HEADER HYDROLASE 27-OCT-04 1XV8
TITLE CRYSTAL STRUCTURE OF HUMAN SALIVARY ALPHA-AMYLASE DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HSA;
COMPND 5 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND 6 EC: 3.2.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: SALIVA
KEYWDS HSA, HUMAN SALIVARY ALPHA-AMYLASE, DIMER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Z.FISHER,L.GOVINDASAMY,C.K.TU,D.N.SILVERMAN,H.RAJANIEMI,R.MCKENNA
REVDAT 7 23-AUG-23 1XV8 1 REMARK LINK
REVDAT 6 25-DEC-19 1XV8 1 SEQADV SEQRES LINK
REVDAT 5 04-APR-18 1XV8 1 REMARK
REVDAT 4 31-JAN-18 1XV8 1 REMARK
REVDAT 3 11-OCT-17 1XV8 1 REMARK
REVDAT 2 24-FEB-09 1XV8 1 VERSN
REVDAT 1 11-OCT-05 1XV8 0
JRNL AUTH S.Z.FISHER,L.GOVINDASAMY,C.K.TU,D.N.SILVERMAN,H.RAJANIEMI,
JRNL AUTH 2 R.MCKENNA
JRNL TITL CRYSTAL STRUCTURE OF HUMAN SALIVARY ALPHA-AMYLASE DIMER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 17504
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : RANDOM
REMARK 3 FREE R VALUE TEST SET SELECTION : 5%
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 843
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 : 7890
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 130
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.415
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1XV8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : NULL
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18579
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15400
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 1JXJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CA ACETATE, 0.1 M NA CACODYLATE
REMARK 280 (PH 6.5), 18% PEG 8K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 100K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 75.40600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.13500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.40600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.13500
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: 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 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 A 77 O HOH A 567 1.17
REMARK 500 CG ASP A 77 O HOH A 567 1.78
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 O ASN A 220 OE1 GLN B 8 3445 1.35
REMARK 500 O HOH A 499 O HOH B 547 3445 1.62
REMARK 500 OG1 THR A 111 OE2 GLU B 484 2655 2.04
REMARK 500 O ASN A 220 CD GLN B 8 3445 2.13
REMARK 500 CA TRP A 221 NE2 GLN B 8 3445 2.16
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 PRO A 332 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO B 332 C - N - CA ANGL. DEV. = 9.4 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 THR A 6 -176.40 -57.15
REMARK 500 GLN A 8 89.36 58.23
REMARK 500 ARG A 10 109.12 -49.32
REMARK 500 TYR A 31 -66.18 -144.05
REMARK 500 PRO A 44 103.01 -36.68
REMARK 500 ARG A 56 75.69 34.55
REMARK 500 PRO A 64 150.42 -48.47
REMARK 500 LEU A 69 76.80 -68.67
REMARK 500 CYS A 70 85.39 -151.97
REMARK 500 THR A 71 -169.67 -116.97
REMARK 500 MET A 102 -131.62 -110.30
REMARK 500 SER A 112 77.79 -65.30
REMARK 500 PHE A 119 140.19 -175.22
REMARK 500 ASN A 137 11.66 -69.42
REMARK 500 TYR A 151 13.57 -66.23
REMARK 500 ASP A 153 68.60 -114.00
REMARK 500 ALA A 154 -45.84 -22.91
REMARK 500 HIS A 215 -167.95 -73.87
REMARK 500 SER A 219 -8.33 -54.19
REMARK 500 TRP A 221 -18.36 -144.16
REMARK 500 ALA A 260 -71.12 -55.69
REMARK 500 ASN A 279 53.90 -93.00
REMARK 500 PRO A 288 126.06 -35.24
REMARK 500 HIS A 305 41.28 -89.20
REMARK 500 ASP A 317 70.94 -104.68
REMARK 500 PRO A 345 67.78 -59.18
REMARK 500 ASN A 350 71.29 31.66
REMARK 500 ASP A 356 1.50 -64.83
REMARK 500 ASN A 364 46.87 73.53
REMARK 500 ASN A 380 22.47 40.14
REMARK 500 SER A 414 -123.55 -128.50
REMARK 500 ALA A 418 145.14 170.18
REMARK 500 THR A 435 138.95 -39.62
REMARK 500 LEU A 438 151.92 178.20
REMARK 500 PRO A 486 25.89 -67.57
REMARK 500 THR B 6 -176.40 -57.13
REMARK 500 GLN B 8 89.40 58.18
REMARK 500 ARG B 10 109.12 -49.34
REMARK 500 TYR B 31 -66.23 -144.00
REMARK 500 PRO B 44 102.97 -36.60
REMARK 500 ARG B 56 75.65 34.60
REMARK 500 PRO B 64 150.42 -48.44
REMARK 500 LEU B 69 76.81 -68.67
REMARK 500 CYS B 70 85.40 -151.97
REMARK 500 THR B 71 -169.62 -116.97
REMARK 500 MET B 102 -131.62 -110.30
REMARK 500 SER B 112 77.80 -65.34
REMARK 500 PHE B 119 140.22 -175.28
REMARK 500 ASN B 137 11.77 -69.45
REMARK 500 TYR B 151 13.53 -66.21
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
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 A 497 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 100 OD1
REMARK 620 2 ARG A 158 O 145.6
REMARK 620 3 ASP A 167 OD1 105.5 90.2
REMARK 620 4 ASP A 167 OD2 68.9 99.7 52.6
REMARK 620 5 HIS A 201 O 77.7 96.2 162.9 140.7
REMARK 620 6 HOH A 510 O 111.5 102.8 64.9 112.9 98.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 497 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 100 OD1
REMARK 620 2 ARG B 158 O 145.6
REMARK 620 3 ASP B 167 OD1 105.5 90.2
REMARK 620 4 ASP B 167 OD2 68.9 99.7 52.6
REMARK 620 5 HIS B 201 O 77.8 96.2 162.9 140.7
REMARK 620 6 HOH B 513 O 111.5 102.9 65.0 112.9 98.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498
DBREF 1XV8 A 1 496 UNP P04745 AMYS_HUMAN 16 511
DBREF 1XV8 B 1 496 UNP P04745 AMYS_HUMAN 16 511
SEQRES 1 A 496 PCA TYR SER SER ASN THR GLN GLN 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 ALA PRO LYS GLY PHE GLY GLY
SEQRES 4 A 496 VAL GLN VAL SER PRO PRO ASN GLU ASN VAL ALA ILE HIS
SEQRES 5 A 496 ASN PRO PHE 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 ASP GLU
SEQRES 7 A 496 PHE ARG ASN 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 ASN ALA VAL SER ALA GLY THR SER SER THR CYS GLY SER
SEQRES 10 A 496 TYR PHE ASN PRO GLY SER ARG ASP PHE PRO ALA VAL PRO
SEQRES 11 A 496 TYR SER GLY TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 A 496 GLY SER GLY ASP ILE GLU ASN TYR ASN ASP ALA THR GLN
SEQRES 13 A 496 VAL ARG ASP CYS ARG LEU SER GLY LEU LEU ASP LEU ALA
SEQRES 14 A 496 LEU GLY LYS ASP TYR VAL ARG SER LYS ILE ALA GLU TYR
SEQRES 15 A 496 MET ASN HIS 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 ILE LEU ASP LYS LEU HIS ASN LEU ASN SER ASN TRP
SEQRES 18 A 496 PHE PRO GLU GLY SER LYS PRO PHE ILE TYR GLN GLU VAL
SEQRES 19 A 496 ILE ASP LEU GLY GLY GLU PRO ILE LYS SER SER ASP 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 ILE ARG LYS TRP ASN GLY GLU LYS
SEQRES 22 A 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 A 496 MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 A 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE
SEQRES 25 A 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS MET 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 PRO ARG TYR PHE GLU ASN GLY
SEQRES 28 A 496 LYS ASP VAL ASN ASP TRP VAL GLY PRO PRO ASN ASP ASN
SEQRES 29 A 496 GLY VAL THR LYS GLU VAL THR ILE ASN PRO ASP THR THR
SEQRES 30 A 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLN
SEQRES 31 A 496 ILE ARG ASN MET VAL ASN PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 A 496 GLN PRO PHE THR ASN TRP TYR 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 THR PHE SER LEU THR LEU GLN THR
SEQRES 35 A 496 GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 A 496 ASP LYS ILE ASN GLY ASN CYS THR GLY ILE LYS ILE TYR
SEQRES 37 A 496 VAL SER ASP ASP GLY LYS ALA HIS PHE SER ILE SER ASN
SEQRES 38 A 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 A 496 LYS LEU
SEQRES 1 B 496 PCA TYR SER SER ASN THR GLN GLN GLY ARG THR SER ILE
SEQRES 2 B 496 VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES 3 B 496 GLU CYS GLU ARG TYR LEU ALA PRO LYS GLY PHE GLY GLY
SEQRES 4 B 496 VAL GLN VAL SER PRO PRO ASN GLU ASN VAL ALA ILE HIS
SEQRES 5 B 496 ASN PRO PHE ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES 6 B 496 SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASP GLU
SEQRES 7 B 496 PHE ARG ASN MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES 8 B 496 ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES 9 B 496 ASN ALA VAL SER ALA GLY THR SER SER THR CYS GLY SER
SEQRES 10 B 496 TYR PHE ASN PRO GLY SER ARG ASP PHE PRO ALA VAL PRO
SEQRES 11 B 496 TYR SER GLY TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 B 496 GLY SER GLY ASP ILE GLU ASN TYR ASN ASP ALA THR GLN
SEQRES 13 B 496 VAL ARG ASP CYS ARG LEU SER GLY LEU LEU ASP LEU ALA
SEQRES 14 B 496 LEU GLY LYS ASP TYR VAL ARG SER LYS ILE ALA GLU TYR
SEQRES 15 B 496 MET ASN HIS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES 16 B 496 ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES 17 B 496 ALA ILE LEU ASP LYS LEU HIS ASN LEU ASN SER ASN TRP
SEQRES 18 B 496 PHE PRO GLU GLY SER LYS PRO PHE ILE TYR GLN GLU VAL
SEQRES 19 B 496 ILE ASP LEU GLY GLY GLU PRO ILE LYS SER SER ASP TYR
SEQRES 20 B 496 PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES 21 B 496 LYS LEU GLY THR VAL ILE ARG LYS TRP ASN GLY GLU LYS
SEQRES 22 B 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 B 496 MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 B 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE
SEQRES 25 B 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS MET ALA VAL
SEQRES 26 B 496 GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES 27 B 496 MET SER SER TYR ARG TRP PRO ARG TYR PHE GLU ASN GLY
SEQRES 28 B 496 LYS ASP VAL ASN ASP TRP VAL GLY PRO PRO ASN ASP ASN
SEQRES 29 B 496 GLY VAL THR LYS GLU VAL THR ILE ASN PRO ASP THR THR
SEQRES 30 B 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLN
SEQRES 31 B 496 ILE ARG ASN MET VAL ASN PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 B 496 GLN PRO PHE THR ASN TRP TYR ASP ASN GLY SER ASN GLN
SEQRES 33 B 496 VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES 34 B 496 ASN ASN ASP ASP TRP THR PHE SER LEU THR LEU GLN THR
SEQRES 35 B 496 GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 B 496 ASP LYS ILE ASN GLY ASN CYS THR GLY ILE LYS ILE TYR
SEQRES 37 B 496 VAL SER ASP ASP GLY LYS ALA HIS PHE SER ILE SER ASN
SEQRES 38 B 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 B 496 LYS LEU
MODRES 1XV8 PCA A 1 GLN PYROGLUTAMIC ACID
MODRES 1XV8 PCA B 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 8
HET PCA B 1 8
HET CA A 497 1
HET CL A 498 1
HET CA B 497 1
HET CL B 498 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 PCA 2(C5 H7 N O3)
FORMUL 3 CA 2(CA 2+)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *130(H2 O)
HELIX 1 1 ARG A 20 TYR A 31 1 12
HELIX 2 2 TRP A 59 GLN A 63 5 5
HELIX 3 3 ASN A 75 ASN A 88 1 14
HELIX 4 4 SER A 132 PHE A 136 5 5
HELIX 5 5 ASP A 153 CYS A 160 1 8
HELIX 6 6 LYS A 172 GLY A 190 1 19
HELIX 7 7 ALA A 198 MET A 202 5 5
HELIX 8 8 TRP A 203 LYS A 213 1 11
HELIX 9 9 LYS A 243 PHE A 248 5 6
HELIX 10 10 GLU A 255 ARG A 267 1 13
HELIX 11 11 LYS A 273 LYS A 278 5 6
HELIX 12 12 GLY A 281 GLY A 285 5 5
HELIX 13 13 PRO A 288 ASP A 290 5 3
HELIX 14 14 ASP A 300 GLY A 304 5 5
HELIX 15 15 GLY A 308 ILE A 312 5 5
HELIX 16 16 THR A 314 TRP A 316 5 3
HELIX 17 17 ASP A 317 HIS A 331 1 15
HELIX 18 18 CYS A 384 ARG A 387 5 4
HELIX 19 19 TRP A 388 VAL A 401 1 14
HELIX 20 20 GLU A 493 LYS A 495 5 3
HELIX 21 21 ARG B 20 TYR B 31 1 12
HELIX 22 22 TRP B 59 GLN B 63 5 5
HELIX 23 23 ASN B 75 ASN B 88 1 14
HELIX 24 24 SER B 132 PHE B 136 5 5
HELIX 25 25 ASP B 153 CYS B 160 1 8
HELIX 26 26 LYS B 172 GLY B 190 1 19
HELIX 27 27 ALA B 198 MET B 202 5 5
HELIX 28 28 TRP B 203 LYS B 213 1 11
HELIX 29 29 LYS B 243 PHE B 248 5 6
HELIX 30 30 GLU B 255 ARG B 267 1 13
HELIX 31 31 LYS B 273 LYS B 278 5 6
HELIX 32 32 GLY B 281 GLY B 285 5 5
HELIX 33 33 PRO B 288 ASP B 290 5 3
HELIX 34 34 ASP B 300 GLY B 304 5 5
HELIX 35 35 GLY B 308 ILE B 312 5 5
HELIX 36 36 THR B 314 TRP B 316 5 3
HELIX 37 37 ASP B 317 HIS B 331 1 15
HELIX 38 38 CYS B 384 ARG B 387 5 4
HELIX 39 39 TRP B 388 VAL B 401 1 14
HELIX 40 40 GLU B 493 LYS B 495 5 3
SHEET 1 A 9 SER A 12 LEU A 16 0
SHEET 2 A 9 GLY A 39 GLN A 41 1 O GLN A 41 N VAL A 14
SHEET 3 A 9 ARG A 92 ALA A 97 1 O TYR A 94 N VAL A 40
SHEET 4 A 9 GLY A 193 ILE A 196 1 O ARG A 195 N VAL A 95
SHEET 5 A 9 PHE A 229 GLN A 232 1 O PHE A 229 N PHE A 194
SHEET 6 A 9 ARG A 252 THR A 254 1 O ARG A 252 N GLN A 232
SHEET 7 A 9 ALA A 292 VAL A 294 1 O LEU A 293 N VAL A 253
SHEET 8 A 9 PHE A 335 SER A 340 1 O PHE A 335 N ALA A 292
SHEET 9 A 9 SER A 12 LEU A 16 1 N HIS A 15 O VAL A 338
SHEET 1 B 2 HIS A 101 GLY A 104 0
SHEET 2 B 2 LEU A 165 ASP A 167 -1 O LEU A 166 N CYS A 103
SHEET 1 C 2 PHE A 348 GLU A 349 0
SHEET 2 C 2 LYS A 352 ASP A 353 -1 O LYS A 352 N GLU A 349
SHEET 1 D 4 PHE A 406 TYR A 410 0
SHEET 2 D 4 ALA A 418 ARG A 421 -1 O GLY A 420 N THR A 407
SHEET 3 D 4 GLY A 425 PHE A 429 -1 O ILE A 427 N PHE A 419
SHEET 4 D 4 PHE A 487 HIS A 491 -1 O ILE A 488 N VAL A 428
SHEET 1 E 2 PHE A 436 GLN A 441 0
SHEET 2 E 2 LYS A 474 ILE A 479 -1 O ALA A 475 N LEU A 440
SHEET 1 F 2 GLY A 447 CYS A 450 0
SHEET 2 F 2 LYS A 466 VAL A 469 -1 O ILE A 467 N TYR A 449
SHEET 1 G 2 LYS A 457 ILE A 458 0
SHEET 2 G 2 ASN A 461 CYS A 462 -1 O ASN A 461 N ILE A 458
SHEET 1 H 9 SER B 12 LEU B 16 0
SHEET 2 H 9 GLY B 39 GLN B 41 1 O GLN B 41 N VAL B 14
SHEET 3 H 9 ARG B 92 ALA B 97 1 O TYR B 94 N VAL B 40
SHEET 4 H 9 GLY B 193 ILE B 196 1 O ARG B 195 N VAL B 95
SHEET 5 H 9 PHE B 229 GLN B 232 1 O PHE B 229 N PHE B 194
SHEET 6 H 9 ARG B 252 THR B 254 1 O ARG B 252 N GLN B 232
SHEET 7 H 9 ALA B 292 VAL B 294 1 O LEU B 293 N VAL B 253
SHEET 8 H 9 PHE B 335 SER B 340 1 O PHE B 335 N ALA B 292
SHEET 9 H 9 SER B 12 LEU B 16 1 N HIS B 15 O VAL B 338
SHEET 1 I 2 HIS B 101 GLY B 104 0
SHEET 2 I 2 LEU B 165 ASP B 167 -1 O LEU B 166 N CYS B 103
SHEET 1 J 2 PHE B 348 GLU B 349 0
SHEET 2 J 2 LYS B 352 ASP B 353 -1 O LYS B 352 N GLU B 349
SHEET 1 K 4 PHE B 406 TYR B 410 0
SHEET 2 K 4 ALA B 418 ARG B 421 -1 O GLY B 420 N THR B 407
SHEET 3 K 4 GLY B 425 PHE B 429 -1 O ILE B 427 N PHE B 419
SHEET 4 K 4 PHE B 487 HIS B 491 -1 O ILE B 488 N VAL B 428
SHEET 1 L 2 PHE B 436 GLN B 441 0
SHEET 2 L 2 LYS B 474 ILE B 479 -1 O ALA B 475 N LEU B 440
SHEET 1 M 2 GLY B 447 CYS B 450 0
SHEET 2 M 2 LYS B 466 VAL B 469 -1 O ILE B 467 N TYR B 449
SHEET 1 N 2 LYS B 457 ILE B 458 0
SHEET 2 N 2 ASN B 461 CYS B 462 -1 O ASN B 461 N ILE B 458
SSBOND 1 CYS A 28 CYS A 86 1555 1555 2.04
SSBOND 2 CYS A 70 CYS A 115 1555 1555 2.02
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
SSBOND 6 CYS B 28 CYS B 86 1555 1555 2.04
SSBOND 7 CYS B 70 CYS B 115 1555 1555 2.03
SSBOND 8 CYS B 141 CYS B 160 1555 1555 2.03
SSBOND 9 CYS B 378 CYS B 384 1555 1555 2.03
SSBOND 10 CYS B 450 CYS B 462 1555 1555 2.03
LINK C PCA A 1 N TYR A 2 1555 1555 1.33
LINK C PCA B 1 N TYR B 2 1555 1555 1.33
LINK OD1 ASN A 100 CA CA A 497 1555 1555 2.27
LINK O ARG A 158 CA CA A 497 1555 1555 2.35
LINK OD1 ASP A 167 CA CA A 497 1555 1555 2.07
LINK OD2 ASP A 167 CA CA A 497 1555 1555 2.68
LINK O HIS A 201 CA CA A 497 1555 1555 2.16
LINK CA CA A 497 O HOH A 510 1555 1555 2.55
LINK OD1 ASN B 100 CA CA B 497 1555 1555 2.27
LINK O ARG B 158 CA CA B 497 1555 1555 2.35
LINK OD1 ASP B 167 CA CA B 497 1555 1555 2.07
LINK OD2 ASP B 167 CA CA B 497 1555 1555 2.68
LINK O HIS B 201 CA CA B 497 1555 1555 2.16
LINK CA CA B 497 O HOH B 513 1555 1555 2.55
CISPEP 1 ASN A 53 PRO A 54 0 -0.28
CISPEP 2 VAL A 129 PRO A 130 0 -0.13
CISPEP 3 ASN B 53 PRO B 54 0 -0.32
CISPEP 4 VAL B 129 PRO B 130 0 -0.11
SITE 1 AC1 5 ASN A 100 ARG A 158 ASP A 167 HIS A 201
SITE 2 AC1 5 HOH A 510
SITE 1 AC2 5 ASN B 100 ARG B 158 ASP B 167 HIS B 201
SITE 2 AC2 5 HOH B 513
SITE 1 AC3 3 ARG B 195 ASN B 298 ARG B 337
SITE 1 AC4 3 ARG A 195 ASN A 298 ARG A 337
CRYST1 150.812 72.270 91.106 90.00 102.80 90.00 C 1 2 1 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 0.006631 0.000000 0.001506 0.00000
SCALE2 0.000000 0.013837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011256 0.00000
HETATM 1 N PCA A 1 56.554 5.323 37.737 1.00 29.87 N
HETATM 2 CA PCA A 1 57.265 5.490 36.420 1.00 29.64 C
HETATM 3 CB PCA A 1 57.956 6.843 36.408 1.00 30.84 C
HETATM 4 CG PCA A 1 58.191 7.190 37.866 1.00 30.89 C
HETATM 5 CD PCA A 1 57.134 6.372 38.569 1.00 30.47 C
HETATM 6 OE PCA A 1 56.802 6.623 39.736 1.00 32.65 O
HETATM 7 C PCA A 1 58.355 4.437 36.234 1.00 27.36 C
HETATM 8 O PCA A 1 58.933 4.307 35.152 1.00 23.41 O
(ATOM LINES ARE NOT SHOWN.)
END
