HEADER HYDROLASE 07-SEP-01 1JXJ
TITLE ROLE OF MOBILE LOOP IN THE MECHANISM OF HUMAN SALIVARY AMYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE, SALIVARY;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SALIVARY ALPHA-AMYALSE; 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 ORGAN: SALIVARY GLANDS;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS AMYLASE, MUTAGENESIS, CATALYSIS, HUMAN, SALIVARY, ENZYME, MOBILE
KEYWDS 2 LOOP, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.RAMASUBBU,C.RAGUNATH,Z.WANG,P.J.MISHRA,L.M.THOMAS
REVDAT 8 16-AUG-23 1JXJ 1 REMARK
REVDAT 7 27-OCT-21 1JXJ 1 REMARK SEQADV LINK
REVDAT 6 25-DEC-19 1JXJ 1 SEQADV SEQRES LINK
REVDAT 5 04-OCT-17 1JXJ 1 REMARK
REVDAT 4 24-FEB-09 1JXJ 1 VERSN
REVDAT 3 22-MAR-05 1JXJ 1 JRNL AUTHOR REMARK
REVDAT 2 27-MAY-03 1JXJ 1 JRNL REMARK
REVDAT 1 14-SEP-01 1JXJ 0
JRNL AUTH N.RAMASUBBU,C.RAGUNATH,P.J.MISHRA,L.M.THOMAS,L.KANDRA
JRNL TITL HUMAN SALIVARY ALPHA-AMYLASE TRP58 SITUATED AT SUBSITE -2 IS
JRNL TITL 2 CRITICAL FOR ENZYME ACTIVITY.
JRNL REF EUR.J.BIOCHEM. V. 271 2517 2004
JRNL REFN ISSN 0014-2956
JRNL PMID 15182367
JRNL DOI 10.1111/J.1432-1033.2004.04182.X
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 34452
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1795
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3940
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.99
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): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.400
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4058 ; 0.015 ; 0.000
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5511 ; 1.617 ; 1.900
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 495 ; 4.826 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 554 ; 0.129 ; 0.200
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 554 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3226 ; 0.007 ; 0.000
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3226 ; 0.007 ; 0.000
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2028 ; 0.220 ; 0.300
REMARK 3 H-BOND (X...Y) OTHERS (A): 471 ; 0.123 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2452 ; 0.798 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3940 ; 1.412 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1606 ; 2.299 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1571 ; 3.419 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JXJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 9.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
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 : 34452
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 65.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.06200
REMARK 200 R SYM FOR SHELL (I) : 0.28100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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 1SMD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CALCIUM CHLORIDE, PH 9.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K, TEMPERATURE 298.0K
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 26.14750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.50900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.62500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.50900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.14750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.62500
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
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: 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 ARG A 124 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 124 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 135 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 317 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 363 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 411 CB - CG - OD2 ANGL. DEV. = 6.1 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 A 31 -55.70 -148.50
REMARK 500 MET A 102 -134.11 -100.55
REMARK 500 ASP A 317 57.42 -110.80
REMARK 500 ASN A 350 75.78 35.57
REMARK 500 SER A 414 -101.00 -132.39
REMARK 500 ASP A 433 37.05 -88.08
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 156.9
REMARK 620 3 ASP A 167 OD1 83.4 116.0
REMARK 620 4 ASP A 167 OD2 127.5 75.6 51.0
REMARK 620 5 HIS A 201 O 77.3 79.6 140.9 154.5
REMARK 620 6 HOH A 540 O 70.2 124.6 76.0 74.1 126.4
REMARK 620 7 HOH A 592 O 105.1 71.9 132.5 92.1 85.6 64.2
REMARK 620 8 HOH A 607 O 102.0 73.9 73.5 89.7 77.8 149.3 144.0
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 A 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SMD RELATED DB: PDB
REMARK 900 HUMAN SALIVARY AMYLASE: NATIVE STRUCTURE
REMARK 900 RELATED ID: 1JXK RELATED DB: PDB
REMARK 900 RELATED ENTRY
DBREF 1JXJ A 1 496 UNP P04745 AMYS_HUMAN 16 511
SEQADV 1JXJ LEU A 58 UNP P04745 TRP 73 ENGINEERED MUTATION
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 LEU 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
MODRES 1JXJ PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 8
HET CA A 497 1
HET CL A 498 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 CA CA 2+
FORMUL 3 CL CL 1-
FORMUL 4 HOH *294(H2 O)
HELIX 1 1 ARG A 20 TYR A 31 1 12
HELIX 2 2 PRO A 57 GLN A 63 5 7
HELIX 3 3 ASN A 75 VAL A 89 1 15
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 ARG A 161 SER A 163 5 3
HELIX 7 7 LYS A 172 GLY A 190 1 19
HELIX 8 8 ALA A 198 MET A 202 5 5
HELIX 9 9 TRP A 203 LYS A 213 1 11
HELIX 10 10 LYS A 243 PHE A 248 5 6
HELIX 11 11 PHE A 256 ARG A 267 1 12
HELIX 12 12 LYS A 273 TRP A 280 5 8
HELIX 13 13 GLY A 281 GLY A 285 5 5
HELIX 14 14 PRO A 288 ASP A 290 5 3
HELIX 15 15 ASP A 300 GLY A 304 5 5
HELIX 16 16 GLY A 308 ILE A 312 5 5
HELIX 17 17 THR A 314 TRP A 316 5 3
HELIX 18 18 ASP A 317 HIS A 331 1 15
HELIX 19 19 CYS A 384 ARG A 387 5 4
HELIX 20 20 TRP A 388 ASP A 402 1 15
HELIX 21 21 GLU A 493 LYS A 495 5 3
SHEET 1 A 9 SER A 12 LEU A 16 0
SHEET 2 A 9 GLY A 39 VAL A 42 1 O GLY A 39 N VAL A 14
SHEET 3 A 9 ARG A 92 ALA A 97 1 O ARG A 92 N VAL A 40
SHEET 4 A 9 GLY A 193 ILE A 196 1 O GLY A 193 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 N ARG A 252 O ILE A 230
SHEET 7 A 9 ALA A 292 VAL A 294 1 N LEU A 293 O VAL A 253
SHEET 8 A 9 PHE A 335 SER A 340 1 O PHE A 335 N VAL A 294
SHEET 9 A 9 SER A 12 LEU A 16 1 O ILE A 13 N 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 N LEU A 166 O CYS A 103
SHEET 1 E 4 PHE A 406 ASP A 411 0
SHEET 2 E 4 GLN A 416 ARG A 421 -1 O ALA A 418 N TYR A 410
SHEET 3 E 4 GLY A 425 ASN A 430 -1 O GLY A 425 N ARG A 421
SHEET 4 E 4 PHE A 487 HIS A 491 -1 O ILE A 488 N VAL A 428
SHEET 1 F 2 PHE A 436 GLN A 441 0
SHEET 2 F 2 LYS A 474 ILE A 479 -1 O ALA A 475 N LEU A 440
SHEET 1 G 2 GLY A 447 CYS A 450 0
SHEET 2 G 2 LYS A 466 VAL A 469 -1 O ILE A 467 N TYR A 449
SSBOND 1 CYS A 28 CYS A 86 1555 1555 2.03
SSBOND 2 CYS A 70 CYS A 115 1555 1555 2.05
SSBOND 3 CYS A 141 CYS A 160 1555 1555 2.04
SSBOND 4 CYS A 378 CYS A 384 1555 1555 2.03
SSBOND 5 CYS A 450 CYS A 462 1555 1555 2.02
LINK C PCA A 1 N TYR A 2 1555 1555 1.33
LINK OD1 ASN A 100 CA CA A 497 1555 1555 2.35
LINK O ARG A 158 CA CA A 497 1555 1555 2.51
LINK OD1 ASP A 167 CA CA A 497 1555 1555 2.44
LINK OD2 ASP A 167 CA CA A 497 1555 1555 2.60
LINK O HIS A 201 CA CA A 497 1555 1555 2.42
LINK CA CA A 497 O HOH A 540 1555 1555 2.42
LINK CA CA A 497 O HOH A 592 1555 1555 2.38
LINK CA CA A 497 O HOH A 607 1555 1555 2.28
CISPEP 1 ASN A 53 PRO A 54 0 -2.68
CISPEP 2 VAL A 129 PRO A 130 0 -5.37
SITE 1 AC1 7 ASN A 100 ARG A 158 ASP A 167 HIS A 201
SITE 2 AC1 7 HOH A 540 HOH A 592 HOH A 607
SITE 1 AC2 3 ARG A 195 ASN A 298 ARG A 337
CRYST1 52.295 75.250 135.018 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 0.019122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013289 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007406 0.00000
HETATM 1 N PCA A 1 12.131 59.032 0.768 1.00 23.69 N
HETATM 2 CA PCA A 1 11.658 58.487 2.090 1.00 23.80 C
HETATM 3 CB PCA A 1 11.982 57.003 2.148 1.00 23.90 C
HETATM 4 CG PCA A 1 13.153 56.808 1.203 1.00 23.59 C
HETATM 5 CD PCA A 1 13.017 57.985 0.268 1.00 24.69 C
HETATM 6 OE PCA A 1 13.599 58.005 -0.825 1.00 25.23 O
HETATM 7 C PCA A 1 12.386 59.143 3.260 1.00 23.74 C
HETATM 8 O PCA A 1 12.022 58.950 4.422 1.00 23.83 O
(ATOM LINES ARE NOT SHOWN.)
END
