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HEADER HYDROLASE 08-JUN-16 5L8S
TITLE THE CRYSTAL STRUCTURE OF A COLD-ADAPTED ACYLAMINOACYL PEPTIDASE
TITLE 2 REVEALS A NOVEL QUATERNARY ARCHITECTURE BASED ON THE ARM-EXCHANGE
TITLE 3 MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINO ACYL PEPTIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PEPTIDASE S9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPOROSARCINA PSYCHROPHILA;
SOURCE 3 ORGANISM_TAXID: 1476;
SOURCE 4 GENE: APH, AZE41_09720;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACYL AMINOACYL PEPTIDASE, ALPHA/BETA HYDROLASE DOMAIN, ARM EXCHANGE,
KEYWDS 2 BETA-PROPELLER DOMAIN, COLD ADAPTATION, DIMERIZATION, PROLINE HINGE,
KEYWDS 3 SPOROSARCINA PSYCHROPHILA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BROCCA,C.FERRARI,A.BARBIROLI,A.PESCE,M.LOTTI,M.NARDINI
REVDAT 1 16-NOV-16 5L8S 0
JRNL AUTH S.BROCCA,C.FERRARI,A.BARBIROLI,A.PESCE,M.LOTTI,M.NARDINI
JRNL TITL A BACTERIAL ACYL AMINOACYL PEPTIDASE COUPLES FLEXIBILITY AND
JRNL TITL 2 STABILITY AS A RESULT OF COLD ADAPTATION.
JRNL REF FEBS J. 2016
JRNL REFN ISSN 1742-464X
JRNL PMID 27739253
JRNL DOI 10.1111/FEBS.13925
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 140806
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7433
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10301
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 545
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19524
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 476
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.37000
REMARK 3 B22 (A**2) : 0.36000
REMARK 3 B33 (A**2) : -0.73000
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): 0.311
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.238
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.174
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.858
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20113 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 18451 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27265 ; 1.282 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 42610 ; 0.727 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2426 ; 6.175 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1027 ;35.123 ;24.430
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3358 ;15.325 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;15.653 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2871 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22893 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4783 ; 0.001 ; 0.020
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): 9674 ; 2.282 ; 4.219
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9673 ; 2.280 ; 4.219
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12089 ; 3.658 ; 6.323
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 12090 ; 3.659 ; 6.323
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10439 ; 2.702 ; 4.555
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 10436 ; 2.689 ; 4.555
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 15164 ; 4.415 ; 6.685
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 22014 ; 6.374 ;33.424
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 21975 ; 6.365 ;33.419
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 : 1.20
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 5L8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93929
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 148344
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 63.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.39900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1VE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.1 M NA-HEPES (PH 7.5),
REMARK 280 AND 0.2 M MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 74.04000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.61500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.61500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.04000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.55000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 O LYS D 518 OH TYR D 524 2.11
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 ASN A 20 143.83 -179.63
REMARK 500 ARG A 58 -28.65 -157.22
REMARK 500 ASP A 79 -163.61 -111.45
REMARK 500 ASP A 83 -53.58 -27.43
REMARK 500 LEU A 101 -61.34 -123.87
REMARK 500 LYS A 128 -70.06 -43.44
REMARK 500 ASN A 130 74.44 -151.96
REMARK 500 LEU A 134 141.53 75.26
REMARK 500 VAL A 154 -61.36 74.15
REMARK 500 MET A 186 -67.01 -130.67
REMARK 500 ASP A 280 42.65 36.07
REMARK 500 SER A 383 -153.68 -130.91
REMARK 500 ASP A 425 54.44 -155.82
REMARK 500 GLU A 428 -85.21 -105.08
REMARK 500 SER A 458 -122.13 62.69
REMARK 500 HIS A 471 33.95 -142.26
REMARK 500 PHE A 482 67.15 27.54
REMARK 500 LEU A 506 -60.72 -107.58
REMARK 500 HIS A 603 93.87 -68.88
REMARK 500 ARG B 58 -35.86 -139.23
REMARK 500 ASP B 79 -156.29 -119.31
REMARK 500 ASP B 81 65.57 35.66
REMARK 500 GLU B 84 -9.76 66.48
REMARK 500 SER B 113 -53.00 -121.72
REMARK 500 LEU B 134 147.85 73.41
REMARK 500 VAL B 154 -47.28 80.39
REMARK 500 MET B 186 -50.62 -120.44
REMARK 500 SER B 383 -157.43 -132.88
REMARK 500 ASP B 425 59.26 -163.16
REMARK 500 GLU B 428 -79.11 -130.44
REMARK 500 ASN B 450 -0.33 70.50
REMARK 500 SER B 458 -119.93 65.78
REMARK 500 HIS B 471 40.73 -146.10
REMARK 500 PHE B 482 61.95 37.32
REMARK 500 ARG C 58 -27.41 -158.25
REMARK 500 ASP C 79 -161.51 -110.56
REMARK 500 LEU C 134 152.99 76.82
REMARK 500 VAL C 154 -61.08 67.53
REMARK 500 LYS C 258 53.79 35.23
REMARK 500 ASN C 321 17.82 -156.33
REMARK 500 ASP C 369 116.82 -35.55
REMARK 500 ASP C 425 70.81 -156.66
REMARK 500 GLU C 428 -85.31 -128.41
REMARK 500 SER C 458 -126.72 61.53
REMARK 500 HIS C 471 35.70 -149.00
REMARK 500 PHE C 482 64.05 30.83
REMARK 500 ARG D 58 -25.03 -158.39
REMARK 500 ASP D 79 -166.14 -108.79
REMARK 500 LYS D 128 -71.86 -37.18
REMARK 500 ASN D 130 71.12 -157.05
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 975 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A 976 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH A 977 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH B 907 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH C 905 DISTANCE = 7.36 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 701
DBREF 5L8S A 1 596 UNP E1VFE0 E1VFE0_SPOPS 1 596
DBREF 5L8S B 1 596 UNP E1VFE0 E1VFE0_SPOPS 1 596
DBREF 5L8S C 1 596 UNP E1VFE0 E1VFE0_SPOPS 1 596
DBREF 5L8S D 1 596 UNP E1VFE0 E1VFE0_SPOPS 1 596
SEQADV 5L8S LEU A 597 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S GLU A 598 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS A 599 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS A 600 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS A 601 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS A 602 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS A 603 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS A 604 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S LEU B 597 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S GLU B 598 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS B 599 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS B 600 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS B 601 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS B 602 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS B 603 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS B 604 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S LEU C 597 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S GLU C 598 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS C 599 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS C 600 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS C 601 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS C 602 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS C 603 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS C 604 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S LEU D 597 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S GLU D 598 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS D 599 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS D 600 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS D 601 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS D 602 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS D 603 UNP E1VFE0 EXPRESSION TAG
SEQADV 5L8S HIS D 604 UNP E1VFE0 EXPRESSION TAG
SEQRES 1 A 604 MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE
SEQRES 2 A 604 ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP
SEQRES 3 A 604 GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS
SEQRES 4 A 604 MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO
SEQRES 5 A 604 TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE
SEQRES 6 A 604 LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE
SEQRES 7 A 604 ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE
SEQRES 8 A 604 PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY
SEQRES 9 A 604 ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA
SEQRES 10 A 604 ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN
SEQRES 11 A 604 PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR
SEQRES 12 A 604 GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR
SEQRES 13 A 604 THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE
SEQRES 14 A 604 VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY
SEQRES 15 A 604 PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO
SEQRES 16 A 604 ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE
SEQRES 17 A 604 THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP
SEQRES 18 A 604 SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER
SEQRES 19 A 604 LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER
SEQRES 20 A 604 ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE
SEQRES 21 A 604 TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR
SEQRES 22 A 604 ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER
SEQRES 23 A 604 LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS
SEQRES 24 A 604 SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL
SEQRES 25 A 604 PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP
SEQRES 26 A 604 LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO
SEQRES 27 A 604 GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER
SEQRES 28 A 604 PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA
SEQRES 29 A 604 LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO
SEQRES 30 A 604 HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG
SEQRES 31 A 604 SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE
SEQRES 32 A 604 PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER
SEQRES 33 A 604 ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY
SEQRES 34 A 604 PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE
SEQRES 35 A 604 GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL
SEQRES 36 A 604 GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS
SEQRES 37 A 604 GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE
SEQRES 38 A 604 PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL
SEQRES 39 A 604 PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY
SEQRES 40 A 604 ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER
SEQRES 41 A 604 PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU
SEQRES 42 A 604 VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU
SEQRES 43 A 604 GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY
SEQRES 44 A 604 ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS
SEQRES 45 A 604 GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER
SEQRES 46 A 604 LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU
SEQRES 47 A 604 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 604 MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE
SEQRES 2 B 604 ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP
SEQRES 3 B 604 GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS
SEQRES 4 B 604 MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO
SEQRES 5 B 604 TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE
SEQRES 6 B 604 LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE
SEQRES 7 B 604 ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE
SEQRES 8 B 604 PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY
SEQRES 9 B 604 ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA
SEQRES 10 B 604 ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN
SEQRES 11 B 604 PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR
SEQRES 12 B 604 GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR
SEQRES 13 B 604 THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE
SEQRES 14 B 604 VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY
SEQRES 15 B 604 PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO
SEQRES 16 B 604 ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE
SEQRES 17 B 604 THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP
SEQRES 18 B 604 SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER
SEQRES 19 B 604 LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER
SEQRES 20 B 604 ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE
SEQRES 21 B 604 TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR
SEQRES 22 B 604 ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER
SEQRES 23 B 604 LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS
SEQRES 24 B 604 SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL
SEQRES 25 B 604 PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP
SEQRES 26 B 604 LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO
SEQRES 27 B 604 GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER
SEQRES 28 B 604 PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA
SEQRES 29 B 604 LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO
SEQRES 30 B 604 HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG
SEQRES 31 B 604 SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE
SEQRES 32 B 604 PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER
SEQRES 33 B 604 ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY
SEQRES 34 B 604 PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE
SEQRES 35 B 604 GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL
SEQRES 36 B 604 GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS
SEQRES 37 B 604 GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE
SEQRES 38 B 604 PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL
SEQRES 39 B 604 PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY
SEQRES 40 B 604 ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER
SEQRES 41 B 604 PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU
SEQRES 42 B 604 VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU
SEQRES 43 B 604 GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY
SEQRES 44 B 604 ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS
SEQRES 45 B 604 GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER
SEQRES 46 B 604 LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU
SEQRES 47 B 604 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 604 MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE
SEQRES 2 C 604 ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP
SEQRES 3 C 604 GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS
SEQRES 4 C 604 MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO
SEQRES 5 C 604 TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE
SEQRES 6 C 604 LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE
SEQRES 7 C 604 ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE
SEQRES 8 C 604 PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY
SEQRES 9 C 604 ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA
SEQRES 10 C 604 ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN
SEQRES 11 C 604 PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR
SEQRES 12 C 604 GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR
SEQRES 13 C 604 THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE
SEQRES 14 C 604 VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY
SEQRES 15 C 604 PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO
SEQRES 16 C 604 ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE
SEQRES 17 C 604 THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP
SEQRES 18 C 604 SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER
SEQRES 19 C 604 LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER
SEQRES 20 C 604 ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE
SEQRES 21 C 604 TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR
SEQRES 22 C 604 ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER
SEQRES 23 C 604 LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS
SEQRES 24 C 604 SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL
SEQRES 25 C 604 PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP
SEQRES 26 C 604 LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO
SEQRES 27 C 604 GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER
SEQRES 28 C 604 PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA
SEQRES 29 C 604 LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO
SEQRES 30 C 604 HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG
SEQRES 31 C 604 SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE
SEQRES 32 C 604 PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER
SEQRES 33 C 604 ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY
SEQRES 34 C 604 PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE
SEQRES 35 C 604 GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL
SEQRES 36 C 604 GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS
SEQRES 37 C 604 GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE
SEQRES 38 C 604 PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL
SEQRES 39 C 604 PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY
SEQRES 40 C 604 ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER
SEQRES 41 C 604 PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU
SEQRES 42 C 604 VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU
SEQRES 43 C 604 GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY
SEQRES 44 C 604 ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS
SEQRES 45 C 604 GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER
SEQRES 46 C 604 LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU
SEQRES 47 C 604 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 604 MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE
SEQRES 2 D 604 ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP
SEQRES 3 D 604 GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS
SEQRES 4 D 604 MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO
SEQRES 5 D 604 TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE
SEQRES 6 D 604 LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE
SEQRES 7 D 604 ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE
SEQRES 8 D 604 PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY
SEQRES 9 D 604 ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA
SEQRES 10 D 604 ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN
SEQRES 11 D 604 PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR
SEQRES 12 D 604 GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR
SEQRES 13 D 604 THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE
SEQRES 14 D 604 VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY
SEQRES 15 D 604 PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO
SEQRES 16 D 604 ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE
SEQRES 17 D 604 THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP
SEQRES 18 D 604 SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER
SEQRES 19 D 604 LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER
SEQRES 20 D 604 ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE
SEQRES 21 D 604 TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR
SEQRES 22 D 604 ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER
SEQRES 23 D 604 LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS
SEQRES 24 D 604 SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL
SEQRES 25 D 604 PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP
SEQRES 26 D 604 LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO
SEQRES 27 D 604 GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER
SEQRES 28 D 604 PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA
SEQRES 29 D 604 LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO
SEQRES 30 D 604 HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG
SEQRES 31 D 604 SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE
SEQRES 32 D 604 PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER
SEQRES 33 D 604 ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY
SEQRES 34 D 604 PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE
SEQRES 35 D 604 GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL
SEQRES 36 D 604 GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS
SEQRES 37 D 604 GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE
SEQRES 38 D 604 PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL
SEQRES 39 D 604 PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY
SEQRES 40 D 604 ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER
SEQRES 41 D 604 PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU
SEQRES 42 D 604 VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU
SEQRES 43 D 604 GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY
SEQRES 44 D 604 ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS
SEQRES 45 D 604 GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER
SEQRES 46 D 604 LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU
SEQRES 47 D 604 HIS HIS HIS HIS HIS HIS
HET SO4 A 701 5
HET SO4 B 701 5
HET SO4 C 701 5
HET SO4 D 701 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 9 HOH *476(H2 O)
HELIX 1 AA1 THR A 8 ARG A 14 5 7
HELIX 2 AA2 LYS A 255 ASN A 257 5 3
HELIX 3 AA3 SER A 337 MET A 341 5 5
HELIX 4 AA4 ARG A 390 GLY A 400 1 11
HELIX 5 AA5 GLY A 415 LEU A 421 1 7
HELIX 6 AA6 GLU A 428 GLY A 445 1 18
HELIX 7 AA7 SER A 458 SER A 472 1 15
HELIX 8 AA8 ASP A 473 PHE A 475 5 3
HELIX 9 AA9 ASP A 486 VAL A 494 1 9
HELIX 10 AB1 PRO A 495 HIS A 497 5 3
HELIX 11 AB2 TRP A 498 LEU A 506 1 9
HELIX 12 AB3 ASP A 512 SER A 520 1 9
HELIX 13 AB4 PRO A 521 MET A 528 5 8
HELIX 14 AB5 LYS A 545 LYS A 558 1 14
HELIX 15 AB6 LYS A 576 HIS A 594 1 19
HELIX 16 AB7 THR B 8 THR B 15 5 8
HELIX 17 AB8 SER B 337 MET B 341 5 5
HELIX 18 AB9 ARG B 390 GLY B 400 1 11
HELIX 19 AC1 GLY B 415 LEU B 421 1 7
HELIX 20 AC2 GLU B 428 GLY B 445 1 18
HELIX 21 AC3 SER B 458 SER B 472 1 15
HELIX 22 AC4 ASP B 473 PHE B 475 5 3
HELIX 23 AC5 ASP B 486 VAL B 494 1 9
HELIX 24 AC6 PRO B 495 HIS B 497 5 3
HELIX 25 AC7 TRP B 498 LEU B 506 1 9
HELIX 26 AC8 ASP B 512 ASP B 519 1 8
HELIX 27 AC9 SER B 520 MET B 528 5 9
HELIX 28 AD1 VAL B 544 GLU B 557 1 14
HELIX 29 AD2 LYS B 576 HIS B 594 1 19
HELIX 30 AD3 THR C 8 PHE C 13 5 6
HELIX 31 AD4 SER C 337 MET C 341 5 5
HELIX 32 AD5 ARG C 390 ARG C 399 1 10
HELIX 33 AD6 GLY C 415 LEU C 421 1 7
HELIX 34 AD7 GLU C 428 GLY C 445 1 18
HELIX 35 AD8 SER C 458 SER C 472 1 15
HELIX 36 AD9 ASP C 473 PHE C 475 5 3
HELIX 37 AE1 ASP C 486 VAL C 494 1 9
HELIX 38 AE2 PRO C 495 HIS C 497 5 3
HELIX 39 AE3 TRP C 498 LEU C 506 1 9
HELIX 40 AE4 ASP C 512 ASP C 519 1 8
HELIX 41 AE5 SER C 520 MET C 528 5 9
HELIX 42 AE6 VAL C 544 LYS C 558 1 15
HELIX 43 AE7 LYS C 576 HIS C 594 1 19
HELIX 44 AE8 THR D 8 PHE D 13 5 6
HELIX 45 AE9 LYS D 255 ASN D 257 5 3
HELIX 46 AF1 SER D 337 MET D 341 5 5
HELIX 47 AF2 ARG D 390 GLY D 400 1 11
HELIX 48 AF3 GLY D 415 LYS D 420 1 6
HELIX 49 AF4 LEU D 421 GLU D 423 5 3
HELIX 50 AF5 GLU D 428 GLY D 445 1 18
HELIX 51 AF6 SER D 458 SER D 472 1 15
HELIX 52 AF7 ASP D 473 PHE D 475 5 3
HELIX 53 AF8 ASP D 486 VAL D 494 1 9
HELIX 54 AF9 PRO D 495 HIS D 497 5 3
HELIX 55 AG1 TRP D 498 LEU D 506 1 9
HELIX 56 AG2 ASP D 512 ASP D 519 1 8
HELIX 57 AG3 SER D 520 MET D 528 5 9
HELIX 58 AG4 VAL D 544 LYS D 558 1 15
HELIX 59 AG5 LYS D 576 HIS D 594 1 19
SHEET 1 AA1 4 ILE A 18 VAL A 23 0
SHEET 2 AA1 4 LEU A 30 ALA A 34 -1 O ASN A 33 N ASN A 20
SHEET 3 AA1 4 ASN A 41 MET A 45 -1 O TRP A 43 N PHE A 32
SHEET 4 AA1 4 TYR A 53 ALA A 56 -1 O TYR A 53 N ALA A 44
SHEET 1 AA2 4 CYS A 62 PHE A 67 0
SHEET 2 AA2 4 VAL A 74 PHE A 78 -1 O LEU A 75 N LYS A 66
SHEET 3 AA2 4 GLN A 87 ILE A 91 -1 O TYR A 89 N ALA A 76
SHEET 4 AA2 4 HIS A 99 ILE A 102 -1 O HIS A 99 N ALA A 90
SHEET 1 AA3 4 TYR A 110 LEU A 115 0
SHEET 2 AA3 4 CYS A 121 THR A 126 -1 O TYR A 123 N HIS A 114
SHEET 3 AA3 4 ASN A 135 ASN A 140 -1 O ARG A 139 N VAL A 122
SHEET 4 AA3 4 ASP A 146 VAL A 151 -1 O LEU A 149 N THR A 136
SHEET 1 AA4 4 THR A 156 VAL A 162 0
SHEET 2 AA4 4 PHE A 169 ALA A 176 -1 O LEU A 172 N GLU A 158
SHEET 3 AA4 4 TYR A 179 LYS A 185 -1 O PHE A 183 N TYR A 171
SHEET 4 AA4 4 THR A 190 ASN A 192 -1 O PHE A 191 N VAL A 184
SHEET 1 AA5 4 ALA A 203 ASP A 210 0
SHEET 2 AA5 4 THR A 213 THR A 218 -1 O ALA A 217 N MET A 204
SHEET 3 AA5 4 TYR A 226 ASP A 231 -1 O TYR A 226 N THR A 218
SHEET 4 AA5 4 GLU A 236 LEU A 241 -1 O LEU A 241 N LEU A 227
SHEET 1 AA6 4 SER A 247 ASP A 254 0
SHEET 2 AA6 4 ALA A 259 LYS A 266 -1 O ALA A 259 N ASP A 254
SHEET 3 AA6 4 THR A 269 ASP A 276 -1 O TYR A 275 N PHE A 260
SHEET 4 AA6 4 LYS A 281 GLU A 284 -1 O GLU A 283 N ARG A 274
SHEET 1 AA7 4 ILE A 291 VAL A 297 0
SHEET 2 AA7 4 LEU A 303 ARG A 308 -1 O LEU A 306 N GLU A 293
SHEET 3 AA7 4 ASN A 315 SER A 319 -1 O SER A 319 N LEU A 303
SHEET 4 AA7 4 LYS A 326 GLN A 327 -1 O LYS A 326 N GLN A 318
SHEET 1 AA8 8 ASP A 345 THR A 350 0
SHEET 2 AA8 8 GLU A 356 PHE A 362 -1 O ILE A 357 N TYR A 349
SHEET 3 AA8 8 THR A 402 PRO A 406 -1 O ILE A 403 N PHE A 362
SHEET 4 AA8 8 THR A 373 PHE A 375 1 N ILE A 374 O THR A 402
SHEET 5 AA8 8 LEU A 452 GLY A 457 1 O PHE A 453 N THR A 373
SHEET 6 AA8 8 ALA A 477 ILE A 481 1 O ILE A 481 N GLY A 456
SHEET 7 AA8 8 MET A 532 GLY A 537 1 O LEU A 533 N ASP A 480
SHEET 8 AA8 8 VAL A 562 LEU A 567 1 O GLU A 563 N VAL A 534
SHEET 1 AA9 4 ILE B 18 VAL B 23 0
SHEET 2 AA9 4 LEU B 30 ALA B 34 -1 O ASN B 33 N ASN B 20
SHEET 3 AA9 4 ASN B 41 MET B 45 -1 O TRP B 43 N PHE B 32
SHEET 4 AA9 4 TYR B 53 ALA B 56 -1 O PHE B 55 N LEU B 42
SHEET 1 AB1 4 CYS B 62 PHE B 67 0
SHEET 2 AB1 4 TYR B 73 PHE B 78 -1 O LEU B 75 N LYS B 66
SHEET 3 AB1 4 GLN B 87 PRO B 92 -1 O ILE B 91 N VAL B 74
SHEET 4 AB1 4 HIS B 99 ILE B 102 -1 O HIS B 99 N ALA B 90
SHEET 1 AB2 4 TYR B 110 LEU B 115 0
SHEET 2 AB2 4 CYS B 121 THR B 126 -1 O TYR B 123 N HIS B 114
SHEET 3 AB2 4 ASN B 135 ASN B 140 -1 O ARG B 137 N TYR B 124
SHEET 4 AB2 4 ASP B 146 VAL B 151 -1 O LEU B 149 N THR B 136
SHEET 1 AB3 4 THR B 156 VAL B 162 0
SHEET 2 AB3 4 PHE B 169 ALA B 176 -1 O VAL B 170 N ALA B 161
SHEET 3 AB3 4 TYR B 179 LYS B 185 -1 O TYR B 179 N PHE B 175
SHEET 4 AB3 4 THR B 190 ASN B 192 -1 O PHE B 191 N VAL B 184
SHEET 1 AB4 4 ALA B 203 PHE B 208 0
SHEET 2 AB4 4 THR B 213 THR B 218 -1 O ALA B 217 N MET B 204
SHEET 3 AB4 4 TYR B 226 ASP B 231 -1 O TYR B 226 N THR B 218
SHEET 4 AB4 4 GLU B 236 LEU B 241 -1 O LEU B 241 N LEU B 227
SHEET 1 AB5 4 SER B 247 ASP B 254 0
SHEET 2 AB5 4 ALA B 259 LYS B 266 -1 O ALA B 259 N ASP B 254
SHEET 3 AB5 4 THR B 269 ASP B 276 -1 O TYR B 273 N LEU B 262
SHEET 4 AB5 4 LYS B 281 CYS B 285 -1 O CYS B 285 N LEU B 272
SHEET 1 AB6 4 ILE B 291 VAL B 297 0
SHEET 2 AB6 4 LEU B 303 ARG B 308 -1 O LEU B 306 N GLU B 293
SHEET 3 AB6 4 ASN B 315 SER B 319 -1 O SER B 319 N LEU B 303
SHEET 4 AB6 4 LYS B 326 GLN B 327 -1 O LYS B 326 N GLN B 318
SHEET 1 AB7 8 ASP B 345 THR B 350 0
SHEET 2 AB7 8 GLU B 356 PHE B 362 -1 O LEU B 361 N ASP B 345
SHEET 3 AB7 8 THR B 402 PRO B 406 -1 O ALA B 405 N LEU B 360
SHEET 4 AB7 8 THR B 373 PHE B 375 1 N ILE B 374 O PHE B 404
SHEET 5 AB7 8 LEU B 452 GLY B 457 1 O PHE B 453 N THR B 373
SHEET 6 AB7 8 ALA B 477 ILE B 481 1 O ILE B 481 N GLY B 456
SHEET 7 AB7 8 MET B 532 GLY B 537 1 O LEU B 533 N ASP B 480
SHEET 8 AB7 8 VAL B 562 LEU B 567 1 O GLU B 563 N VAL B 534
SHEET 1 AB8 4 ILE C 18 VAL C 23 0
SHEET 2 AB8 4 LEU C 30 ALA C 34 -1 O VAL C 31 N ALA C 22
SHEET 3 AB8 4 ASN C 41 MET C 45 -1 O TRP C 43 N PHE C 32
SHEET 4 AB8 4 TYR C 53 ALA C 56 -1 O PHE C 55 N LEU C 42
SHEET 1 AB9 4 CYS C 62 PHE C 67 0
SHEET 2 AB9 4 TYR C 73 PHE C 78 -1 O LEU C 75 N LYS C 66
SHEET 3 AB9 4 GLN C 87 PRO C 92 -1 O ILE C 91 N VAL C 74
SHEET 4 AB9 4 HIS C 99 ILE C 102 -1 O HIS C 99 N ALA C 90
SHEET 1 AC1 4 TYR C 110 LEU C 115 0
SHEET 2 AC1 4 CYS C 121 THR C 126 -1 O TYR C 123 N HIS C 114
SHEET 3 AC1 4 ASN C 135 ASN C 140 -1 O ARG C 139 N VAL C 122
SHEET 4 AC1 4 ASP C 146 VAL C 151 -1 O LEU C 149 N THR C 136
SHEET 1 AC2 4 THR C 156 VAL C 162 0
SHEET 2 AC2 4 SER C 168 ALA C 176 -1 O LEU C 172 N GLU C 158
SHEET 3 AC2 4 TYR C 179 MET C 186 -1 O TYR C 179 N PHE C 175
SHEET 4 AC2 4 GLU C 189 ASN C 192 -1 O PHE C 191 N VAL C 184
SHEET 1 AC3 4 ALA C 203 ASP C 210 0
SHEET 2 AC3 4 THR C 213 THR C 218 -1 O ALA C 217 N MET C 204
SHEET 3 AC3 4 TYR C 226 ASP C 231 -1 O TYR C 226 N THR C 218
SHEET 4 AC3 4 GLU C 236 LEU C 241 -1 O LEU C 241 N LEU C 227
SHEET 1 AC4 4 SER C 247 ASP C 254 0
SHEET 2 AC4 4 ALA C 259 LYS C 266 -1 O ALA C 259 N ASP C 254
SHEET 3 AC4 4 THR C 269 ASP C 276 -1 O TYR C 273 N LEU C 262
SHEET 4 AC4 4 LYS C 281 GLU C 284 -1 O GLU C 283 N ARG C 274
SHEET 1 AC5 4 ILE C 291 VAL C 297 0
SHEET 2 AC5 4 LEU C 303 SER C 309 -1 O LEU C 306 N GLU C 293
SHEET 3 AC5 4 VAL C 312 SER C 319 -1 O SER C 319 N LEU C 303
SHEET 4 AC5 4 LYS C 326 GLN C 327 -1 O LYS C 326 N GLN C 318
SHEET 1 AC6 8 ASP C 345 THR C 350 0
SHEET 2 AC6 8 GLU C 356 PHE C 362 -1 O LEU C 361 N ASP C 345
SHEET 3 AC6 8 THR C 402 PRO C 406 -1 O ILE C 403 N PHE C 362
SHEET 4 AC6 8 THR C 373 PHE C 375 1 N ILE C 374 O THR C 402
SHEET 5 AC6 8 LEU C 452 GLY C 457 1 O PHE C 453 N THR C 373
SHEET 6 AC6 8 VAL C 478 ILE C 481 1 O ILE C 481 N GLY C 456
SHEET 7 AC6 8 MET C 532 GLY C 537 1 O LEU C 533 N VAL C 478
SHEET 8 AC6 8 VAL C 562 LEU C 567 1 O LEU C 565 N VAL C 534
SHEET 1 AC7 4 ILE D 18 VAL D 23 0
SHEET 2 AC7 4 LEU D 30 ALA D 34 -1 O VAL D 31 N ALA D 22
SHEET 3 AC7 4 ASN D 41 MET D 45 -1 O TRP D 43 N PHE D 32
SHEET 4 AC7 4 TYR D 53 ALA D 56 -1 O PHE D 55 N LEU D 42
SHEET 1 AC8 4 CYS D 62 PHE D 67 0
SHEET 2 AC8 4 VAL D 74 PHE D 78 -1 O LEU D 75 N LYS D 66
SHEET 3 AC8 4 GLN D 87 ILE D 91 -1 O TYR D 89 N ALA D 76
SHEET 4 AC8 4 HIS D 99 ILE D 102 -1 O ILE D 102 N ILE D 88
SHEET 1 AC9 4 TYR D 110 LEU D 115 0
SHEET 2 AC9 4 CYS D 121 THR D 126 -1 O TYR D 123 N HIS D 114
SHEET 3 AC9 4 ASN D 135 ASN D 140 -1 O ARG D 137 N TYR D 124
SHEET 4 AC9 4 ASP D 146 VAL D 151 -1 O ASN D 150 N THR D 136
SHEET 1 AD1 4 THR D 156 VAL D 162 0
SHEET 2 AD1 4 SER D 168 ALA D 176 -1 O VAL D 170 N ALA D 161
SHEET 3 AD1 4 TYR D 179 MET D 186 -1 O TYR D 179 N PHE D 175
SHEET 4 AD1 4 GLU D 189 ASN D 192 -1 O PHE D 191 N VAL D 184
SHEET 1 AD2 4 ALA D 203 ASP D 210 0
SHEET 2 AD2 4 THR D 213 THR D 218 -1 O ALA D 217 N MET D 204
SHEET 3 AD2 4 TYR D 226 ASP D 231 -1 O TYR D 226 N THR D 218
SHEET 4 AD2 4 GLU D 236 LEU D 241 -1 O LEU D 241 N LEU D 227
SHEET 1 AD3 4 SER D 247 ASP D 254 0
SHEET 2 AD3 4 ALA D 259 LYS D 266 -1 O ALA D 259 N ASP D 254
SHEET 3 AD3 4 THR D 269 ASP D 276 -1 O THR D 269 N LYS D 266
SHEET 4 AD3 4 LYS D 281 GLU D 284 -1 O GLU D 283 N ARG D 274
SHEET 1 AD4 4 ILE D 291 VAL D 297 0
SHEET 2 AD4 4 LEU D 303 SER D 309 -1 O LEU D 306 N GLU D 293
SHEET 3 AD4 4 VAL D 312 SER D 319 -1 O SER D 319 N LEU D 303
SHEET 4 AD4 4 LYS D 326 GLN D 327 -1 O LYS D 326 N GLN D 318
SHEET 1 AD5 8 ASP D 345 THR D 350 0
SHEET 2 AD5 8 GLU D 356 PHE D 362 -1 O LEU D 361 N ASP D 345
SHEET 3 AD5 8 THR D 402 PRO D 406 -1 O ILE D 403 N PHE D 362
SHEET 4 AD5 8 THR D 373 PHE D 375 1 N ILE D 374 O THR D 402
SHEET 5 AD5 8 LEU D 452 GLY D 457 1 O PHE D 453 N THR D 373
SHEET 6 AD5 8 VAL D 478 ILE D 481 1 O VAL D 479 N LEU D 454
SHEET 7 AD5 8 MET D 532 GLY D 537 1 O LEU D 533 N ASP D 480
SHEET 8 AD5 8 VAL D 562 LEU D 567 1 O LEU D 565 N VAL D 534
CISPEP 1 LEU A 47 PRO A 48 0 4.39
CISPEP 2 GLY A 380 PRO A 381 0 0.00
CISPEP 3 LEU B 47 PRO B 48 0 4.47
CISPEP 4 GLY B 380 PRO B 381 0 0.38
CISPEP 5 LEU C 47 PRO C 48 0 6.55
CISPEP 6 GLY C 380 PRO C 381 0 3.26
CISPEP 7 LEU D 47 PRO D 48 0 4.13
CISPEP 8 GLY D 380 PRO D 381 0 4.40
SITE 1 AC1 5 ASP A 369 GLY A 371 GLY A 445 PHE A 446
SITE 2 AC1 5 ASP A 448
SITE 1 AC2 5 GLY B 371 GLY B 445 PHE B 446 THR B 447
SITE 2 AC2 5 ASP B 448
SITE 1 AC3 5 ASP C 369 GLY C 371 GLY C 445 PHE C 446
SITE 2 AC3 5 ASP C 448
SITE 1 AC4 5 ASP D 369 GLY D 371 GLY D 445 PHE D 446
SITE 2 AC4 5 ASP D 448
CRYST1 148.080 151.100 191.230 90.00 90.00 90.00 P 21 21 21 16
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 0.006753 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005229 0.00000
TER 4894 HIS A 604
TER 9788 HIS B 604
TER 14676 HIS C 604
TER 19570 HIS D 604
MASTER 363 0 4 59 144 0 8 620020 4 20 188
END |