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PDBsum entry 1q4n

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Hydrolase PDB id
1q4n
Jmol
Contents
Protein chain
496 a.a. *
Ligands
TAM
Metals
_CA
_CL
Waters ×324
* Residue conservation analysis
HEADER    HYDROLASE                               04-AUG-03   1Q4N
TITLE     STRUCTURAL STUDIES OF PHE256TRP OF HUMAN SALIVARY ALPHA-
TITLE    2 AMYLASE: IMPLICATIONS FOR THE ROLE OF A CONSERVED WATER
TITLE    3 MOLECULE AND ITS ASSOCIATED CHAIN IN ENZYME ACTIVITY
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE, SALIVARY;
COMPND   3 CHAIN: X;
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND   5 EC: 3.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AMY1A OR AMY1;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVL1392
KEYWDS    AMYLASE, MUTAGENESIS, TRIS, INHIBITOR, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.RAMASUBBU
REVDAT   3   24-FEB-09 1Q4N    1       VERSN
REVDAT   2   25-JAN-05 1Q4N    1       TITLE
REVDAT   1   16-MAR-04 1Q4N    0
JRNL        AUTH   N.RAMASUBBU,K.SUNDAR,C.RAGUNATH,M.M.RAFI
JRNL        TITL   STRUCTURAL STUDIES OF A PHE256TRP MUTANT OF HUMAN
JRNL        TITL 2 SALIVARY ALPHA-AMYLASE: IMPLICATIONS FOR THE ROLE
JRNL        TITL 3 OF A CONSERVED WATER MOLECULE IN ENZYME ACTIVITY
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 421   115 2004
JRNL        REFN                   ISSN 0003-9861
JRNL        PMID   14678792
JRNL        DOI    10.1016/J.ABB.2003.10.007
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.07 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
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) : 2.07
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.17
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0
REMARK   3   NUMBER OF REFLECTIONS             : 29010
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) : 0.159
REMARK   3   R VALUE            (WORKING SET) : 0.156
REMARK   3   FREE R VALUE                     : 0.206
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1551
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) : 2.07
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.12
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1221
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3710
REMARK   3   BIN FREE R VALUE SET COUNT          : 73
REMARK   3   BIN FREE R VALUE                    : 0.4210
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3949
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 13
REMARK   3   SOLVENT ATOMS            : 324
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 28.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.75
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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): 0.202
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.831
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4080 ; 0.016 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  3457 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5542 ; 1.547 ; 1.913
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8038 ; 0.920 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   495 ; 6.949 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   554 ; 0.098 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4658 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   908 ; 0.006 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   861 ; 0.199 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4394 ; 0.246 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2285 ; 0.087 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   266 ; 0.165 ; 0.200
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):     6 ; 0.074 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    52 ; 0.299 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.164 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2456 ; 0.791 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3946 ; 1.432 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1624 ; 2.225 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1596 ; 3.477 ; 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  : NULL
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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 1Q4N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-03.
REMARK 100 THE RCSB ID CODE IS RCSB019910.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-01
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 9.00
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 RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30610
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.070
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.100
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.0
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1MFV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CALCIUM CHLORIDE, TRIS, PH
REMARK 280  9.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 100K
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       25.95000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.41000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.10000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.41000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.95000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.10000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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   OD2  ASP X   290     O    HOH X   724              2.06
REMARK 500   O    HOH X   631     O    HOH X   696              2.16
REMARK 500   O    HOH X   696     O    HOH X   748              2.18
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    ASP X  77   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 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 X  31      -53.23   -148.43
REMARK 500    MET X 102     -145.29   -103.49
REMARK 500    TRP X 280      133.73    -38.18
REMARK 500    PHE X 295      149.38   -176.84
REMARK 500    ASP X 317       58.21   -105.25
REMARK 500    ASN X 350       59.58     21.20
REMARK 500    SER X 414     -112.19   -133.80
REMARK 500    ASP X 433       30.79    -82.54
REMARK 500    ASN X 459       75.64     26.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA X 950  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH X 587   O
REMARK 620 2 ASP X 167   OD1  74.2
REMARK 620 3 HOH X 526   O   151.4 127.3
REMARK 620 4 ASN X 100   OD1 105.5  85.8  95.7
REMARK 620 5 ARG X 158   O    77.9 116.7  75.1 157.0
REMARK 620 6 ASP X 167   OD2  87.9  49.4  94.0 128.1  74.3
REMARK 620 7 HIS X 201   O    81.8 144.4  85.2  75.7  82.4 156.1
REMARK 620 8 HOH X 563   O   148.0  74.5  59.1  65.4 123.0  76.8 121.9
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 CA X 950
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL X 951
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM X 900
DBREF  1Q4N X    1   496  UNP    P04745   AMYS_HUMAN      16    511
SEQADV 1Q4N PCA X    1  UNP  P04745    GLN    16 MODIFIED RESIDUE
SEQADV 1Q4N TRP X  256  UNP  P04745    PHE   271 ENGINEERED
SEQRES   1 X  496  PCA TYR SER SER ASN THR GLN GLN GLY ARG THR SER ILE
SEQRES   2 X  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES   3 X  496  GLU CYS GLU ARG TYR LEU ALA PRO LYS GLY PHE GLY GLY
SEQRES   4 X  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL ALA ILE HIS
SEQRES   5 X  496  ASN PRO PHE ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES   6 X  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASP GLU
SEQRES   7 X  496  PHE ARG ASN MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES   8 X  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES   9 X  496  ASN ALA VAL SER ALA GLY THR SER SER THR CYS GLY SER
SEQRES  10 X  496  TYR PHE ASN PRO GLY SER ARG ASP PHE PRO ALA VAL PRO
SEQRES  11 X  496  TYR SER GLY TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES  12 X  496  GLY SER GLY ASP ILE GLU ASN TYR ASN ASP ALA THR GLN
SEQRES  13 X  496  VAL ARG ASP CYS ARG LEU SER GLY LEU LEU ASP LEU ALA
SEQRES  14 X  496  LEU GLY LYS ASP TYR VAL ARG SER LYS ILE ALA GLU TYR
SEQRES  15 X  496  MET ASN HIS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES  16 X  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES  17 X  496  ALA ILE LEU ASP LYS LEU HIS ASN LEU ASN SER ASN TRP
SEQRES  18 X  496  PHE PRO GLU GLY SER LYS PRO PHE ILE TYR GLN GLU VAL
SEQRES  19 X  496  ILE ASP LEU GLY GLY GLU PRO ILE LYS SER SER ASP TYR
SEQRES  20 X  496  PHE GLY ASN GLY ARG VAL THR GLU TRP LYS TYR GLY ALA
SEQRES  21 X  496  LYS LEU GLY THR VAL ILE ARG LYS TRP ASN GLY GLU LYS
SEQRES  22 X  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES  23 X  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES  24 X  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE
SEQRES  25 X  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS MET ALA VAL
SEQRES  26 X  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES  27 X  496  MET SER SER TYR ARG TRP PRO ARG TYR PHE GLU ASN GLY
SEQRES  28 X  496  LYS ASP VAL ASN ASP TRP VAL GLY PRO PRO ASN ASP ASN
SEQRES  29 X  496  GLY VAL THR LYS GLU VAL THR ILE ASN PRO ASP THR THR
SEQRES  30 X  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLN
SEQRES  31 X  496  ILE ARG ASN MET VAL ASN PHE ARG ASN VAL VAL ASP GLY
SEQRES  32 X  496  GLN PRO PHE THR ASN TRP TYR ASP ASN GLY SER ASN GLN
SEQRES  33 X  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES  34 X  496  ASN ASN ASP ASP TRP THR PHE SER LEU THR LEU GLN THR
SEQRES  35 X  496  GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES  36 X  496  ASP LYS ILE ASN GLY ASN CYS THR GLY ILE LYS ILE TYR
SEQRES  37 X  496  VAL SER ASP ASP GLY LYS ALA HIS PHE SER ILE SER ASN
SEQRES  38 X  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES  39 X  496  LYS LEU
MODRES 1Q4N PCA X    1  GLU  PYROGLUTAMIC ACID
HET    PCA  X   1       8
HET     CA  X 950       1
HET     CL  X 951       1
HET    TAM  X 900      11
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE
FORMUL   1  PCA    C5 H7 N O3
FORMUL   2   CA    CA 2+
FORMUL   3   CL    CL 1-
FORMUL   4  TAM    C7 H17 N O3
FORMUL   5  HOH   *324(H2 O)
HELIX    1   1 ARG X   20  TYR X   31  1                                  12
HELIX    2   2 PRO X   57  GLN X   63  5                                   7
HELIX    3   3 ASN X   75  VAL X   89  1                                  15
HELIX    4   4 SER X  132  PHE X  136  5                                   5
HELIX    5   5 ASP X  153  CYS X  160  1                                   8
HELIX    6   6 LYS X  172  GLY X  190  1                                  19
HELIX    7   7 ALA X  198  MET X  202  5                                   5
HELIX    8   8 TRP X  203  ASP X  212  1                                  10
HELIX    9   9 LYS X  243  PHE X  248  5                                   6
HELIX   10  10 TRP X  256  ARG X  267  1                                  12
HELIX   11  11 LYS X  273  TRP X  280  5                                   8
HELIX   12  12 GLY X  281  GLY X  285  5                                   5
HELIX   13  13 ASP X  300  GLY X  304  5                                   5
HELIX   14  14 GLY X  308  ILE X  312  5                                   5
HELIX   15  15 THR X  314  TRP X  316  5                                   3
HELIX   16  16 ASP X  317  HIS X  331  1                                  15
HELIX   17  17 CYS X  384  ARG X  387  5                                   4
HELIX   18  18 TRP X  388  VAL X  401  1                                  14
HELIX   19  19 GLU X  493  LYS X  495  5                                   3
SHEET    1   A 9 SER X  12  LEU X  16  0
SHEET    2   A 9 GLY X  39  VAL X  42  1  O  GLN X  41   N  VAL X  14
SHEET    3   A 9 ARG X  92  ALA X  97  1  O  TYR X  94   N  VAL X  40
SHEET    4   A 9 GLY X 193  ILE X 196  1  O  ARG X 195   N  ALA X  97
SHEET    5   A 9 PHE X 229  GLN X 232  1  O  TYR X 231   N  ILE X 196
SHEET    6   A 9 ARG X 252  THR X 254  1  O  THR X 254   N  GLN X 232
SHEET    7   A 9 ALA X 292  VAL X 294  1  O  LEU X 293   N  VAL X 253
SHEET    8   A 9 PHE X 335  SER X 340  1  O  PHE X 335   N  VAL X 294
SHEET    9   A 9 SER X  12  LEU X  16  1  N  HIS X  15   O  VAL X 338
SHEET    1   B 2 HIS X 101  GLY X 104  0
SHEET    2   B 2 LEU X 165  ASP X 167 -1  O  LEU X 166   N  CYS X 103
SHEET    1   C 2 PHE X 348  GLU X 349  0
SHEET    2   C 2 LYS X 352  ASP X 353 -1  O  LYS X 352   N  GLU X 349
SHEET    1   D 2 ASN X 362  ASP X 363  0
SHEET    2   D 2 VAL X 366  THR X 367 -1  O  VAL X 366   N  ASP X 363
SHEET    1   E 4 PHE X 406  ASP X 411  0
SHEET    2   E 4 GLN X 416  ARG X 421 -1  O  GLY X 420   N  THR X 407
SHEET    3   E 4 GLY X 425  ASN X 430 -1  O  PHE X 429   N  VAL X 417
SHEET    4   E 4 PHE X 487  HIS X 491 -1  O  ILE X 490   N  PHE X 426
SHEET    1   F 2 PHE X 436  GLN X 441  0
SHEET    2   F 2 LYS X 474  ILE X 479 -1  O  ILE X 479   N  PHE X 436
SHEET    1   G 2 GLY X 447  CYS X 450  0
SHEET    2   G 2 LYS X 466  VAL X 469 -1  O  ILE X 467   N  TYR X 449
SHEET    1   H 2 LYS X 457  ILE X 458  0
SHEET    2   H 2 ASN X 461  CYS X 462 -1  O  ASN X 461   N  ILE X 458
SSBOND   1 CYS X   28    CYS X   86                          1555   1555  2.04
SSBOND   2 CYS X   70    CYS X  115                          1555   1555  2.09
SSBOND   3 CYS X  141    CYS X  160                          1555   1555  2.04
SSBOND   4 CYS X  378    CYS X  384                          1555   1555  1.99
SSBOND   5 CYS X  450    CYS X  462                          1555   1555  2.04
LINK         C   PCA X   1                 N   TYR X   2     1555   1555  1.33
LINK        CA    CA X 950                 O   HOH X 587     1555   1555  2.41
LINK        CA    CA X 950                 OD1 ASP X 167     1555   1555  2.46
LINK        CA    CA X 950                 O   HOH X 526     1555   1555  2.59
LINK        CA    CA X 950                 OD1 ASN X 100     1555   1555  2.53
LINK        CA    CA X 950                 O   ARG X 158     1555   1555  2.29
LINK        CA    CA X 950                 OD2 ASP X 167     1555   1555  2.74
LINK        CA    CA X 950                 O   HIS X 201     1555   1555  2.39
LINK        CA    CA X 950                 O   HOH X 563     1555   1555  2.62
CISPEP   1 ASN X   53    PRO X   54          0        -3.19
CISPEP   2 VAL X  129    PRO X  130          0        -9.07
SITE     1 AC1  7 ASN X 100  ARG X 158  ASP X 167  HIS X 201
SITE     2 AC1  7 HOH X 526  HOH X 563  HOH X 587
SITE     1 AC2  3 ARG X 195  ASN X 298  ARG X 337
SITE     1 AC3  9 TYR X  62  HIS X 101  ASP X 197  ALA X 198
SITE     2 AC3  9 GLU X 233  ASP X 300  HOH X 608  HOH X 635
SITE     3 AC3  9 HOH X 697
CRYST1   51.900   74.200  134.820  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      0.019267  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013477  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007417        0.00000
      
PROCHECK
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 References