HEADER GLYCOSYLTRANSFERASE 15-JUN-96 1PIG
TITLE PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE;
COMPND 5 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 ORGAN: PANCREAS
KEYWDS ALPHA-AMYLASE ALPHA-1, 4-GLUCAN-4-GLUCANOHYDROLASE
KEYWDS 2 GLYCOSYLTRANSFERASE, GLYCOSYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MACHIUS,L.VERTESY,R.HUBER,G.WIEGAND
REVDAT 8 09-AUG-23 1PIG 1 REMARK HETSYN LINK
REVDAT 7 29-JUL-20 1PIG 1 COMPND REMARK HETNAM LINK
REVDAT 7 2 1 SITE ATOM
REVDAT 6 25-DEC-19 1PIG 1 SEQRES
REVDAT 5 20-NOV-19 1PIG 1 REMARK SEQADV LINK
REVDAT 4 08-SEP-09 1PIG 1 HETATM HETNAM
REVDAT 3 24-FEB-09 1PIG 1 VERSN
REVDAT 2 01-APR-03 1PIG 1 JRNL
REVDAT 1 07-DEC-96 1PIG 0
JRNL AUTH M.MACHIUS,L.VERTESY,R.HUBER,G.WIEGAND
JRNL TITL CARBOHYDRATE AND PROTEIN-BASED INHIBITORS OF PORCINE
JRNL TITL 2 PANCREATIC ALPHA-AMYLASE: STRUCTURE ANALYSIS AND COMPARISON
JRNL TITL 3 OF THEIR BINDING CHARACTERISTICS.
JRNL REF J.MOL.BIOL. V. 260 409 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8757803
JRNL DOI 10.1006/JMBI.1996.0410
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.WIEGAND,O.EPP,R.HUBER
REMARK 1 TITL THE CRYSTAL STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE IN
REMARK 1 TITL 2 COMPLEX WITH THE MICROBIAL INHIBITOR TENDAMISTAT
REMARK 1 REF J.MOL.BIOL. V. 247 99 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.QIAN,R.HASER,F.PAYAN
REMARK 1 TITL CARBOHYDRATE BINDING SITES IN A PANCREATIC
REMARK 1 TITL 2 ALPHA-AMYLASE-SUBSTRATE COMPLEX, DERIVED FROM X-RAY
REMARK 1 TITL 3 STRUCTURE ANALYSIS AT 2.1 ANGSTROM RESOLUTION
REMARK 1 REF PROTEIN SCI. V. 4 747 1995
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 3
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 4
REMARK 1 AUTH M.QIAN,R.HASER,G.BUISSON,E.DUEE,F.PAYAN
REMARK 1 TITL THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. STRUCTURE OF
REMARK 1 TITL 2 THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A
REMARK 1 TITL 3 CARBOHYDRATE INHIBITOR REFINED TO 2.2-A RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 33 6284 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.QIAN,R.HASER,F.PAYAN
REMARK 1 TITL STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG PANCREATIC
REMARK 1 TITL 2 ALPHA-AMYLASE AT 2.1 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 231 785 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 44944
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.500
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4366
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.60
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 : 3904
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 125
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.30
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) : 0.20
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.200
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 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500
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 1PIG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175694.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-95
REMARK 200 TEMPERATURE (KELVIN) : 275
REMARK 200 PH : 6.0-10.0
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, ROTAVATA/AGROVATA
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47260
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: 1PIF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION; 10 MICROLITER OF
REMARK 280 PROTEIN (15 MG/ML IN 0.1 M AMMONIUM CACODYLATE, PH 10.0 0.001 M
REMARK 280 V-1532) WERE STEPWISE CONCENTRATED OVER 0.1, 0.15, AND 0.25 M
REMARK 280 AMMONIUM CACODYLATE, PH 6.0., VAPOR DIFFUSION
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 35.25000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.35000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.35000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.40000
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: A, B, C, D, E
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 TRP A 134 CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 480 TRP A 134 CH2
REMARK 480 ASN A 350 CB CG OD1 ND2
REMARK 480 GLU A 352 CD OE1 OE2
REMARK 480 ASN A 460 CB CG OD1 ND2
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 -59.22 -138.02
REMARK 500 MET A 102 -150.75 -108.07
REMARK 500 ALA A 133 -39.87 -39.74
REMARK 500 THR A 219 -7.90 -59.95
REMARK 500 ASP A 317 57.91 -111.84
REMARK 500 ASP A 402 119.39 -39.72
REMARK 500 SER A 414 -102.08 -136.01
REMARK 500 ASP A 433 31.29 -95.30
REMARK 500 SER A 437 87.91 -150.97
REMARK 500 PRO A 486 39.22 -73.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 468 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 TRESTATIN LIKE COMPOUNDS HAVE BEEN ISOLATED FROM
REMARK 600 STREPTOMYCES GALBUS CULTURE MEDIUM AND TREATED WITH
REMARK 600 ALPHA-AMYLASE FROM BACILLUS SUBTILIS. FROM THAT MIXTURE,
REMARK 600 A SUBSTANCE WITH MOLECULAR WEIGHT 1272.5 CONTAINING TWO
REMARK 600 NITROGEN ATOMS COULD BE ISOLATED. THE PRELIMINARY
REMARK 600 STRUCTURE OF THIS COMPOUND HAS BEEN DETERMINED USING MASS
REMARK 600 SPECTROMETRY AND FOUND TO COMPRISE 2 CYC, 2 GLA, AND 4 GLC
REMARK 600 RESIDUES. THE MOLECULE SEEN IN THE ELECTRON DENSITY HAS
REMARK 600 THE SEQUENCE GLA-GLC-CYC-GLA-GLC-GLC AND RESULTS FROM
REMARK 600 PROCESSING OF THE ORIGINAL COMPOUND BY ALPHA-AMYLASE, A
REMARK 600 PHENOMENON WHICH WAS ALREADY OBSERVED WITH ACARBOSE (SEE
REMARK 600 REFERENCE 3 FOR DETAILS).
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 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 100 OD1
REMARK 620 2 ARG A 158 O 154.2
REMARK 620 3 ASP A 167 OD1 86.1 111.4
REMARK 620 4 ASP A 167 OD2 127.9 77.2 50.7
REMARK 620 5 HIS A 201 O 69.5 85.3 139.4 162.5
REMARK 620 6 HOH A2094 O 104.6 75.9 137.2 93.9 81.7
REMARK 620 7 HOH A2095 O 68.2 130.8 82.5 77.5 115.1 64.6
REMARK 620 8 HOH A2102 O 101.1 71.2 66.3 87.7 86.5 145.8 148.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CATALYTICALLY ACTIVE RESIDUES.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CHLORIDE BINDING SITE.
DBREF 1PIG A 2 496 UNP P00690 AMYP_PIG 2 496
SEQADV 1PIG VAL A 49 UNP P00690 ILE 49 CONFLICT
SEQADV 1PIG SER A 243 UNP P00690 GLN 243 CONFLICT
SEQADV 1PIG SER A 310 UNP P00690 ALA 310 CONFLICT
SEQADV 1PIG GLN A 404 UNP P00690 GLU 404 CONFLICT
SEQADV 1PIG ASN A 451 UNP P00690 ASP 451 CONFLICT
SEQADV 1PIG GLN A 484 UNP P00690 GLU 484 CONFLICT
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 VAL 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 SER 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 SER 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 SER 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 GLU 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 GLU
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 ASN 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 GLN ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 A 496 LYS LEU
MODRES 1PIG PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 8
HET GLC B 1 11
HET AGL B 2 10
HET BGC C 1 12
HET GLC C 2 11
HET AGL C 3 10
HET GLC D 1 12
HET GLC D 2 11
HET GLC E 1 12
HET BGC E 2 11
HET HMC A 703 11
HET BGC A1002 12
HET CA A 500 1
HET CL A 600 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM AGL 4-AMINO-4,6-DIDEOXY-ALPHA-D-GLUCOPYRANOSE
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM HMC 5-HYDROXYMETHYL-CHONDURITOL
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN AGL 4,6-DIDEOXY-4-AMINO-ALPHA-D-GLUCOSE; 4-AMINO-4-DEOXY-
HETSYN 2 AGL ALPHA-D-QUINOVOPYRANOSE; 4-AMINO-4,6-DIDEOXY-ALPHA-D-
HETSYN 3 AGL GLUCOSE; 4-AMINO-4,6-DIDEOXY-D-GLUCOSE; 4-AMINO-4,6-
HETSYN 4 AGL DIDEOXY-GLUCOSE
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 GLC 5(C6 H12 O6)
FORMUL 2 AGL 2(C6 H13 N O4)
FORMUL 3 BGC 3(C6 H12 O6)
FORMUL 6 HMC C7 H12 O5
FORMUL 8 CA CA 2+
FORMUL 9 CL CL 1-
FORMUL 10 HOH *228(H2 O)
HELIX 1 1 TRP A 21 ARG A 30 1 10
HELIX 2 2 TRP A 58 TYR A 62 5 5
HELIX 3 3 GLU A 76 VAL A 89 1 14
HELIX 4 4 PRO A 121 SER A 123 5 3
HELIX 5 5 ALA A 133 ASP A 135 5 3
HELIX 6 6 PRO A 154 ASP A 159 1 6
HELIX 7 7 ASP A 173 ILE A 189 1 17
HELIX 8 8 SER A 199 HIS A 201 5 3
HELIX 9 9 PRO A 204 LYS A 213 1 10
HELIX 10 10 SER A 244 TYR A 247 5 4
HELIX 11 11 PHE A 256 ARG A 267 1 12
HELIX 12 12 MET A 274 ASN A 279 5 6
HELIX 13 13 GLU A 282 TRP A 284 5 3
HELIX 14 14 SER A 289 ARG A 291 5 3
HELIX 15 15 ASN A 301 ARG A 303 5 3
HELIX 16 16 GLY A 309 SER A 311 5 3
HELIX 17 17 PHE A 315 ALA A 330 5 16
HELIX 18 18 GLU A 385 ARG A 387 5 3
HELIX 19 19 ARG A 389 VAL A 401 1 13
HELIX 20 20 ALA A 492 SER A 494 5 3
SHEET 1 A 6 THR A 336 SER A 340 0
SHEET 2 A 6 SER A 12 LEU A 16 1 N ILE A 13 O THR A 336
SHEET 3 A 6 GLY A 39 VAL A 42 1 N GLY A 39 O VAL A 14
SHEET 4 A 6 ARG A 92 ALA A 97 1 N ARG A 92 O VAL A 40
SHEET 5 A 6 GLY A 193 ILE A 196 1 N GLY A 193 O VAL A 95
SHEET 6 A 6 PHE A 229 GLN A 232 1 N PHE A 229 O PHE A 194
SHEET 1 B 3 GLN A 416 ARG A 421 0
SHEET 2 B 3 GLY A 425 ASN A 430 -1 N PHE A 429 O VAL A 417
SHEET 3 B 3 PHE A 487 HIS A 491 -1 N ILE A 490 O PHE A 426
SHEET 1 C 2 LEU A 436 GLN A 441 0
SHEET 2 C 2 THR A 474 ILE A 479 -1 N ILE A 479 O LEU A 436
SHEET 1 D 2 GLY A 447 CYS A 450 0
SHEET 2 D 2 LYS A 466 VAL A 469 -1 N VAL A 469 O GLY A 447
SSBOND 1 CYS A 28 CYS A 86 1555 1555 2.03
SSBOND 2 CYS A 70 CYS A 115 1555 1555 2.03
SSBOND 3 CYS A 141 CYS A 160 1555 1555 2.03
SSBOND 4 CYS A 378 CYS A 384 1555 1555 2.03
SSBOND 5 CYS A 450 CYS A 462 1555 1555 2.03
LINK C PCA A 1 N TYR A 2 1555 1555 1.33
LINK O4 HMC A 703 C1 GLC B 1 1555 1555 1.41
LINK C1 HMC A 703 N4 AGL C 3 1555 1555 1.47
LINK O4 GLC B 1 C1 AGL B 2 1555 1555 1.41
LINK O4 BGC C 1 C1 GLC C 2 1555 1555 1.40
LINK O4 GLC C 2 C1 AGL C 3 1555 1555 1.40
LINK O4 GLC D 1 C1 GLC D 2 1555 1555 1.40
LINK O4 GLC E 1 C1 BGC E 2 1555 1555 1.39
LINK OD1 ASN A 100 CA CA A 500 1555 1555 2.45
LINK O ARG A 158 CA CA A 500 1555 1555 2.36
LINK OD1 ASP A 167 CA CA A 500 1555 1555 2.51
LINK OD2 ASP A 167 CA CA A 500 1555 1555 2.58
LINK O HIS A 201 CA CA A 500 1555 1555 2.41
LINK CA CA A 500 O HOH A2094 1555 1555 2.50
LINK CA CA A 500 O HOH A2095 1555 1555 2.43
LINK CA CA A 500 O HOH A2102 1555 1555 2.58
CISPEP 1 ASN A 53 PRO A 54 0 -0.30
CISPEP 2 VAL A 129 PRO A 130 0 0.04
SITE 1 AS 3 ASP A 197 GLU A 233 ASP A 300
SITE 1 CA 4 ASN A 100 ARG A 158 ASP A 167 HIS A 201
SITE 1 CL 3 ARG A 195 ASN A 298 ARG A 337
CRYST1 70.500 114.800 118.700 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 0.014184 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008425 0.00000
HETATM 1 N PCA A 1 40.881 12.650 34.096 1.00 39.67 N
HETATM 2 CA PCA A 1 40.558 13.344 35.344 1.00 35.81 C
HETATM 3 CB PCA A 1 41.321 12.588 36.432 1.00 36.73 C
HETATM 4 CG PCA A 1 42.510 12.105 35.629 1.00 39.27 C
HETATM 5 CD PCA A 1 41.992 11.931 34.217 1.00 44.13 C
HETATM 6 OE PCA A 1 42.181 11.388 33.124 1.00 50.73 O
HETATM 7 C PCA A 1 40.787 14.838 35.457 1.00 33.67 C
HETATM 8 O PCA A 1 40.277 15.448 36.392 1.00 33.98 O
(ATOM LINES ARE NOT SHOWN.)
END