HEADER HYDROLASE 17-AUG-12 4GN7
TITLE MOUSE SMP30/GNL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGUCALCIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SMP30, GNL, RC, GLUCONOLACTONASE, SENESCENCE MARKER PROTEIN
COMPND 5 30;
COMPND 6 EC: 3.1.1.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: SMP30;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21B(+)
KEYWDS BETA PROPELLER STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.AIZAWA,M.SENDA,A.HARADA,N.MARUYAMA,T.ISHIDA,T.AIGAKI,A.ISHIGAMI,
AUTHOR 2 T.SENDA
REVDAT 2 08-NOV-23 4GN7 1 REMARK LINK
REVDAT 1 10-APR-13 4GN7 0
JRNL AUTH S.AIZAWA,M.SENDA,A.HARADA,N.MARUYAMA,T.ISHIDA,T.AIGAKI,
JRNL AUTH 2 A.ISHIGAMI,T.SENDA
JRNL TITL STRUCTURAL BASIS OF THE GAMMA-LACTONE-RING FORMATION IN
JRNL TITL 2 ASCORBIC ACID BIOSYNTHESIS BY THE SENESCENCE MARKER
JRNL TITL 3 PROTEIN-30/GLUCONOLACTONASE
JRNL REF PLOS ONE V. 8 53706 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 23349732
JRNL DOI 10.1371/JOURNAL.PONE.0053706
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 66221
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3311
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 51.3568 - 5.6226 0.99 2790 147 0.1879 0.1820
REMARK 3 2 5.6226 - 4.4636 1.00 2703 142 0.1428 0.1656
REMARK 3 3 4.4636 - 3.8996 1.00 2669 140 0.1431 0.1661
REMARK 3 4 3.8996 - 3.5432 1.00 2654 140 0.1579 0.1910
REMARK 3 5 3.5432 - 3.2893 1.00 2620 138 0.1796 0.1978
REMARK 3 6 3.2893 - 3.0953 1.00 2640 139 0.1968 0.2249
REMARK 3 7 3.0953 - 2.9403 1.00 2627 138 0.2216 0.2818
REMARK 3 8 2.9403 - 2.8124 1.00 2621 138 0.2252 0.2484
REMARK 3 9 2.8124 - 2.7041 1.00 2636 139 0.2169 0.2626
REMARK 3 10 2.7041 - 2.6108 1.00 2600 137 0.2129 0.2596
REMARK 3 11 2.6108 - 2.5292 1.00 2610 137 0.2011 0.2483
REMARK 3 12 2.5292 - 2.4569 1.00 2609 137 0.2009 0.2479
REMARK 3 13 2.4569 - 2.3922 1.00 2586 136 0.1973 0.2575
REMARK 3 14 2.3922 - 2.3338 1.00 2579 136 0.1941 0.2254
REMARK 3 15 2.3338 - 2.2808 1.00 2610 138 0.2014 0.2218
REMARK 3 16 2.2808 - 2.2322 1.00 2621 138 0.1936 0.2310
REMARK 3 17 2.2322 - 2.1876 1.00 2589 136 0.1947 0.2543
REMARK 3 18 2.1876 - 2.1463 1.00 2581 136 0.2020 0.2480
REMARK 3 19 2.1463 - 2.1080 1.00 2611 137 0.2075 0.2421
REMARK 3 20 2.1080 - 2.0722 1.00 2574 136 0.2028 0.2498
REMARK 3 21 2.0722 - 2.0388 1.00 2613 137 0.1986 0.2502
REMARK 3 22 2.0388 - 2.0074 1.00 2564 135 0.2150 0.2482
REMARK 3 23 2.0074 - 1.9779 1.00 2567 135 0.2144 0.2604
REMARK 3 24 1.9779 - 1.9501 1.00 2636 139 0.2242 0.2709
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4791
REMARK 3 ANGLE : 1.169 6513
REMARK 3 CHIRALITY : 0.087 705
REMARK 3 PLANARITY : 0.005 840
REMARK 3 DIHEDRAL : 13.526 1719
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GN7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074394.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98000
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66230
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 76.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4GN9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 100MM TRIS-HCL,
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.27233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 98.54467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 98.54467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.27233
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 2
REMARK 465 MET B 1
REMARK 465 SER B 2
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 GLU A 24 CG CD OE1 OE2
REMARK 470 GLN A 48 CG CD OE1 NE2
REMARK 470 LYS A 98 CG CD CE NZ
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 GLU B 24 CG CD OE1 OE2
REMARK 470 VAL B 45 CG1 CG2
REMARK 470 GLN B 48 CG CD OE1 NE2
REMARK 470 GLN B 65 CD OE1 NE2
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 470 GLU B 120 CG CD OE1 OE2
REMARK 470 GLU B 128 CG CD OE1 OE2
REMARK 470 LYS B 253 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 VAL A 107 N CA C O CB CG1 CG2
REMARK 480 VAL B 107 N CA C O CB CG1 CG2
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 ARG A 11 77.13 -106.75
REMARK 500 CYS A 16 86.43 -152.90
REMARK 500 ASN A 103 -119.22 -121.08
REMARK 500 HIS A 141 7.22 81.23
REMARK 500 TYR A 146 -61.19 -91.92
REMARK 500 ASP A 148 -160.06 -110.21
REMARK 500 ASN A 154 -137.56 -136.08
REMARK 500 GLN A 201 -134.10 53.22
REMARK 500 ASP A 204 -112.98 -122.45
REMARK 500 ASN A 220 -10.52 81.40
REMARK 500 ARG B 11 65.27 -104.82
REMARK 500 CYS B 16 84.23 -154.00
REMARK 500 ASN B 103 -115.20 -120.85
REMARK 500 ALA B 125 18.66 55.27
REMARK 500 ASP B 148 -166.34 -109.23
REMARK 500 ASN B 154 -134.65 -129.15
REMARK 500 GLN B 201 -129.63 56.55
REMARK 500 ASP B 204 -113.41 -129.04
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 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 18 OE2
REMARK 620 2 ASN A 154 OD1 167.9
REMARK 620 3 ASP A 204 OD2 99.1 74.4
REMARK 620 4 HOH A 576 O 88.6 81.0 87.5
REMARK 620 5 HOH A 577 O 88.0 101.7 87.4 173.3
REMARK 620 6 HOH A 578 O 86.8 99.6 174.0 91.7 93.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 18 OE2
REMARK 620 2 GLU B 18 OE1 43.9
REMARK 620 3 ASN B 154 OD1 177.1 137.3
REMARK 620 4 ASP B 204 OD2 101.2 117.0 75.9
REMARK 620 5 HOH B 528 O 95.3 57.1 84.6 88.4
REMARK 620 6 HOH B 553 O 80.7 120.3 99.3 89.4 174.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GN8 RELATED DB: PDB
REMARK 900 RELATED ID: 4GN9 RELATED DB: PDB
REMARK 900 RELATED ID: 4GNA RELATED DB: PDB
REMARK 900 RELATED ID: 4GNB RELATED DB: PDB
REMARK 900 RELATED ID: 4GNC RELATED DB: PDB
DBREF 4GN7 A 1 299 UNP Q64374 RGN_MOUSE 1 299
DBREF 4GN7 B 1 299 UNP Q64374 RGN_MOUSE 1 299
SEQRES 1 A 299 MET SER SER ILE LYS VAL GLU CYS VAL LEU ARG GLU ASN
SEQRES 2 A 299 TYR ARG CYS GLY GLU SER PRO VAL TRP GLU GLU ALA SER
SEQRES 3 A 299 GLN SER LEU LEU PHE VAL ASP ILE PRO SER LYS ILE ILE
SEQRES 4 A 299 CYS ARG TRP ASP THR VAL SER ASN GLN VAL GLN ARG VAL
SEQRES 5 A 299 ALA VAL ASP ALA PRO VAL SER SER VAL ALA LEU ARG GLN
SEQRES 6 A 299 LEU GLY GLY TYR VAL ALA THR ILE GLY THR LYS PHE CYS
SEQRES 7 A 299 ALA LEU ASN TRP GLU ASN GLN SER VAL PHE VAL LEU ALA
SEQRES 8 A 299 MET VAL ASP GLU ASP LYS LYS ASN ASN ARG PHE ASN ASP
SEQRES 9 A 299 GLY LYS VAL ASP PRO ALA GLY ARG TYR PHE ALA GLY THR
SEQRES 10 A 299 MET ALA GLU GLU THR ALA PRO ALA VAL LEU GLU ARG HIS
SEQRES 11 A 299 GLN GLY SER LEU TYR SER LEU PHE PRO ASP HIS SER VAL
SEQRES 12 A 299 LYS LYS TYR PHE ASP GLN VAL ASP ILE SER ASN GLY LEU
SEQRES 13 A 299 ASP TRP SER LEU ASP HIS LYS ILE PHE TYR TYR ILE ASP
SEQRES 14 A 299 SER LEU SER TYR THR VAL ASP ALA PHE ASP TYR ASP LEU
SEQRES 15 A 299 GLN THR GLY GLN ILE SER ASN ARG ARG ILE VAL TYR LYS
SEQRES 16 A 299 MET GLU LYS ASP GLU GLN ILE PRO ASP GLY MET CYS ILE
SEQRES 17 A 299 ASP ALA GLU GLY LYS LEU TRP VAL ALA CYS TYR ASN GLY
SEQRES 18 A 299 GLY ARG VAL ILE ARG LEU ASP PRO GLU THR GLY LYS ARG
SEQRES 19 A 299 LEU GLN THR VAL LYS LEU PRO VAL ASP LYS THR THR SER
SEQRES 20 A 299 CYS CYS PHE GLY GLY LYS ASP TYR SER GLU MET TYR VAL
SEQRES 21 A 299 THR CYS ALA ARG ASP GLY LEU ASN ALA GLU GLY LEU LEU
SEQRES 22 A 299 ARG GLN PRO ASP ALA GLY ASN ILE PHE LYS ILE THR GLY
SEQRES 23 A 299 LEU GLY VAL LYS GLY ILE ALA PRO TYR SER TYR ALA GLY
SEQRES 1 B 299 MET SER SER ILE LYS VAL GLU CYS VAL LEU ARG GLU ASN
SEQRES 2 B 299 TYR ARG CYS GLY GLU SER PRO VAL TRP GLU GLU ALA SER
SEQRES 3 B 299 GLN SER LEU LEU PHE VAL ASP ILE PRO SER LYS ILE ILE
SEQRES 4 B 299 CYS ARG TRP ASP THR VAL SER ASN GLN VAL GLN ARG VAL
SEQRES 5 B 299 ALA VAL ASP ALA PRO VAL SER SER VAL ALA LEU ARG GLN
SEQRES 6 B 299 LEU GLY GLY TYR VAL ALA THR ILE GLY THR LYS PHE CYS
SEQRES 7 B 299 ALA LEU ASN TRP GLU ASN GLN SER VAL PHE VAL LEU ALA
SEQRES 8 B 299 MET VAL ASP GLU ASP LYS LYS ASN ASN ARG PHE ASN ASP
SEQRES 9 B 299 GLY LYS VAL ASP PRO ALA GLY ARG TYR PHE ALA GLY THR
SEQRES 10 B 299 MET ALA GLU GLU THR ALA PRO ALA VAL LEU GLU ARG HIS
SEQRES 11 B 299 GLN GLY SER LEU TYR SER LEU PHE PRO ASP HIS SER VAL
SEQRES 12 B 299 LYS LYS TYR PHE ASP GLN VAL ASP ILE SER ASN GLY LEU
SEQRES 13 B 299 ASP TRP SER LEU ASP HIS LYS ILE PHE TYR TYR ILE ASP
SEQRES 14 B 299 SER LEU SER TYR THR VAL ASP ALA PHE ASP TYR ASP LEU
SEQRES 15 B 299 GLN THR GLY GLN ILE SER ASN ARG ARG ILE VAL TYR LYS
SEQRES 16 B 299 MET GLU LYS ASP GLU GLN ILE PRO ASP GLY MET CYS ILE
SEQRES 17 B 299 ASP ALA GLU GLY LYS LEU TRP VAL ALA CYS TYR ASN GLY
SEQRES 18 B 299 GLY ARG VAL ILE ARG LEU ASP PRO GLU THR GLY LYS ARG
SEQRES 19 B 299 LEU GLN THR VAL LYS LEU PRO VAL ASP LYS THR THR SER
SEQRES 20 B 299 CYS CYS PHE GLY GLY LYS ASP TYR SER GLU MET TYR VAL
SEQRES 21 B 299 THR CYS ALA ARG ASP GLY LEU ASN ALA GLU GLY LEU LEU
SEQRES 22 B 299 ARG GLN PRO ASP ALA GLY ASN ILE PHE LYS ILE THR GLY
SEQRES 23 B 299 LEU GLY VAL LYS GLY ILE ALA PRO TYR SER TYR ALA GLY
HET CA A 301 1
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HET SO4 A 307 5
HET CA B 301 1
HET SO4 B 302 5
HET SO4 B 303 5
HET SO4 B 304 5
HET SO4 B 305 5
HET SO4 B 306 5
HET SO4 B 307 5
HET SO4 B 308 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 SO4 13(O4 S 2-)
FORMUL 18 HOH *373(H2 O)
HELIX 1 1 GLU A 24 SER A 26 5 3
HELIX 2 2 GLU A 197 GLN A 201 5 5
HELIX 3 3 GLY A 252 SER A 256 5 5
HELIX 4 4 ASN A 268 GLN A 275 1 8
HELIX 5 5 GLU B 197 GLN B 201 5 5
HELIX 6 6 GLY B 252 SER B 256 5 5
HELIX 7 7 ASN B 268 GLN B 275 1 8
SHEET 1 A 4 LYS A 5 LEU A 10 0
SHEET 2 A 4 ILE A 281 THR A 285 -1 O LYS A 283 N GLU A 7
SHEET 3 A 4 GLU A 257 CYS A 262 -1 N MET A 258 O ILE A 284
SHEET 4 A 4 THR A 245 GLY A 251 -1 N GLY A 251 O GLU A 257
SHEET 1 B 4 GLY A 17 GLU A 23 0
SHEET 2 B 4 SER A 28 ASP A 33 -1 O LEU A 30 N VAL A 21
SHEET 3 B 4 ILE A 38 ASP A 43 -1 O CYS A 40 N PHE A 31
SHEET 4 B 4 GLN A 48 ALA A 53 -1 O GLN A 50 N ARG A 41
SHEET 1 C 4 VAL A 58 LEU A 63 0
SHEET 2 C 4 TYR A 69 ILE A 73 -1 O VAL A 70 N ALA A 62
SHEET 3 C 4 LYS A 76 ASN A 81 -1 O LEU A 80 N TYR A 69
SHEET 4 C 4 SER A 86 MET A 92 -1 O LEU A 90 N PHE A 77
SHEET 1 D 4 ASN A 100 VAL A 107 0
SHEET 2 D 4 TYR A 113 ALA A 119 -1 O GLY A 116 N ASN A 103
SHEET 3 D 4 GLY A 132 LEU A 137 -1 O TYR A 135 N ALA A 115
SHEET 4 D 4 VAL A 143 VAL A 150 -1 O VAL A 150 N GLY A 132
SHEET 1 E 4 SER A 153 TRP A 158 0
SHEET 2 E 4 ILE A 164 ASP A 169 -1 O TYR A 166 N ASP A 157
SHEET 3 E 4 THR A 174 TYR A 180 -1 O ASP A 176 N TYR A 167
SHEET 4 E 4 ILE A 187 LYS A 195 -1 O VAL A 193 N VAL A 175
SHEET 1 F 4 ILE A 202 ILE A 208 0
SHEET 2 F 4 LEU A 214 TYR A 219 -1 O TRP A 215 N CYS A 207
SHEET 3 F 4 ARG A 223 LEU A 227 -1 O LEU A 227 N LEU A 214
SHEET 4 F 4 ARG A 234 LYS A 239 -1 O LEU A 235 N ARG A 226
SHEET 1 G 4 LYS B 5 LEU B 10 0
SHEET 2 G 4 ILE B 281 THR B 285 -1 O LYS B 283 N GLU B 7
SHEET 3 G 4 GLU B 257 CYS B 262 -1 N MET B 258 O ILE B 284
SHEET 4 G 4 THR B 245 GLY B 251 -1 N CYS B 249 O TYR B 259
SHEET 1 H 4 GLY B 17 GLU B 23 0
SHEET 2 H 4 SER B 28 ASP B 33 -1 O SER B 28 N GLU B 23
SHEET 3 H 4 ILE B 38 ASP B 43 -1 O TRP B 42 N LEU B 29
SHEET 4 H 4 GLN B 48 ALA B 53 -1 O GLN B 50 N ARG B 41
SHEET 1 I 4 VAL B 58 LEU B 63 0
SHEET 2 I 4 TYR B 69 ILE B 73 -1 O VAL B 70 N ALA B 62
SHEET 3 I 4 LYS B 76 ASN B 81 -1 O LEU B 80 N TYR B 69
SHEET 4 I 4 SER B 86 MET B 92 -1 O LEU B 90 N PHE B 77
SHEET 1 J 4 ASN B 100 VAL B 107 0
SHEET 2 J 4 TYR B 113 ALA B 119 -1 O GLY B 116 N ASN B 103
SHEET 3 J 4 GLY B 132 LEU B 137 -1 O LEU B 137 N TYR B 113
SHEET 4 J 4 VAL B 143 VAL B 150 -1 O VAL B 150 N GLY B 132
SHEET 1 K 4 SER B 153 TRP B 158 0
SHEET 2 K 4 ILE B 164 ASP B 169 -1 O TYR B 166 N ASP B 157
SHEET 3 K 4 THR B 174 TYR B 180 -1 O ASP B 176 N TYR B 167
SHEET 4 K 4 ILE B 187 LYS B 195 -1 O SER B 188 N ASP B 179
SHEET 1 L 4 ILE B 202 ILE B 208 0
SHEET 2 L 4 LEU B 214 TYR B 219 -1 O TRP B 215 N CYS B 207
SHEET 3 L 4 ARG B 223 ASP B 228 -1 O LEU B 227 N LEU B 214
SHEET 4 L 4 LYS B 233 LYS B 239 -1 O LEU B 235 N ARG B 226
LINK OE2 GLU A 18 CA CA A 301 1555 1555 2.22
LINK OD1 ASN A 154 CA CA A 301 1555 1555 2.38
LINK OD2 ASP A 204 CA CA A 301 1555 1555 2.17
LINK CA CA A 301 O HOH A 576 1555 1555 2.11
LINK CA CA A 301 O HOH A 577 1555 1555 2.34
LINK CA CA A 301 O HOH A 578 1555 1555 2.37
LINK OE2 GLU B 18 CA CA B 301 1555 1555 2.28
LINK OE1 GLU B 18 CA CA B 301 1555 1555 3.17
LINK OD1 ASN B 154 CA CA B 301 1555 1555 2.22
LINK OD2 ASP B 204 CA CA B 301 1555 1555 2.25
LINK CA CA B 301 O HOH B 528 1555 1555 2.27
LINK CA CA B 301 O HOH B 553 1555 1555 2.36
SITE 1 AC1 6 GLU A 18 ASN A 154 ASP A 204 HOH A 576
SITE 2 AC1 6 HOH A 577 HOH A 578
SITE 1 AC2 4 ARG A 234 GLN A 236 THR A 237 HOH A 473
SITE 1 AC3 5 SER A 188 ASN A 189 ARG A 190 HOH A 583
SITE 2 AC3 5 HOH B 476
SITE 1 AC4 3 ARG A 64 ARG B 274 HOH B 426
SITE 1 AC5 9 GLY A 68 ASN A 81 TRP A 82 GLU A 83
SITE 2 AC5 9 HOH A 442 HOH A 500 HOH A 505 HOH A 581
SITE 3 AC5 9 HOH A 608
SITE 1 AC6 2 ARG A 11 HOH A 512
SITE 1 AC7 2 LYS A 97 GLN A 149
SITE 1 AC8 5 GLU B 18 ASN B 154 ASP B 204 HOH B 528
SITE 2 AC8 5 HOH B 553
SITE 1 AC9 3 ARG A 15 HOH A 483 ARG B 15
SITE 1 BC1 4 ARG B 234 GLN B 236 THR B 237 HOH B 530
SITE 1 BC2 6 PRO A 139 ASP A 140 HOH A 481 ARG B 223
SITE 2 BC2 6 LYS B 239 HOH B 538
SITE 1 BC3 6 PRO B 124 ASN B 220 LYS B 244 GLY B 266
SITE 2 BC3 6 HOH B 471 HOH B 537
SITE 1 BC4 6 ARG B 112 PHE B 138 PRO B 139 GLN B 183
SITE 2 BC4 6 HOH B 533 HOH B 534
SITE 1 BC5 1 ASN B 268
SITE 1 BC6 3 ARG B 41 HOH B 489 HOH B 554
CRYST1 102.678 102.678 147.817 90.00 90.00 120.00 P 31 2 1 12
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 0.009739 0.005623 0.000000 0.00000
SCALE2 0.000000 0.011246 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006765 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
