HEADER LYASE 22-MAR-11 3R6Q
TITLE A TRICLINIC-LATTICE STRUCTURE OF ASPARTASE FROM BACILLUS SP. YM55-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 4.3.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 96471;
SOURCE 4 STRAIN: YM55-1;
SOURCE 5 GENE: ASPB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAD/MYC-HIS A
KEYWDS ASPARTASE, ASPARTATE AMMONIA LYASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.FIBRIANSAH,V.PUTHAN VEETIL,G.J.POELARENDS,A.-M.W.H.THUNNISSEN
REVDAT 3 13-SEP-23 3R6Q 1 REMARK SEQADV LINK
REVDAT 2 10-AUG-11 3R6Q 1 JRNL
REVDAT 1 13-JUL-11 3R6Q 0
JRNL AUTH G.FIBRIANSAH,V.P.VEETIL,G.J.POELARENDS,A.M.THUNNISSEN
JRNL TITL STRUCTURAL BASIS FOR THE CATALYTIC MECHANISM OF ASPARTATE
JRNL TITL 2 AMMONIA LYASE.
JRNL REF BIOCHEMISTRY V. 50 6053 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21661762
JRNL DOI 10.1021/BI200497Y
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 3 NUMBER OF REFLECTIONS : 161826
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8118
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11681
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 617
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 28552
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 888
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : -0.42000
REMARK 3 B12 (A**2) : 0.12000
REMARK 3 B13 (A**2) : -0.18000
REMARK 3 B23 (A**2) : -0.16000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.282
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.178
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 29041 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 39301 ; 1.211 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3709 ; 5.096 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1291 ;40.599 ;25.538
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5213 ;16.625 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 128 ;16.454 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4515 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21700 ; 0.005 ; 0.021
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): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): 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): 18382 ; 0.444 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 29705 ; 0.854 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10659 ; 1.378 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9595 ; 2.298 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 466
REMARK 3 RESIDUE RANGE : B 5 B 466
REMARK 3 RESIDUE RANGE : C 5 C 466
REMARK 3 RESIDUE RANGE : D 5 D 466
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0040 0.2530 0.0340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0170 T22: 0.0096
REMARK 3 T33: 0.0347 T12: 0.0026
REMARK 3 T13: -0.0076 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.2612 L22: 0.1043
REMARK 3 L33: 0.2354 L12: 0.0196
REMARK 3 L13: 0.0472 L23: 0.0182
REMARK 3 S TENSOR
REMARK 3 S11: 0.0410 S12: 0.0123 S13: -0.0117
REMARK 3 S21: 0.0073 S22: -0.0290 S23: -0.0042
REMARK 3 S31: 0.0555 S32: 0.0058 S33: -0.0120
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 5 E 466
REMARK 3 RESIDUE RANGE : F 4 F 466
REMARK 3 RESIDUE RANGE : G 5 G 466
REMARK 3 RESIDUE RANGE : H 5 H 466
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5840 50.1410 -70.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0169 T22: 0.0124
REMARK 3 T33: 0.0318 T12: 0.0032
REMARK 3 T13: 0.0017 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.2635 L22: 0.0939
REMARK 3 L33: 0.2261 L12: 0.0321
REMARK 3 L13: -0.0609 L23: -0.0233
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: 0.0117 S13: 0.0046
REMARK 3 S21: 0.0083 S22: -0.0305 S23: 0.0051
REMARK 3 S31: -0.0559 S32: -0.0083 S33: -0.0119
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3R6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064558.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : DIAMOND (111)AND GE (220)
REMARK 200 CRYSTALS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 161833
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 140.222
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.24600
REMARK 200 R SYM FOR SHELL (I) : 0.24600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 1J3U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M NASCN, 10 MM CACL2, 0.1 M
REMARK 280 HEPES, PH 7.0, 20% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 THR A 3
REMARK 465 ASP A 4
REMARK 465 ARG A 467
REMARK 465 LYS A 468
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 ASP B 4
REMARK 465 ARG B 467
REMARK 465 LYS B 468
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 THR C 3
REMARK 465 ASP C 4
REMARK 465 ARG C 467
REMARK 465 LYS C 468
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 THR D 3
REMARK 465 ASP D 4
REMARK 465 ARG D 467
REMARK 465 LYS D 468
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 THR E 3
REMARK 465 ASP E 4
REMARK 465 ARG E 467
REMARK 465 LYS E 468
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 THR F 3
REMARK 465 ARG F 467
REMARK 465 LYS F 468
REMARK 465 MET G 1
REMARK 465 ASN G 2
REMARK 465 THR G 3
REMARK 465 ASP G 4
REMARK 465 ARG G 467
REMARK 465 LYS G 468
REMARK 465 MET H 1
REMARK 465 ASN H 2
REMARK 465 THR H 3
REMARK 465 ASP H 4
REMARK 465 ARG H 467
REMARK 465 LYS H 468
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 OE1 GLU H 44 O HOH H 483 2.18
REMARK 500 OE2 GLU G 200 OE1 GLU H 357 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 ARG D 296 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG G 296 NE - CZ - NH2 ANGL. DEV. = -3.6 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 PHE A 11 -6.84 -56.74
REMARK 500 ALA A 192 -104.66 -114.97
REMARK 500 THR A 230 -152.61 52.68
REMARK 500 ASN A 237 -12.19 79.13
REMARK 500 SER A 300 151.82 -48.47
REMARK 500 ILE A 320 18.54 -154.91
REMARK 500 MET A 321 75.26 -170.39
REMARK 500 PHE A 356 -128.91 48.90
REMARK 500 CYS A 387 -61.52 -123.83
REMARK 500 ASN A 413 -56.88 -27.17
REMARK 500 GLU A 437 16.72 -68.74
REMARK 500 ALA A 465 -105.00 -139.30
REMARK 500 ILE B 36 -65.52 -93.76
REMARK 500 HIS B 134 -63.59 -105.04
REMARK 500 ALA B 192 -110.71 -124.13
REMARK 500 THR B 230 -157.76 44.71
REMARK 500 LEU B 236 108.29 -57.35
REMARK 500 ASN B 237 -6.01 94.21
REMARK 500 PHE B 356 -124.47 47.79
REMARK 500 CYS B 387 -67.68 -146.52
REMARK 500 ILE B 408 -31.86 -30.41
REMARK 500 LEU B 454 40.68 -87.15
REMARK 500 ILE C 36 -62.02 -95.42
REMARK 500 SER C 138 -6.57 71.44
REMARK 500 ALA C 192 -116.48 -121.42
REMARK 500 THR C 230 -162.51 49.57
REMARK 500 ASN C 237 -0.09 68.64
REMARK 500 PHE C 356 -123.29 47.44
REMARK 500 CYS C 387 -69.25 -153.60
REMARK 500 ILE C 408 -35.00 -24.71
REMARK 500 VAL C 416 -40.44 -141.48
REMARK 500 LEU C 454 31.67 -85.38
REMARK 500 ALA C 465 -92.45 -4.66
REMARK 500 HIS D 134 -60.05 -104.06
REMARK 500 SER D 138 16.63 60.00
REMARK 500 ASP D 143 -49.78 -133.29
REMARK 500 ALA D 192 -99.13 -125.07
REMARK 500 THR D 230 -158.63 51.64
REMARK 500 ASN D 237 -11.39 79.52
REMARK 500 MET D 321 60.52 -112.60
REMARK 500 PHE D 356 -127.17 46.65
REMARK 500 CYS D 387 -65.07 -132.58
REMARK 500 ASN D 413 -71.11 -24.55
REMARK 500 PHE E 11 -9.53 -58.95
REMARK 500 ILE E 36 -61.39 -92.07
REMARK 500 ALA E 192 -107.86 -119.30
REMARK 500 THR E 230 -151.14 54.28
REMARK 500 ASN E 237 -5.36 73.19
REMARK 500 PHE E 356 -126.19 48.79
REMARK 500 CYS E 387 -58.46 -135.31
REMARK 500
REMARK 500 THIS ENTRY HAS 76 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 469 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 393 O
REMARK 620 2 GLU A 395 OE1 73.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 469 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 67 OD2
REMARK 620 2 ALA H 393 O 146.6
REMARK 620 3 GLU H 395 OE1 140.3 73.0
REMARK 620 4 HOH H 851 O 83.5 121.0 64.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 469 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA D 393 O
REMARK 620 2 GLU D 395 OE1 64.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 469 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA E 393 O
REMARK 620 2 GLU E 395 OE2 75.7
REMARK 620 N 1
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 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 469
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R6V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ASPARTASE FROM BACILLUS SP. YM55-1 WITH BOUND
REMARK 900 L-ASPARTATE
REMARK 900 RELATED ID: 3R6Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHYMOTRYPSIN-TREATED ASPARTASE FROM BACILLUS
REMARK 900 SP. YM55-1
DBREF 3R6Q A 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
DBREF 3R6Q B 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
DBREF 3R6Q C 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
DBREF 3R6Q D 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
DBREF 3R6Q E 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
DBREF 3R6Q F 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
DBREF 3R6Q G 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
DBREF 3R6Q H 1 468 UNP Q9LCC6 Q9LCC6_9BACI 1 468
SEQADV 3R6Q ILE A 460 UNP Q9LCC6 THR 460 CONFLICT
SEQADV 3R6Q ILE B 460 UNP Q9LCC6 THR 460 CONFLICT
SEQADV 3R6Q ILE C 460 UNP Q9LCC6 THR 460 CONFLICT
SEQADV 3R6Q ILE D 460 UNP Q9LCC6 THR 460 CONFLICT
SEQADV 3R6Q ILE E 460 UNP Q9LCC6 THR 460 CONFLICT
SEQADV 3R6Q ILE F 460 UNP Q9LCC6 THR 460 CONFLICT
SEQADV 3R6Q ILE G 460 UNP Q9LCC6 THR 460 CONFLICT
SEQADV 3R6Q ILE H 460 UNP Q9LCC6 THR 460 CONFLICT
SEQRES 1 A 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 A 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 A 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 A 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 A 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 A 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 A 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 A 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 A 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 A 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 A 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 A 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 A 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 A 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 A 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 A 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 A 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 A 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 A 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 A 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 A 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 A 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 A 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 A 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 A 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 A 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 A 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 A 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 A 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 A 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 A 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 A 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 A 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 A 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 A 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 A 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
SEQRES 1 B 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 B 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 B 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 B 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 B 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 B 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 B 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 B 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 B 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 B 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 B 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 B 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 B 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 B 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 B 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 B 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 B 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 B 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 B 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 B 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 B 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 B 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 B 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 B 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 B 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 B 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 B 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 B 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 B 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 B 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 B 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 B 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 B 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 B 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 B 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 B 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
SEQRES 1 C 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 C 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 C 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 C 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 C 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 C 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 C 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 C 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 C 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 C 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 C 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 C 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 C 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 C 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 C 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 C 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 C 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 C 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 C 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 C 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 C 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 C 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 C 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 C 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 C 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 C 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 C 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 C 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 C 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 C 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 C 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 C 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 C 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 C 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 C 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 C 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
SEQRES 1 D 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 D 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 D 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 D 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 D 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 D 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 D 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 D 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 D 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 D 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 D 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 D 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 D 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 D 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 D 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 D 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 D 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 D 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 D 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 D 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 D 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 D 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 D 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 D 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 D 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 D 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 D 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 D 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 D 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 D 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 D 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 D 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 D 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 D 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 D 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 D 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
SEQRES 1 E 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 E 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 E 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 E 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 E 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 E 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 E 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 E 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 E 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 E 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 E 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 E 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 E 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 E 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 E 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 E 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 E 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 E 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 E 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 E 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 E 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 E 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 E 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 E 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 E 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 E 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 E 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 E 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 E 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 E 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 E 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 E 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 E 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 E 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 E 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 E 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
SEQRES 1 F 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 F 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 F 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 F 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 F 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 F 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 F 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 F 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 F 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 F 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 F 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 F 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 F 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 F 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 F 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 F 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 F 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 F 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 F 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 F 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 F 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 F 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 F 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 F 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 F 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 F 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 F 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 F 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 F 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 F 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 F 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 F 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 F 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 F 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 F 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 F 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
SEQRES 1 G 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 G 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 G 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 G 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 G 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 G 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 G 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 G 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 G 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 G 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 G 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 G 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 G 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 G 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 G 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 G 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 G 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 G 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 G 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 G 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 G 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 G 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 G 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 G 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 G 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 G 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 G 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 G 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 G 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 G 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 G 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 G 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 G 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 G 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 G 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 G 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
SEQRES 1 H 468 MET ASN THR ASP VAL ARG ILE GLU LYS ASP PHE LEU GLY
SEQRES 2 H 468 GLU LYS GLU ILE PRO LYS ASP ALA TYR TYR GLY VAL GLN
SEQRES 3 H 468 THR ILE ARG ALA THR GLU ASN PHE PRO ILE THR GLY TYR
SEQRES 4 H 468 ARG ILE HIS PRO GLU LEU ILE LYS SER LEU GLY ILE VAL
SEQRES 5 H 468 LYS LYS SER ALA ALA LEU ALA ASN MET GLU VAL GLY LEU
SEQRES 6 H 468 LEU ASP LYS GLU VAL GLY GLN TYR ILE VAL LYS ALA ALA
SEQRES 7 H 468 ASP GLU VAL ILE GLU GLY LYS TRP ASN ASP GLN PHE ILE
SEQRES 8 H 468 VAL ASP PRO ILE GLN GLY GLY ALA GLY THR SER ILE ASN
SEQRES 9 H 468 MET ASN ALA ASN GLU VAL ILE ALA ASN ARG ALA LEU GLU
SEQRES 10 H 468 LEU MET GLY GLU GLU LYS GLY ASN TYR SER LYS ILE SER
SEQRES 11 H 468 PRO ASN SER HIS VAL ASN MET SER GLN SER THR ASN ASP
SEQRES 12 H 468 ALA PHE PRO THR ALA THR HIS ILE ALA VAL LEU SER LEU
SEQRES 13 H 468 LEU ASN GLN LEU ILE GLU THR THR LYS TYR MET GLN GLN
SEQRES 14 H 468 GLU PHE MET LYS LYS ALA ASP GLU PHE ALA GLY VAL ILE
SEQRES 15 H 468 LYS MET GLY ARG THR HIS LEU GLN ASP ALA VAL PRO ILE
SEQRES 16 H 468 LEU LEU GLY GLN GLU PHE GLU ALA TYR ALA ARG VAL ILE
SEQRES 17 H 468 ALA ARG ASP ILE GLU ARG ILE ALA ASN THR ARG ASN ASN
SEQRES 18 H 468 LEU TYR ASP ILE ASN MET GLY ALA THR ALA VAL GLY THR
SEQRES 19 H 468 GLY LEU ASN ALA ASP PRO GLU TYR ILE SER ILE VAL THR
SEQRES 20 H 468 GLU HIS LEU ALA LYS PHE SER GLY HIS PRO LEU ARG SER
SEQRES 21 H 468 ALA GLN HIS LEU VAL ASP ALA THR GLN ASN THR ASP CYS
SEQRES 22 H 468 TYR THR GLU VAL SER SER ALA LEU LYS VAL CYS MET ILE
SEQRES 23 H 468 ASN MET SER LYS ILE ALA ASN ASP LEU ARG LEU MET ALA
SEQRES 24 H 468 SER GLY PRO ARG ALA GLY LEU SER GLU ILE VAL LEU PRO
SEQRES 25 H 468 ALA ARG GLN PRO GLY SER SER ILE MET PRO GLY LYS VAL
SEQRES 26 H 468 ASN PRO VAL MET PRO GLU VAL MET ASN GLN VAL ALA PHE
SEQRES 27 H 468 GLN VAL PHE GLY ASN ASP LEU THR ILE THR SER ALA SER
SEQRES 28 H 468 GLU ALA GLY GLN PHE GLU LEU ASN VAL MET GLU PRO VAL
SEQRES 29 H 468 LEU PHE PHE ASN LEU ILE GLN SER ILE SER ILE MET THR
SEQRES 30 H 468 ASN VAL PHE LYS SER PHE THR GLU ASN CYS LEU LYS GLY
SEQRES 31 H 468 ILE LYS ALA ASN GLU GLU ARG MET LYS GLU TYR VAL GLU
SEQRES 32 H 468 LYS SER ILE GLY ILE ILE THR ALA ILE ASN PRO HIS VAL
SEQRES 33 H 468 GLY TYR GLU THR ALA ALA LYS LEU ALA ARG GLU ALA TYR
SEQRES 34 H 468 LEU THR GLY GLU SER ILE ARG GLU LEU CYS ILE LYS TYR
SEQRES 35 H 468 GLY VAL LEU THR GLU GLU GLN LEU ASN GLU ILE LEU ASN
SEQRES 36 H 468 PRO TYR GLU MET ILE HIS PRO GLY ILE ALA GLY ARG LYS
HET CA A 469 1
HET CA D 469 1
HET CA E 469 1
HET CA H 469 1
HETNAM CA CALCIUM ION
FORMUL 9 CA 4(CA 2+)
FORMUL 13 HOH *888(H2 O)
HELIX 1 1 GLY A 24 PHE A 34 1 11
HELIX 2 2 HIS A 42 VAL A 63 1 22
HELIX 3 3 ASP A 67 GLU A 83 1 17
HELIX 4 4 TRP A 86 PHE A 90 5 5
HELIX 5 5 GLY A 100 MET A 119 1 20
HELIX 6 6 SER A 140 PHE A 178 1 39
HELIX 7 7 LEU A 197 THR A 218 1 22
HELIX 8 8 THR A 218 TYR A 223 1 6
HELIX 9 9 ASP A 239 GLY A 255 1 17
HELIX 10 10 HIS A 263 ASN A 270 1 8
HELIX 11 11 THR A 271 SER A 300 1 30
HELIX 12 12 PRO A 327 ALA A 353 1 27
HELIX 13 13 MET A 361 CYS A 387 1 27
HELIX 14 14 LEU A 388 ILE A 391 5 4
HELIX 15 15 ASN A 394 LYS A 404 1 11
HELIX 16 16 ILE A 408 THR A 431 1 24
HELIX 17 17 ILE A 435 ILE A 440 1 6
HELIX 18 18 THR A 446 LEU A 454 1 9
HELIX 19 19 ASN A 455 ILE A 460 1 6
HELIX 20 20 GLY B 24 PHE B 34 1 11
HELIX 21 21 HIS B 42 VAL B 63 1 22
HELIX 22 22 ASP B 67 GLU B 83 1 17
HELIX 23 23 TRP B 86 PHE B 90 5 5
HELIX 24 24 GLY B 100 GLY B 120 1 21
HELIX 25 25 SER B 140 PHE B 178 1 39
HELIX 26 26 LEU B 197 TYR B 223 1 27
HELIX 27 27 ASP B 239 GLY B 255 1 17
HELIX 28 28 HIS B 263 ASN B 270 1 8
HELIX 29 29 THR B 271 SER B 300 1 30
HELIX 30 30 PRO B 327 ALA B 353 1 27
HELIX 31 31 MET B 361 CYS B 387 1 27
HELIX 32 32 LEU B 388 ILE B 391 5 4
HELIX 33 33 ASN B 394 LYS B 404 1 11
HELIX 34 34 ILE B 408 ASN B 413 1 6
HELIX 35 35 PRO B 414 VAL B 416 5 3
HELIX 36 36 GLY B 417 GLY B 432 1 16
HELIX 37 37 SER B 434 TYR B 442 1 9
HELIX 38 38 THR B 446 LEU B 454 1 9
HELIX 39 39 TYR B 457 HIS B 461 5 5
HELIX 40 40 GLY C 24 PHE C 34 1 11
HELIX 41 41 HIS C 42 VAL C 63 1 22
HELIX 42 42 ASP C 67 GLU C 83 1 17
HELIX 43 43 TRP C 86 PHE C 90 5 5
HELIX 44 44 GLY C 100 MET C 119 1 20
HELIX 45 45 SER C 140 PHE C 178 1 39
HELIX 46 46 LEU C 197 THR C 218 1 22
HELIX 47 47 ARG C 219 TYR C 223 1 5
HELIX 48 48 ASP C 239 GLY C 255 1 17
HELIX 49 49 HIS C 263 ASN C 270 1 8
HELIX 50 50 THR C 271 SER C 300 1 30
HELIX 51 51 PRO C 327 ALA C 353 1 27
HELIX 52 52 MET C 361 CYS C 387 1 27
HELIX 53 53 LEU C 388 ILE C 391 5 4
HELIX 54 54 ASN C 394 LYS C 404 1 11
HELIX 55 55 ILE C 408 ASN C 413 1 6
HELIX 56 56 PRO C 414 VAL C 416 5 3
HELIX 57 57 GLY C 417 GLY C 432 1 16
HELIX 58 58 SER C 434 TYR C 442 1 9
HELIX 59 59 THR C 446 LEU C 454 1 9
HELIX 60 60 TYR C 457 HIS C 461 5 5
HELIX 61 61 GLY D 24 PHE D 34 1 11
HELIX 62 62 HIS D 42 VAL D 63 1 22
HELIX 63 63 ASP D 67 GLU D 83 1 17
HELIX 64 64 TRP D 86 PHE D 90 5 5
HELIX 65 65 GLY D 97 ALA D 99 5 3
HELIX 66 66 GLY D 100 MET D 119 1 20
HELIX 67 67 SER D 140 PHE D 178 1 39
HELIX 68 68 LEU D 197 THR D 218 1 22
HELIX 69 69 ARG D 219 LEU D 222 5 4
HELIX 70 70 ASP D 239 GLY D 255 1 17
HELIX 71 71 HIS D 263 ASN D 270 1 8
HELIX 72 72 THR D 271 SER D 300 1 30
HELIX 73 73 PRO D 327 ALA D 353 1 27
HELIX 74 74 MET D 361 CYS D 387 1 27
HELIX 75 75 LEU D 388 ILE D 391 5 4
HELIX 76 76 ASN D 394 LYS D 404 1 11
HELIX 77 77 ILE D 408 GLY D 432 1 25
HELIX 78 78 SER D 434 TYR D 442 1 9
HELIX 79 79 THR D 446 LEU D 454 1 9
HELIX 80 80 ASN D 455 ILE D 460 1 6
HELIX 81 81 GLY E 24 PHE E 34 1 11
HELIX 82 82 HIS E 42 VAL E 63 1 22
HELIX 83 83 ASP E 67 GLU E 83 1 17
HELIX 84 84 TRP E 86 PHE E 90 5 5
HELIX 85 85 GLY E 97 ALA E 99 5 3
HELIX 86 86 GLY E 100 MET E 119 1 20
HELIX 87 87 SER E 140 PHE E 178 1 39
HELIX 88 88 LEU E 197 THR E 218 1 22
HELIX 89 89 ARG E 219 LEU E 222 5 4
HELIX 90 90 ASP E 239 GLY E 255 1 17
HELIX 91 91 HIS E 263 ASN E 270 1 8
HELIX 92 92 THR E 271 SER E 300 1 30
HELIX 93 93 PRO E 327 ALA E 353 1 27
HELIX 94 94 MET E 361 CYS E 387 1 27
HELIX 95 95 LEU E 388 ILE E 391 5 4
HELIX 96 96 ASN E 394 LYS E 404 1 11
HELIX 97 97 ILE E 408 GLY E 432 1 25
HELIX 98 98 SER E 434 GLY E 443 1 10
HELIX 99 99 GLU E 448 LEU E 454 1 7
HELIX 100 100 TYR E 457 HIS E 461 5 5
HELIX 101 101 GLY F 24 PHE F 34 1 11
HELIX 102 102 HIS F 42 GLY F 64 1 23
HELIX 103 103 ASP F 67 GLU F 83 1 17
HELIX 104 104 TRP F 86 PHE F 90 5 5
HELIX 105 105 GLY F 100 MET F 119 1 20
HELIX 106 106 SER F 140 PHE F 178 1 39
HELIX 107 107 LEU F 197 THR F 218 1 22
HELIX 108 108 ARG F 219 LEU F 222 5 4
HELIX 109 109 ASP F 239 GLY F 255 1 17
HELIX 110 110 HIS F 263 ASN F 270 1 8
HELIX 111 111 THR F 271 SER F 300 1 30
HELIX 112 112 PRO F 327 ALA F 353 1 27
HELIX 113 113 MET F 361 CYS F 387 1 27
HELIX 114 114 LEU F 388 ILE F 391 5 4
HELIX 115 115 ASN F 394 LYS F 404 1 11
HELIX 116 116 ILE F 408 GLY F 417 1 10
HELIX 117 117 GLY F 417 GLY F 432 1 16
HELIX 118 118 SER F 434 TYR F 442 1 9
HELIX 119 119 THR F 446 LEU F 454 1 9
HELIX 120 120 TYR F 457 HIS F 461 5 5
HELIX 121 121 GLY G 24 PHE G 34 1 11
HELIX 122 122 HIS G 42 VAL G 63 1 22
HELIX 123 123 ASP G 67 GLU G 83 1 17
HELIX 124 124 TRP G 86 PHE G 90 5 5
HELIX 125 125 GLY G 100 MET G 119 1 20
HELIX 126 126 SER G 140 PHE G 178 1 39
HELIX 127 127 LEU G 197 THR G 218 1 22
HELIX 128 128 ARG G 219 TYR G 223 1 5
HELIX 129 129 ASP G 239 GLY G 255 1 17
HELIX 130 130 HIS G 263 ASN G 270 1 8
HELIX 131 131 THR G 271 ALA G 299 1 29
HELIX 132 132 PRO G 327 ALA G 353 1 27
HELIX 133 133 MET G 361 CYS G 387 1 27
HELIX 134 134 LEU G 388 ILE G 391 5 4
HELIX 135 135 ASN G 394 LYS G 404 1 11
HELIX 136 136 ILE G 408 GLY G 417 1 10
HELIX 137 137 GLY G 417 GLY G 432 1 16
HELIX 138 138 SER G 434 TYR G 442 1 9
HELIX 139 139 THR G 446 LEU G 454 1 9
HELIX 140 140 TYR G 457 HIS G 461 5 5
HELIX 141 141 GLY H 24 PHE H 34 1 11
HELIX 142 142 HIS H 42 VAL H 63 1 22
HELIX 143 143 ASP H 67 GLU H 83 1 17
HELIX 144 144 TRP H 86 PHE H 90 5 5
HELIX 145 145 GLY H 97 ALA H 99 5 3
HELIX 146 146 GLY H 100 MET H 119 1 20
HELIX 147 147 SER H 140 PHE H 178 1 39
HELIX 148 148 LEU H 197 THR H 218 1 22
HELIX 149 149 THR H 218 TYR H 223 1 6
HELIX 150 150 ASP H 239 GLY H 255 1 17
HELIX 151 151 HIS H 263 ASN H 270 1 8
HELIX 152 152 THR H 271 SER H 300 1 30
HELIX 153 153 PRO H 327 GLU H 352 1 26
HELIX 154 154 MET H 361 CYS H 387 1 27
HELIX 155 155 LEU H 388 ILE H 391 5 4
HELIX 156 156 ASN H 394 SER H 405 1 12
HELIX 157 157 ILE H 408 GLY H 417 1 10
HELIX 158 158 GLY H 417 GLY H 432 1 16
HELIX 159 159 SER H 434 TYR H 442 1 9
HELIX 160 160 THR H 446 LEU H 454 1 9
HELIX 161 161 TYR H 457 HIS H 461 5 5
SHEET 1 A 2 ARG A 6 ASP A 10 0
SHEET 2 A 2 GLY A 13 ILE A 17 -1 O LYS A 15 N GLU A 8
SHEET 1 B 2 ILE A 182 THR A 187 0
SHEET 2 B 2 GLN A 190 LEU A 196 -1 O ILE A 195 N LYS A 183
SHEET 1 C 2 ASP A 224 ILE A 225 0
SHEET 2 C 2 ARG A 259 SER A 260 1 O ARG A 259 N ILE A 225
SHEET 1 D 2 ILE A 309 VAL A 310 0
SHEET 2 D 2 LYS A 392 ALA A 393 -1 O LYS A 392 N VAL A 310
SHEET 1 E 2 ILE B 7 ASP B 10 0
SHEET 2 E 2 GLY B 13 GLU B 16 -1 O GLY B 13 N ASP B 10
SHEET 1 F 2 ILE B 182 THR B 187 0
SHEET 2 F 2 GLN B 190 LEU B 196 -1 O ILE B 195 N LYS B 183
SHEET 1 G 2 ASP B 224 ILE B 225 0
SHEET 2 G 2 ARG B 259 SER B 260 1 O ARG B 259 N ILE B 225
SHEET 1 H 2 ILE B 309 VAL B 310 0
SHEET 2 H 2 LYS B 392 ALA B 393 -1 O LYS B 392 N VAL B 310
SHEET 1 I 2 ARG C 6 LYS C 9 0
SHEET 2 I 2 GLU C 14 ILE C 17 -1 O LYS C 15 N GLU C 8
SHEET 1 J 2 ILE C 182 THR C 187 0
SHEET 2 J 2 GLN C 190 LEU C 196 -1 O ILE C 195 N LYS C 183
SHEET 1 K 2 ASP C 224 ILE C 225 0
SHEET 2 K 2 ARG C 259 SER C 260 1 O ARG C 259 N ILE C 225
SHEET 1 L 2 ILE C 309 VAL C 310 0
SHEET 2 L 2 LYS C 392 ALA C 393 -1 O LYS C 392 N VAL C 310
SHEET 1 M 2 ARG D 6 ASP D 10 0
SHEET 2 M 2 GLY D 13 ILE D 17 -1 O ILE D 17 N ARG D 6
SHEET 1 N 2 ILE D 182 THR D 187 0
SHEET 2 N 2 GLN D 190 LEU D 196 -1 O ILE D 195 N LYS D 183
SHEET 1 O 2 ASP D 224 ILE D 225 0
SHEET 2 O 2 ARG D 259 SER D 260 1 O ARG D 259 N ILE D 225
SHEET 1 P 2 ILE D 309 VAL D 310 0
SHEET 2 P 2 LYS D 392 ALA D 393 -1 O LYS D 392 N VAL D 310
SHEET 1 Q 2 ARG E 6 GLU E 8 0
SHEET 2 Q 2 LYS E 15 ILE E 17 -1 O LYS E 15 N GLU E 8
SHEET 1 R 2 ILE E 182 THR E 187 0
SHEET 2 R 2 GLN E 190 LEU E 196 -1 O ILE E 195 N LYS E 183
SHEET 1 S 2 ASP E 224 ILE E 225 0
SHEET 2 S 2 ARG E 259 SER E 260 1 O ARG E 259 N ILE E 225
SHEET 1 T 2 ILE E 309 VAL E 310 0
SHEET 2 T 2 LYS E 392 ALA E 393 -1 O LYS E 392 N VAL E 310
SHEET 1 U 2 VAL F 5 ASP F 10 0
SHEET 2 U 2 GLY F 13 PRO F 18 -1 O ILE F 17 N ARG F 6
SHEET 1 V 2 ILE F 182 THR F 187 0
SHEET 2 V 2 GLN F 190 LEU F 196 -1 O ILE F 195 N LYS F 183
SHEET 1 W 2 ASP F 224 ILE F 225 0
SHEET 2 W 2 ARG F 259 SER F 260 1 O ARG F 259 N ILE F 225
SHEET 1 X 2 ILE F 309 VAL F 310 0
SHEET 2 X 2 LYS F 392 ALA F 393 -1 O LYS F 392 N VAL F 310
SHEET 1 Y 2 ARG G 6 ASP G 10 0
SHEET 2 Y 2 GLY G 13 ILE G 17 -1 O ILE G 17 N ARG G 6
SHEET 1 Z 2 ILE G 182 THR G 187 0
SHEET 2 Z 2 GLN G 190 LEU G 196 -1 O ILE G 195 N LYS G 183
SHEET 1 AA 2 ASP G 224 ILE G 225 0
SHEET 2 AA 2 ARG G 259 SER G 260 1 O ARG G 259 N ILE G 225
SHEET 1 AB 2 ILE G 309 VAL G 310 0
SHEET 2 AB 2 LYS G 392 ALA G 393 -1 O LYS G 392 N VAL G 310
SHEET 1 AC 2 ARG H 6 ASP H 10 0
SHEET 2 AC 2 GLY H 13 ILE H 17 -1 O ILE H 17 N ARG H 6
SHEET 1 AD 2 ILE H 182 THR H 187 0
SHEET 2 AD 2 GLN H 190 LEU H 196 -1 O ILE H 195 N LYS H 183
SHEET 1 AE 2 ASP H 224 ILE H 225 0
SHEET 2 AE 2 ARG H 259 SER H 260 1 O ARG H 259 N ILE H 225
SHEET 1 AF 2 ILE H 309 VAL H 310 0
SHEET 2 AF 2 LYS H 392 ALA H 393 -1 O LYS H 392 N VAL H 310
LINK O ALA A 393 CA CA A 469 1555 1555 2.56
LINK OE1 GLU A 395 CA CA A 469 1555 1555 2.17
LINK OD2 ASP D 67 CA CA H 469 1555 1555 2.55
LINK O ALA D 393 CA CA D 469 1555 1555 2.54
LINK OE1 GLU D 395 CA CA D 469 1555 1555 2.15
LINK O ALA E 393 CA CA E 469 1555 1555 2.61
LINK OE2 GLU E 395 CA CA E 469 1555 1555 2.56
LINK O ALA H 393 CA CA H 469 1555 1555 2.46
LINK OE1 GLU H 395 CA CA H 469 1555 1555 2.52
LINK CA CA H 469 O HOH H 851 1555 1555 2.52
CISPEP 1 GLY A 301 PRO A 302 0 12.41
CISPEP 2 GLY B 301 PRO B 302 0 3.95
CISPEP 3 GLY C 301 PRO C 302 0 3.14
CISPEP 4 GLY D 301 PRO D 302 0 12.09
CISPEP 5 GLY E 301 PRO E 302 0 14.63
CISPEP 6 GLY F 301 PRO F 302 0 15.83
CISPEP 7 GLY G 301 PRO G 302 0 10.34
CISPEP 8 GLY H 301 PRO H 302 0 5.41
SITE 1 AC1 3 ALA A 393 GLU A 395 ASP E 67
SITE 1 AC2 3 ALA D 393 GLU D 395 ASP H 67
SITE 1 AC3 3 ASP A 67 ALA E 393 GLU E 395
SITE 1 AC4 4 ASP D 67 ALA H 393 GLU H 395 HOH H 851
CRYST1 75.594 118.194 140.226 89.85 89.59 76.51 P 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 0.013229 -0.003174 -0.000093 0.00000
SCALE2 0.000000 0.008701 -0.000008 0.00000
SCALE3 0.000000 0.000000 0.007132 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
