HEADER HYDROLASE 09-MAR-13 4JKK
TITLE CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE BETA-GLUCURONIDASE IN
TITLE 2 SPACE GROUP I222
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GLUCURONIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.31;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE;
SOURCE 3 ORGANISM_TAXID: 208435;
SOURCE 4 STRAIN: ATCC BAA-611 / 2603 V/R;
SOURCE 5 GENE: SAG0698;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-AI (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALPHA/BETA BARREL, BETA-SANDWICH, SUGAR-BINDING DOMAIN, GLYCOSYL
KEYWDS 2 HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.D.WALLACE,M.R.REDINBO
REVDAT 3 28-FEB-24 4JKK 1 REMARK SEQADV
REVDAT 2 21-OCT-15 4JKK 1 JRNL
REVDAT 1 17-SEP-14 4JKK 0
JRNL AUTH B.D.WALLACE,A.B.ROBERTS,R.M.POLLET,J.D.INGLE,K.A.BIERNAT,
JRNL AUTH 2 S.J.PELLOCK,M.K.VENKATESH,L.GUTHRIE,S.K.O'NEAL,S.J.ROBINSON,
JRNL AUTH 3 M.DOLLINGER,E.FIGUEROA,S.R.MCSHANE,R.D.COHEN,J.JIN,S.V.FRYE,
JRNL AUTH 4 W.C.ZAMBONI,C.PEPE-RANNEY,S.MANI,L.KELLY,M.R.REDINBO
JRNL TITL STRUCTURE AND INHIBITION OF MICROBIOME BETA-GLUCURONIDASES
JRNL TITL 2 ESSENTIAL TO THE ALLEVIATION OF CANCER DRUG TOXICITY.
JRNL REF CHEM.BIOL. V. 22 1238 2015
JRNL REFN ISSN 1074-5521
JRNL PMID 26364932
JRNL DOI 10.1016/J.CHEMBIOL.2015.08.005
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 18110
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 938
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) : 2.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1099
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.1640
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 295
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : 0.84000
REMARK 3 B33 (A**2) : -0.60000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.311
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.208
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.616
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4950 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6725 ; 1.436 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 600 ; 6.360 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 260 ;37.319 ;24.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 855 ;17.994 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;19.167 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 727 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3828 ; 0.006 ; 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): 2952 ; 0.926 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4799 ; 1.820 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1998 ; 2.731 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1919 ; 4.531 ; 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 : BABINET MODEL WITH 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: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4JKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078162.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL WITH K-B BIOMORPH
REMARK 200 MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18183
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 99.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-28% PEG 3350, 0.1-0.3 M KSCN, 0.02%
REMARK 280 SODIUM AZIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.91450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 99.66600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.91450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 99.66600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.91450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 99.66600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.91450
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 99.66600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 78440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG MG A 601 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 985 LIES ON A SPECIAL POSITION.
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 SER A -2
REMARK 465 PHE A 360
REMARK 465 ASN A 361
REMARK 465 ALA A 362
REMARK 465 SER A 363
REMARK 465 LEU A 364
REMARK 465 ASP A 365
REMARK 465 LEU A 366
REMARK 465 SER A 367
REMARK 465 PRO A 368
REMARK 465 LYS A 369
REMARK 465 SER A 597
REMARK 465 VAL A 598
REMARK 465 LYS A 599
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 70 CG CD CE NZ
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 ARG A 189 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 ARG A 213 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 257 CG OD1 OD2
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 CG GLU A 36 O HOH A 957 1.77
REMARK 500 OE1 GLU A 552 O HOH A 981 1.95
REMARK 500 NZ LYS A 425 O HOH A 960 2.03
REMARK 500 NE2 GLN A 358 O HOH A 908 2.07
REMARK 500 O HOH A 944 O HOH A 957 2.10
REMARK 500 O HOH A 864 O HOH A 865 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 42 154.08 174.20
REMARK 500 SER A 83 155.64 172.59
REMARK 500 GLU A 147 -4.28 71.16
REMARK 500 ASN A 158 34.72 -96.64
REMARK 500 ASP A 160 48.82 -100.92
REMARK 500 SER A 230 -6.79 79.67
REMARK 500 LEU A 243 13.97 54.85
REMARK 500 ASP A 262 143.71 -171.17
REMARK 500 ILE A 300 -66.88 72.65
REMARK 500 HIS A 329 54.68 -118.98
REMARK 500 PRO A 352 40.46 -77.12
REMARK 500 ASN A 371 -157.16 -179.85
REMARK 500 GLN A 378 48.03 -91.68
REMARK 500 TRP A 467 -58.67 -121.18
REMARK 500 TYR A 518 -22.07 93.96
REMARK 500 LYS A 595 25.59 124.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JKL RELATED DB: PDB
REMARK 900 RELATED ID: 4JKM RELATED DB: PDB
DBREF 4JKK A 1 599 UNP Q8E0N2 Q8E0N2_STRA5 1 599
SEQADV 4JKK SER A -2 UNP Q8E0N2 EXPRESSION TAG
SEQADV 4JKK ASN A -1 UNP Q8E0N2 EXPRESSION TAG
SEQADV 4JKK ALA A 0 UNP Q8E0N2 EXPRESSION TAG
SEQRES 1 A 602 SER ASN ALA MET LEU TYR PRO LEU LEU THR LYS THR ARG
SEQRES 2 A 602 ASN THR TYR ASP LEU GLY GLY ILE TRP ASN PHE LYS LEU
SEQRES 3 A 602 GLY GLU HIS ASN PRO ASN GLU LEU LEU PRO SER ASP GLU
SEQRES 4 A 602 VAL MET VAL ILE PRO THR SER PHE ASN ASP LEU MET VAL
SEQRES 5 A 602 SER LYS GLU LYS ARG ASP TYR ILE GLY ASP PHE TRP TYR
SEQRES 6 A 602 GLU LYS VAL ILE GLU VAL PRO LYS VAL SER GLU ASP GLU
SEQRES 7 A 602 GLU MET VAL LEU ARG PHE GLY SER VAL THR HIS GLN ALA
SEQRES 8 A 602 LYS ILE TYR VAL ASP GLY VAL LEU VAL GLY GLU HIS LYS
SEQRES 9 A 602 GLY GLY PHE THR PRO PHE GLU VAL LEU VAL PRO GLU CYS
SEQRES 10 A 602 LYS TYR ASN ASN GLU LYS ILE LYS VAL SER ILE CYS ALA
SEQRES 11 A 602 ASN ASN VAL LEU ASP TYR THR THR LEU PRO VAL GLY ASN
SEQRES 12 A 602 TYR SER GLU ILE ILE GLN GLU ASP GLY SER ILE LYS LYS
SEQRES 13 A 602 LYS VAL ARG GLU ASN PHE ASP PHE PHE ASN TYR ALA GLY
SEQRES 14 A 602 VAL HIS ARG PRO LEU LYS LEU MET ILE ARG PRO LYS ASN
SEQRES 15 A 602 HIS ILE PHE ASP ILE THR ILE THR SER ARG LEU SER ASP
SEQRES 16 A 602 ASP LEU GLN SER ALA ASP LEU HIS PHE LEU VAL GLU THR
SEQRES 17 A 602 ASN GLN LYS VAL ASP GLU VAL ARG ILE SER VAL PHE ASP
SEQRES 18 A 602 GLU ASP ASN LYS LEU VAL GLY GLU THR LYS ASP SER ARG
SEQRES 19 A 602 LEU PHE LEU SER ASP VAL HIS LEU TRP GLU VAL LEU ASN
SEQRES 20 A 602 ALA TYR LEU TYR THR ALA ARG VAL GLU ILE PHE VAL ASP
SEQRES 21 A 602 ASN GLN LEU GLN ASP VAL TYR GLU GLU ASN PHE GLY LEU
SEQRES 22 A 602 ARG GLU ILE GLU VAL THR ASN GLY GLN PHE LEU LEU ASN
SEQRES 23 A 602 ARG LYS PRO ILE TYR PHE LYS GLY PHE GLY LYS HIS GLU
SEQRES 24 A 602 ASP THR PHE ILE ASN GLY ARG GLY LEU ASN GLU ALA ALA
SEQRES 25 A 602 ASN LEU MET ASP LEU ASN LEU LEU LYS ASP MET GLY ALA
SEQRES 26 A 602 ASN SER PHE ARG THR SER HIS TYR PRO TYR SER GLU GLU
SEQRES 27 A 602 MET MET ARG LEU ALA ASP ARG MET GLY VAL LEU VAL ILE
SEQRES 28 A 602 ASP GLU VAL PRO ALA VAL GLY LEU PHE GLN ASN PHE ASN
SEQRES 29 A 602 ALA SER LEU ASP LEU SER PRO LYS ASP ASN GLY THR TRP
SEQRES 30 A 602 ASN LEU MET GLN THR LYS ALA ALA HIS GLU GLN ALA ILE
SEQRES 31 A 602 GLN GLU LEU VAL LYS ARG ASP LYS ASN HIS PRO SER VAL
SEQRES 32 A 602 VAL MET TRP VAL VAL ALA ASN GLU PRO ALA SER HIS GLU
SEQRES 33 A 602 ALA GLY ALA HIS ASP TYR PHE GLU PRO LEU VAL LYS LEU
SEQRES 34 A 602 TYR LYS ASP LEU ASP PRO GLN LYS ARG PRO VAL THR LEU
SEQRES 35 A 602 VAL ASN ILE LEU MET ALA THR PRO ASP ARG ASP GLN VAL
SEQRES 36 A 602 MET ASP LEU VAL ASP VAL VAL CYS LEU ASN ARG TYR TYR
SEQRES 37 A 602 GLY TRP TYR VAL ASP HIS GLY ASP LEU THR ASN ALA GLU
SEQRES 38 A 602 VAL GLY ILE ARG LYS GLU LEU LEU GLU TRP GLN ASP LYS
SEQRES 39 A 602 PHE PRO ASP LYS PRO ILE ILE ILE THR GLU TYR GLY ALA
SEQRES 40 A 602 ASP THR LEU PRO GLY LEU HIS SER THR TRP ASN ILE PRO
SEQRES 41 A 602 TYR THR GLU GLU PHE GLN CYS ASP PHE TYR GLU MET SER
SEQRES 42 A 602 HIS ARG VAL PHE ASP GLY ILE PRO ASN LEU VAL GLY GLU
SEQRES 43 A 602 GLN VAL TRP ASN PHE ALA ASP PHE GLU THR ASN LEU MET
SEQRES 44 A 602 ILE LEU ARG VAL GLN GLY ASN HIS LYS GLY LEU PHE SER
SEQRES 45 A 602 ARG ASN ARG GLN PRO LYS GLN VAL VAL LYS GLU PHE LYS
SEQRES 46 A 602 LYS ARG TRP MET THR ILE PRO HIS TYR HIS ASN LYS LYS
SEQRES 47 A 602 ASN SER VAL LYS
HET MG A 601 1
HETNAM MG MAGNESIUM ION
FORMUL 2 MG MG 2+
FORMUL 3 HOH *295(H2 O)
HELIX 1 1 ASN A 45 MET A 48 5 4
HELIX 2 2 SER A 50 ASP A 55 1 6
HELIX 3 3 PRO A 112 TYR A 116 5 5
HELIX 4 4 ASN A 306 MET A 320 1 15
HELIX 5 5 SER A 333 GLY A 344 1 12
HELIX 6 6 THR A 379 LYS A 395 1 17
HELIX 7 7 GLY A 415 ASP A 431 1 17
HELIX 8 8 VAL A 452 VAL A 456 5 5
HELIX 9 9 ASP A 473 PHE A 492 1 20
HELIX 10 10 THR A 519 ASP A 535 1 17
HELIX 11 11 GLN A 576 MET A 586 1 11
SHEET 1 A 4 ASN A 11 ASP A 14 0
SHEET 2 A 4 LEU A 171 PRO A 177 -1 O LEU A 173 N TYR A 13
SHEET 3 A 4 GLU A 75 PHE A 81 -1 N VAL A 78 O MET A 174
SHEET 4 A 4 PHE A 107 LEU A 110 -1 O VAL A 109 N LEU A 79
SHEET 1 B 6 VAL A 37 ILE A 40 0
SHEET 2 B 6 GLY A 17 LEU A 23 -1 N TRP A 19 O MET A 38
SHEET 3 B 6 ASP A 59 GLU A 67 -1 O TRP A 61 N LYS A 22
SHEET 4 B 6 LYS A 120 ASN A 128 -1 O ILE A 121 N ILE A 66
SHEET 5 B 6 GLN A 87 VAL A 92 -1 N TYR A 91 O SER A 124
SHEET 6 B 6 VAL A 95 LYS A 101 -1 O VAL A 97 N ILE A 90
SHEET 1 C 2 THR A 42 SER A 43 0
SHEET 2 C 2 GLY A 166 VAL A 167 -1 O VAL A 167 N THR A 42
SHEET 1 D 2 GLY A 139 ILE A 145 0
SHEET 2 D 2 ILE A 151 GLU A 157 -1 O LYS A 152 N ILE A 144
SHEET 1 E 3 ILE A 181 LEU A 190 0
SHEET 2 E 3 ALA A 197 THR A 205 -1 O GLU A 204 N ASP A 183
SHEET 3 E 3 ARG A 231 LEU A 234 -1 O LEU A 232 N LEU A 199
SHEET 1 F 4 LEU A 223 THR A 227 0
SHEET 2 F 4 GLU A 211 PHE A 217 -1 N ILE A 214 O THR A 227
SHEET 3 F 4 TYR A 248 PHE A 255 -1 O ARG A 251 N SER A 215
SHEET 4 F 4 LEU A 260 PHE A 268 -1 O GLU A 266 N ALA A 250
SHEET 1 G 3 ILE A 273 THR A 276 0
SHEET 2 G 3 GLN A 279 LEU A 282 -1 O LEU A 281 N GLU A 274
SHEET 3 G 3 LYS A 285 PRO A 286 -1 O LYS A 285 N LEU A 282
SHEET 1 H 9 PHE A 289 GLY A 293 0
SHEET 2 H 9 SER A 324 ARG A 326 1 N SER A 324 O LYS A 290
SHEET 3 H 9 LEU A 346 GLU A 350 1 O ILE A 348 N PHE A 325
SHEET 4 H 9 VAL A 400 ASN A 407 1 O MET A 402 N ASP A 349
SHEET 5 H 9 VAL A 437 ASN A 441 1 O THR A 438 N TRP A 403
SHEET 6 H 9 VAL A 458 ASN A 462 1 O ASN A 462 N ASN A 441
SHEET 7 H 9 ILE A 497 GLU A 501 1 O ILE A 498 N VAL A 459
SHEET 8 H 9 LEU A 540 VAL A 545 1 O GLN A 544 N ILE A 499
SHEET 9 H 9 PHE A 289 GLY A 293 1 N GLY A 293 O VAL A 545
CISPEP 1 ILE A 40 PRO A 41 0 -3.57
CISPEP 2 THR A 85 HIS A 86 0 2.62
CISPEP 3 LEU A 136 PRO A 137 0 3.11
CISPEP 4 ASP A 148 GLY A 149 0 -3.06
CISPEP 5 SER A 328 HIS A 329 0 -6.90
CISPEP 6 ASP A 370 ASN A 371 0 9.27
CISPEP 7 TRP A 546 ASN A 547 0 5.00
CISPEP 8 LYS A 595 ASN A 596 0 8.82
SITE 1 AC1 2 GLY A 372 TRP A 374
CRYST1 68.814 83.829 199.332 90.00 90.00 90.00 I 2 2 2 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 0.014532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005017 0.00000
(ATOM LINES ARE NOT SHOWN.)
END