILE
SEQRES  11 A  363  ALA GLY ASN TYR THR THR THR GLU LEU SER TYR GLU GLU
SEQRES  12 A  363  VAL LEU ASN ASP GLY ASP VAL ASN ILE PRO GLU TYR VAL
SEQRES  13 A  363  ASP TRP ARG GLN LYS GLY ALA VAL THR PRO VAL LYS ASN
SEQRES  14 A  363  GLN GLY SER CYS GLY SER ALA TRP ALA PHE SER ALA VAL
SEQRES  15 A  363  SER THR ILE GLU SER ILE ILE LYS ILE ARG THR GLY ASN
SEQRES  16 A  363  LEU ASN GLU TYR SER GLU GLN GLU LEU LEU ASP CYS ASP
SEQRES  17 A  363  ARG ARG SER TYR GLY CYS ASN GLY GLY TYR PRO TRP SER
SEQRES  18 A  363  ALA LEU GLN LEU VAL ALA GLN TYR GLY ILE HIS TYR ARG
SEQRES  19 A  363  ASN THR TYR PRO TYR GLU GLY VAL GLN ARG TYR CYS ARG
SEQRES  20 A  363  SER ARG GLU LYS GLY PRO TYR ALA ALA LYS THR ASP GLY
SEQRES  21 A  363  VAL ARG GLN VAL GLN PRO TYR ASN GLU GLY ALA LEU LEU
SEQRES  22 A  363  TYR SER ILE ALA ASN GLN PRO VAL SER VAL VAL LEU GLU
SEQRES  23 A  363  ALA ALA GLY LYS ASP PHE GLN LEU TYR ARG GLY GLY ILE
SEQRES  24 A  363  PHE VAL GLY PRO CYS GLY ASN LYS VAL ASP HIS ALA VAL
SEQRES  25 A  363  ALA ALA VAL GLY TYR GLY PRO ASN TYR ILE LEU ILE ARG
SEQRES  26 A  363  ASN SER TRP GLY THR GLY TRP GLY GLU ASN GLY TYR ILE
SEQRES  27 A  363  ARG ILE LYS ARG GLY THR GLY ASN SER TYR GLY VAL CYS
SEQRES  28 A  363  GLY LEU TYR THR SER SER PHE TYR PRO VAL LYS ASN
SEQRES   1 C  363  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES   2 C  363  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE
SEQRES   3 C  363  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES   4 C  363  ASP ASP ASP LYS MET ASP PHE SER ILE VAL GLY TYR SER
SEQRES   5 C  363  GLN ASN ASP LEU THR SER THR GLU ARG LEU ILE GLN LEU
SEQRES   6 C  363  PHE GLU SER TRP MET LEU LYS HIS ASN LYS ILE TYR LYS
SEQRES   7 C  363  ASN ILE ASP GLU LYS ILE TYR ARG PHE GLU ILE PHE LYS
SEQRES   8 C  363  ASP ASN LEU LYS TYR ILE ASP GLU THR ASN LYS LYS ASN
SEQRES   9 C  363  ASN SER TYR TRP LEU GLY LEU ASN VAL PHE ALA ASP MET
SEQRES  10 C  363  SER ASN ASP GLU PHE LYS GLU LYS TYR THR GLY SER ILE
SEQRES  11 C  363  ALA GLY ASN TYR THR THR THR GLU LEU SER TYR GLU GLU
SEQRES  12 C  363  VAL LEU ASN ASP GLY ASP VAL ASN ILE PRO GLU TYR VAL
SEQRES  13 C  363  ASP TRP ARG GLN LYS GLY ALA VAL THR PRO VAL LYS ASN
SEQRES  14 C  363  GLN GLY SER CYS GLY SER ALA TRP ALA PHE SER ALA VAL
SEQRES  15 C  363  SER THR ILE GLU SER ILE ILE LYS ILE ARG THR GLY ASN
SEQRES  16 C  363  LEU ASN GLU TYR SER GLU GLN GLU LEU LEU ASP CYS ASP
SEQRES  17 C  363  ARG ARG SER TYR GLY CYS ASN GLY GLY TYR PRO TRP SER
SEQRES  18 C  363  ALA LEU GLN LEU VAL ALA GLN TYR GLY ILE HIS TYR ARG
SEQRES  19 C  363  ASN THR TYR PRO TYR GLU GLY VAL GLN ARG TYR CYS ARG
SEQRES  20 C  363  SER ARG GLU LYS GLY PRO TYR ALA ALA LYS THR ASP GLY
SEQRES  21 C  363  VAL ARG GLN VAL GLN PRO TYR ASN GLU GLY ALA LEU LEU
SEQRES  22 C  363  TYR SER ILE ALA ASN GLN PRO VAL SER VAL VAL LEU GLU
SEQRES  23 C  363  ALA ALA GLY LYS ASP PHE GLN LEU TYR ARG GLY GLY ILE
SEQRES  24 C  363  PHE VAL GLY PRO CYS GLY ASN LYS VAL ASP HIS ALA VAL
SEQRES  25 C  363  ALA ALA VAL GLY TYR GLY PRO ASN TYR ILE LEU ILE ARG
SEQRES  26 C  363  ASN SER TRP GLY THR GLY TRP GLY GLU ASN GLY TYR ILE
SEQRES  27 C  363  ARG ILE LYS ARG GLY THR GLY ASN SER TYR GLY VAL CYS
SEQRES  28 C  363  GLY LEU TYR THR SER SER PHE TYR PRO VAL LYS ASN
HET     CL  A 320       1
HETNAM      CL CHLORIDE ION
FORMUL   3   CL    CL 1-
FORMUL   4  HOH   *133(H2 O)
HELIX    1   1 SER A   14  HIS A   29  1                                  16
HELIX    2   2 ASN A   35  ASN A   57  1                                  23
HELIX    3   3 SER A   74  THR A   83  1                                  10
HELIX    4   4 ARG A  115  GLY A  118  5                                   4
HELIX    5   5 SER A  131  GLY A  150  1                                  20
HELIX    6   6 SER A  156  ASP A  164  1                                   9
HELIX    7   7 TYR A  168  GLY A  172  5                                   5
HELIX    8   8 TYR A  174  TYR A  185  1                                  12
HELIX    9   9 ARG A  203  GLY A  208  5                                   6
HELIX   10  10 ASN A  224  ALA A  233  1                                  10
HELIX   11  11 GLY A  245  LEU A  250  1                                   6
HELIX   12  12 GLY A  305  LEU A  309  5                                   5
HELIX   13  13 THR C   15  HIS C   29  1                                  15
HELIX   14  14 ASN C   35  ASN C   57  1                                  23
HELIX   15  15 SER C   74  THR C   83  1                                  10
HELIX   16  16 ARG C  115  GLY C  118  5                                   4
HELIX   17  17 SER C  131  GLY C  150  1                                  20
HELIX   18  18 SER C  156  ASP C  164  1                                   9
HELIX   19  19 TYR C  168  GLY C  172  5                                   5
HELIX   20  20 TYR C  174  TYR C  185  1                                  12
HELIX   21  21 TYR C  189  TYR C  193  5                                   5
HELIX   22  22 CYS C  202  GLY C  208  5                                   7
HELIX   23  23 ASN C  224  ALA C  233  1                                  10
HELIX   24  24 GLY C  245  LEU C  250  1                                   6
HELIX   25  25 GLY C  305  LEU C  309  5                                   5
SHEET    1   A 6 TYR A  63  LEU A  65  0
SHEET    2   A 6 TYR A 251  PHE A 256 -1  O  GLY A 253   N  TRP A  64
SHEET    3   A 6 TYR A 293  LYS A 297  1  O  LYS A 297   N  PHE A 256
SHEET    4   A 6 TYR A 277  ARG A 281 -1  N  ILE A 278   O  ILE A 296
SHEET    5   A 6 HIS A 266  GLY A 274 -1  N  ALA A 269   O  ARG A 281
SHEET    6   A 6 VAL A 112  ASP A 113 -1  N  VAL A 112   O  TYR A 273
SHEET    1   B 6 TYR A  63  LEU A  65  0
SHEET    2   B 6 TYR A 251  PHE A 256 -1  O  GLY A 253   N  TRP A  64
SHEET    3   B 6 TYR A 293  LYS A 297  1  O  LYS A 297   N  PHE A 256
SHEET    4   B 6 TYR A 277  ARG A 281 -1  N  ILE A 278   O  ILE A 296
SHEET    5   B 6 HIS A 266  GLY A 274 -1  N  ALA A 269   O  ARG A 281
SHEET    6   B 6 VAL A 237  LEU A 241 -1  N  VAL A 237   O  ALA A 270
SHEET    1   C 2 GLY A 216  VAL A 220  0
SHEET    2   C 2 SER A 313  VAL A 317 -1  O  VAL A 317   N  GLY A 216
SHEET    1   D 6 TYR C  63  LEU C  65  0
SHEET    2   D 6 TYR C 251  PHE C 256 -1  O  GLY C 253   N  TRP C  64
SHEET    3   D 6 TYR C 293  LYS C 297  1  O  LYS C 297   N  PHE C 256
SHEET    4   D 6 TYR C 277  ARG C 281 -1  N  ILE C 280   O  ILE C 294
SHEET    5   D 6 HIS C 266  GLY C 274 -1  N  ALA C 269   O  ARG C 281
SHEET    6   D 6 VAL C 112  ASP C 113 -1  N  VAL C 112   O  TYR C 273
SHEET    1   E 8 TYR C  63  LEU C  65  0
SHEET    2   E 8 TYR C 251  PHE C 256 -1  O  GLY C 253   N  TRP C  64
SHEET    3   E 8 TYR C 293  LYS C 297  1  O  LYS C 297   N  PHE C 256
SHEET    4   E 8 TYR C 277  ARG C 281 -1  N  ILE C 280   O  ILE C 294
SHEET    5   E 8 HIS C 266  GLY C 274 -1  N  ALA C 269   O  ARG C 281
SHEET    6   E 8 VAL C 237  LEU C 241 -1  N  VAL C 237   O  ALA C 270
SHEET    7   E 8 SER C 313  VAL C 317 -1  O  PHE C 314   N  SER C 238
SHEET    8   E 8 GLY C 216  GLN C 219 -1  N  GLY C 216   O  VAL C 317
SSBOND   1 CYS A  129    CYS A  170                          1555   1555  2.12
SSBOND   2 CYS A  163    CYS A  202                          1555   1555  2.04
SSBOND   3 CYS A  260    CYS A  307                          1555   1555  2.15
SSBOND   4 CYS C  129    CYS C  170                          1555   1555  2.09
SSBOND   5 CYS C  163    CYS C  202                          1555   1555  2.07
SSBOND   6 CYS C  260    CYS C  307                          1555   1555  2.06
CISPEP   1 GLY A  258    PRO A  259          0         8.58
CISPEP   2 GLY C  258    PRO C  259          0        11.23
SITE     1 AC1  3 ASN A 191  THR A 192  CYS A 260
CRYST1   42.925   74.775  116.510  90.00  93.03  90.00 P 1 21 1      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      0.023296  0.000000  0.001231        0.00000
SCALE2      0.000000  0.013373  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008595        0.00000
      
PROCHECK
Go to PROCHECK summary
 References