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PDBsum entry 1tmq

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Top Page protein metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
1tmq
Jmol
Contents
Protein chains
471 a.a.
117 a.a.
Metals
_CA
_CL
Waters ×331
HEADER    HYDROLASE/HYDROLASE INHIBITOR           13-JAN-98   1TMQ
TITLE     STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN
TITLE    2 COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (ALPHA-AMYLASE);
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.1;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: PROTEIN (RAGI BIFUNCTIONAL INHIBITOR);
COMPND   7 CHAIN: B
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TENEBRIO MOLITOR;
SOURCE   3 ORGANISM_COMMON: YELLOW MEALWORM;
SOURCE   4 ORGANISM_TAXID: 7067;
SOURCE   5 TISSUE: LARVAE;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: ELEUSINE CORACANA;
SOURCE   8 ORGANISM_COMMON: FINGER MILLET;
SOURCE   9 ORGANISM_TAXID: 4511;
SOURCE  10 ORGAN: SEED
KEYWDS    ALPHA-AMYLASE, CARBOHYDRATE METABOLISM, ALPHA-1, 4-GLUCAN-4-
KEYWDS   2 GLUCANOHYDROLASE, HYDROLASE BIFUNCTIONAL ALPHA-
KEYWDS   3 AMYLASE/TRYPSIN INHIBITOR, COMPLEX (ENZYME/ INHIBITOR),
KEYWDS   4 HYDROLASE/HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    F.X.GOMIS-RUETH,S.STROBL,R.GLOCKSHUBER
REVDAT   3   24-FEB-09 1TMQ    1       VERSN
REVDAT   2   29-DEC-99 1TMQ    4       HEADER COMPND REMARK JRNL
REVDAT   2 2                   4       ATOM   SOURCE SEQRES
REVDAT   1   02-MAR-99 1TMQ    0
JRNL        AUTH   S.STROBL,K.MASKOS,G.WIEGAND,R.HUBER,F.X.GOMIS-RUTH,
JRNL        AUTH 2 R.GLOCKSHUBER
JRNL        TITL   A NOVEL STRATEGY FOR INHIBITION OF ALPHA-AMYLASES:
JRNL        TITL 2 YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE
JRNL        TITL 3 RAGI BIFUNCTIONAL INHIBITOR AT 2.5 A RESOLUTION.
JRNL        REF    STRUCTURE                     V.   6   911 1998
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   9687373
JRNL        DOI    10.1016/S0969-2126(98)00092-6
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.STROBL,F.X.GOMIS-RUTH,K.MASKOS,G.FRANK,R.HUBER,
REMARK   1  AUTH 2 R.GLOCKSHUBER
REMARK   1  TITL   THE ALPHA-AMYLASE FROM THE YELLOW MEAL WORM:
REMARK   1  TITL 2 COMPLETE PRIMARY STRUCTURE, CRYSTALLIZATION AND
REMARK   1  TITL 3 PRELIMINARY X-RAY ANALYSIS
REMARK   1  REF    FEBS LETT.                    V. 409   109 1997
REMARK   1  REFN                   ISSN 0014-5793
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 26825
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREE R FACTOR
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.191
REMARK   3   FREE R VALUE                     : 0.261
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4487
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 3
REMARK   3   SOLVENT ATOMS            : 330
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1TMQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-99.
REMARK 100 THE RCSB ID CODE IS RCSB008384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
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                  : GRAPHITE CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM V. 5.30
REMARK 200  DATA SCALING SOFTWARE          : CCP4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28178
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : 0.09300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.28400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1BIP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM AMMONIUM PHOSPHATE, 100MM
REMARK 280  TRIS-HCL, PH 8.5, 50% (W/V) 2-METHYL-2,4- PENTANEDIOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.77000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.77000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.58000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       93.43500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.58000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       93.43500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.77000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.58000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       93.43500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       55.77000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.58000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       93.43500
REMARK 290   SMTRY3   8  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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE ALPHA-AMYLASE N-TERMINUS BLOCKS AGAINST
REMARK 400 AMINOPEPTIDASE ACTIVITY BY GLUTAMINE CYCLIZATION TO RENDER
REMARK 400 PYROGLUTAMATE
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    SER A  12      143.89     76.12
REMARK 500    PHE A  31      -50.02   -135.34
REMARK 500    ASN A  68      101.96   -167.95
REMARK 500    MET A 100     -123.91   -116.72
REMARK 500    ASN A 137        3.98   -151.82
REMARK 500    ASN A 266       32.69    -97.00
REMARK 500    ASP A 350      -75.22     -5.32
REMARK 500    ASP A 351       32.39    -73.97
REMARK 500    ASN A 352       22.11     47.42
REMARK 500    ASP A 390     -113.54   -165.45
REMARK 500    VAL B 502      -94.12     65.12
REMARK 500    MET B 510     -109.30   -127.22
REMARK 500    MET B 564      -72.23    -68.56
REMARK 500    LEU B 579       68.26    -69.14
REMARK 500    GLU B 602     -112.00    -96.51
REMARK 500    LEU B 615     -174.56    -66.88
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 B1035        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH B1133        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH B1134        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH A1141        DISTANCE =  5.48 ANGSTROMS
REMARK 525    HOH A1144        DISTANCE =  7.68 ANGSTROMS
REMARK 525    HOH A1163        DISTANCE =  5.85 ANGSTROMS
REMARK 525    HOH A1172        DISTANCE =  6.85 ANGSTROMS
REMARK 525    HOH A1198        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH A1199        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH A1200        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH A1201        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH A1203        DISTANCE =  7.48 ANGSTROMS
REMARK 525    HOH A1284        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH A1291        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH A1314        DISTANCE =  6.06 ANGSTROMS
REMARK 525    HOH A1317        DISTANCE =  6.38 ANGSTROMS
REMARK 525    HOH A1319        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A1324        DISTANCE =  8.46 ANGSTROMS
REMARK 525    HOH A1330        DISTANCE =  5.55 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 A1001  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 146   O
REMARK 620 2 HIS A 189   O    81.3
REMARK 620 3 ASN A  98   OD1 154.8  76.6
REMARK 620 4 ASP A 155   CG   98.3 161.6  98.8
REMARK 620 5 ASP A 155   OD1 109.9 138.0  79.7  25.3
REMARK 620 6 ASP A 155   OD2  83.4 164.7 118.5  24.8  50.0
REMARK 620 7 HOH A1049   O    68.0  85.3  97.9  77.6  64.1  90.1
REMARK 620 8 HOH A5011   O    82.2  83.7 107.1 114.6 136.8  93.1 149.5
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 CL A 1002
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001
DBREF  1TMQ A    1   471  UNP    P56634   AMY_TENMO        2    471
DBREF  1TMQ B  501   617  UNP    P01087   IAAT_ELECO       1    117
SEQADV 1TMQ PCA A    1  UNP  P56634    GLN     1 MODIFIED RESIDUE
SEQADV 1TMQ SER B  570  UNP  P01087    PRO    70 CONFLICT
SEQRES   1 A  471  PCA LYS ASP ALA ASN PHE ALA SER GLY ARG ASN SER ILE
SEQRES   2 A  471  VAL HIS LEU PHE GLU TRP LYS TRP ASN ASP ILE ALA ASP
SEQRES   3 A  471  GLU CYS GLU ARG PHE LEU GLN PRO GLN GLY PHE GLY GLY
SEQRES   4 A  471  VAL GLN ILE SER PRO PRO ASN GLU TYR LEU VAL ALA ASP
SEQRES   5 A  471  GLY ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL SER TYR
SEQRES   6 A  471  ILE ILE ASN THR ARG SER GLY ASP GLU SER ALA PHE THR
SEQRES   7 A  471  ASP MET THR ARG ARG CYS ASN ASP ALA GLY VAL ARG ILE
SEQRES   8 A  471  TYR VAL ASP ALA VAL ILE ASN HIS MET THR GLY MET ASN
SEQRES   9 A  471  GLY VAL GLY THR SER GLY SER SER ALA ASP HIS ASP GLY
SEQRES  10 A  471  MET ASN TYR PRO ALA VAL PRO TYR GLY SER GLY ASP PHE
SEQRES  11 A  471  HIS SER PRO CYS GLU VAL ASN ASN TYR GLN ASP ALA ASP
SEQRES  12 A  471  ASN VAL ARG ASN CYS GLU LEU VAL GLY LEU ARG ASP LEU
SEQRES  13 A  471  ASN GLN GLY SER ASP TYR VAL ARG GLY VAL LEU ILE ASP
SEQRES  14 A  471  TYR MET ASN HIS MET ILE ASP LEU GLY VAL ALA GLY PHE
SEQRES  15 A  471  ARG VAL ASP ALA ALA LYS HIS MET SER PRO GLY ASP LEU
SEQRES  16 A  471  SER VAL ILE PHE SER GLY LEU LYS ASN LEU ASN THR ASP
SEQRES  17 A  471  TYR GLY PHE ALA ASP GLY ALA ARG PRO PHE ILE TYR GLN
SEQRES  18 A  471  GLU VAL ILE ASP LEU GLY GLY GLU ALA ILE SER LYS ASN
SEQRES  19 A  471  GLU TYR THR GLY PHE GLY CYS VAL LEU GLU PHE GLN PHE
SEQRES  20 A  471  GLY VAL SER LEU GLY ASN ALA PHE GLN GLY GLY ASN GLN
SEQRES  21 A  471  LEU LYS ASN LEU ALA ASN TRP GLY PRO GLU TRP GLY LEU
SEQRES  22 A  471  LEU GLU GLY LEU ASP ALA VAL VAL PHE VAL ASP ASN HIS
SEQRES  23 A  471  ASP ASN GLN ARG THR GLY GLY SER GLN ILE LEU THR TYR
SEQRES  24 A  471  LYS ASN PRO LYS PRO TYR LYS MET ALA ILE ALA PHE MET
SEQRES  25 A  471  LEU ALA HIS PRO TYR GLY THR THR ARG ILE MET SER SER
SEQRES  26 A  471  PHE ASP PHE THR ASP ASN ASP GLN GLY PRO PRO GLN ASP
SEQRES  27 A  471  GLY SER GLY ASN LEU ILE SER PRO GLY ILE ASN ASP ASP
SEQRES  28 A  471  ASN THR CYS SER ASN GLY TYR VAL CYS GLU HIS ARG TRP
SEQRES  29 A  471  ARG GLN VAL TYR GLY MET VAL GLY PHE ARG ASN ALA VAL
SEQRES  30 A  471  GLU GLY THR GLN VAL GLU ASN TRP TRP SER ASN ASP ASP
SEQRES  31 A  471  ASN GLN ILE ALA PHE SER ARG GLY SER GLN GLY PHE VAL
SEQRES  32 A  471  ALA PHE THR ASN GLY GLY ASP LEU ASN GLN ASN LEU ASN
SEQRES  33 A  471  THR GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER
SEQRES  34 A  471  GLY GLU LEU SER GLY GLY SER CYS THR GLY LYS SER VAL
SEQRES  35 A  471  THR VAL GLY ASP ASN GLY SER ALA ASP ILE SER LEU GLY
SEQRES  36 A  471  SER ALA GLU ASP ASP GLY VAL LEU ALA ILE HIS VAL ASN
SEQRES  37 A  471  ALA LYS LEU
SEQRES   1 B  117  SER VAL GLY THR SER CYS ILE PRO GLY MET ALA ILE PRO
SEQRES   2 B  117  HIS ASN PRO LEU ASP SER CYS ARG TRP TYR VAL SER THR
SEQRES   3 B  117  ARG THR CYS GLY VAL GLY PRO ARG LEU ALA THR GLN GLU
SEQRES   4 B  117  MET LYS ALA ARG CYS CYS ARG GLN LEU GLU ALA ILE PRO
SEQRES   5 B  117  ALA TYR CYS ARG CYS GLU ALA VAL ARG ILE LEU MET ASP
SEQRES   6 B  117  GLY VAL VAL THR SER SER GLY GLN HIS GLU GLY ARG LEU
SEQRES   7 B  117  LEU GLN ASP LEU PRO GLY CYS PRO ARG GLN VAL GLN ARG
SEQRES   8 B  117  ALA PHE ALA PRO LYS LEU VAL THR GLU VAL GLU CYS ASN
SEQRES   9 B  117  LEU ALA THR ILE HIS GLY GLY PRO PHE CYS LEU SER LEU
MODRES 1TMQ PCA A    1  GLU  PYROGLUTAMIC ACID
HET    PCA  A   1       8
HET     CL  A1002       1
HET     CA  A1001       1
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM      CL CHLORIDE ION
HETNAM      CA CALCIUM ION
FORMUL   1  PCA    C5 H7 N O3
FORMUL   3   CL    CL 1-
FORMUL   4   CA    CA 2+
FORMUL   5  HOH   *331(H2 O)
HELIX    1   1 TRP A   21  ARG A   30  1                                  10
HELIX    2   2 TRP A   56  TYR A   60  5                                   5
HELIX    3   3 GLU A   74  ASP A   86  1                                  13
HELIX    4   4 SER A  127  ASP A  129  5                                   3
HELIX    5   5 ALA A  142  ASN A  147  1                                   6
HELIX    6   6 ASP A  161  ASP A  176  1                                  16
HELIX    7   7 ALA A  187  HIS A  189  5                                   3
HELIX    8   8 PRO A  192  GLY A  201  1                                  10
HELIX    9   9 THR A  207  TYR A  209  5                                   3
HELIX   10  10 LYS A  233  GLU A  235  5                                   3
HELIX   11  11 PHE A  245  GLN A  256  1                                  12
HELIX   12  12 LEU A  261  ASN A  266  5                                   6
HELIX   13  13 PRO A  269  TRP A  271  5                                   3
HELIX   14  14 GLY A  276  ASP A  278  5                                   3
HELIX   15  15 ASN A  288  THR A  291  1                                   4
HELIX   16  16 TYR A  299  ALA A  314  5                                  16
HELIX   17  17 GLU A  361  ARG A  363  5                                   3
HELIX   18  18 ARG A  365  ALA A  376  1                                  12
HELIX   19  19 VAL B  502  SER B  505  5                                   4
HELIX   20  20 ASP B  518  CYS B  529  5                                  12
HELIX   21  21 THR B  537  GLU B  549  1                                  13
HELIX   22  22 ALA B  553  ASP B  565  1                                  13
HELIX   23  23 ARG B  587  VAL B  598  1                                  12
SHEET    1   A 6 ARG A 321  SER A 324  0
SHEET    2   A 6 ILE A  13  LEU A  16  1  N  ILE A  13   O  ILE A 322
SHEET    3   A 6 GLY A  39  GLN A  41  1  N  GLY A  39   O  VAL A  14
SHEET    4   A 6 ARG A  90  ALA A  95  1  N  ARG A  90   O  VAL A  40
SHEET    5   A 6 GLY A 181  VAL A 184  1  N  GLY A 181   O  VAL A  93
SHEET    6   A 6 PHE A 218  GLN A 221  1  N  PHE A 218   O  PHE A 182
SHEET    1   B 2 GLY A 347  ASN A 349  0
SHEET    2   B 2 THR A 353  SER A 355 -1  N  SER A 355   O  GLY A 347
SHEET    1   C 3 GLN A 392  SER A 396  0
SHEET    2   C 3 GLY A 401  THR A 406 -1  N  PHE A 405   O  ILE A 393
SHEET    3   C 3 VAL A 462  HIS A 466 -1  N  ILE A 465   O  PHE A 402
SHEET    1   D 2 LEU A 411  ASN A 416  0
SHEET    2   D 2 SER A 449  LEU A 454 -1  N  LEU A 454   O  LEU A 411
SHEET    1   E 2 GLY A 422  CYS A 425  0
SHEET    2   E 2 SER A 441  VAL A 444 -1  N  VAL A 444   O  GLY A 422
SSBOND   1 CYS A   28    CYS A   84                          1555   1555  2.03
SSBOND   2 CYS A  134    CYS A  148                          1555   1555  2.03
SSBOND   3 CYS A  354    CYS A  360                          1555   1555  2.02
SSBOND   4 CYS A  425    CYS A  437                          1555   1555  2.02
SSBOND   5 CYS B  506    CYS B  555                          1555   1555  2.03
SSBOND   6 CYS B  520    CYS B  544                          1555   1555  2.04
SSBOND   7 CYS B  529    CYS B  585                          1555   1555  2.03
SSBOND   8 CYS B  545    CYS B  603                          1555   1555  2.02
SSBOND   9 CYS B  557    CYS B  614                          1555   1555  2.03
LINK         C   PCA A   1                 N   LYS A   2     1555   1555  1.32
LINK        CA    CA A1001                 O   ARG A 146     1555   1555  2.28
LINK        CA    CA A1001                 O   HIS A 189     1555   1555  2.40
LINK         OD1 ASN A  98                CA    CA A1001     1555   1555  2.42
LINK         CG  ASP A 155                CA    CA A1001     1555   1555  2.92
LINK         OD1 ASP A 155                CA    CA A1001     1555   1555  2.67
LINK         OD2 ASP A 155                CA    CA A1001     1555   1555  2.46
LINK        CA    CA A1001                 O   HOH A1049     1555   1555  2.57
LINK        CA    CA A1001                 O   HOH A5011     1555   1555  2.09
CISPEP   1 VAL A  123    PRO A  124          0        -0.93
SITE     1 AC1  5 ARG A 183  LEU A 243  ASN A 285  ARG A 321
SITE     2 AC1  5 HOH A1067
SITE     1 AC2  6 ASN A  98  ARG A 146  ASP A 155  HIS A 189
SITE     2 AC2  6 HOH A1049  HOH A5011
CRYST1   79.160  186.870  111.540  90.00  90.00  90.00 C 2 2 21      8
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      0.012633  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005351  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008965        0.00000
      
PROCHECK
Go to PROCHECK summary
 References