HEADER HYDROLASE 20-APR-18 5ZQY
TITLE CRYSTAL STRUCTURE OF A POLY(ADP-RIBOSE) GLYCOHYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ADP-RIBOSE) GLYCOHYDROLASE ARH3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ADP-RIBOSYLHYDROLASE 3,[PROTEIN ADP-RIBOSYLARGININE]
COMPND 5 HYDROLASE-LIKE PROTEIN 2;
COMPND 6 EC: 3.2.1.143;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADPRHL2, ARH3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLY(ADP-RIBOSE) GLYCOHYDROLASE, LYASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WANG,Z.YUAN,Y.MA,J.WANG,X.LIU
REVDAT 3 22-NOV-23 5ZQY 1 HETSYN LINK
REVDAT 2 26-SEP-18 5ZQY 1 JRNL
REVDAT 1 15-AUG-18 5ZQY 0
JRNL AUTH M.WANG,Z.YUAN,R.XIE,Y.MA,X.LIU,X.YU
JRNL TITL STRUCTURE-FUNCTION ANALYSES REVEAL THE MECHANISM OF THE
JRNL TITL 2 ARH3-DEPENDENT HYDROLYSIS OF ADP-RIBOSYLATION.
JRNL REF J. BIOL. CHEM. V. 293 14470 2018
JRNL REFN ESSN 1083-351X
JRNL PMID 30045870
JRNL DOI 10.1074/JBC.RA118.004284
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3092)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 40881
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1986
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 37.3601 - 3.7995 0.95 2864 146 0.1564 0.1651
REMARK 3 2 3.7995 - 3.0162 0.97 2859 146 0.1512 0.1597
REMARK 3 3 3.0162 - 2.6351 0.97 2864 147 0.1586 0.1908
REMARK 3 4 2.6351 - 2.3942 0.97 2839 144 0.1685 0.1773
REMARK 3 5 2.3942 - 2.2226 0.97 2848 146 0.1563 0.1601
REMARK 3 6 2.2226 - 2.0916 0.96 2789 143 0.1501 0.1705
REMARK 3 7 2.0916 - 1.9868 0.97 2846 144 0.1547 0.1955
REMARK 3 8 1.9868 - 1.9003 0.96 2808 142 0.1585 0.2096
REMARK 3 9 1.9003 - 1.8272 0.97 2825 143 0.1578 0.1975
REMARK 3 10 1.8272 - 1.7641 0.96 2805 145 0.1570 0.1931
REMARK 3 11 1.7641 - 1.7090 0.96 2809 142 0.1570 0.1882
REMARK 3 12 1.7090 - 1.6601 0.96 2807 141 0.1610 0.2051
REMARK 3 13 1.6601 - 1.6164 0.94 2741 142 0.1609 0.2127
REMARK 3 14 1.6164 - 1.5770 0.76 2191 115 0.1771 0.2260
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.006 2776
REMARK 3 ANGLE : 0.918 3770
REMARK 3 CHIRALITY : 0.050 415
REMARK 3 PLANARITY : 0.005 497
REMARK 3 DIHEDRAL : 5.280 2856
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 5ZQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1300007506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40881
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.577
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20700
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: PHENIX
REMARK 200 STARTING MODEL: 2FOZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.0, PEG MME 2000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 38.37000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 15
REMARK 465 PRO A 16
REMARK 465 GLY A 17
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 O2D AR6 A 403 O HOH A 501 2.15
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 76 -161.68 -125.46
REMARK 500 ALA A 94 164.38 174.19
REMARK 500 ASP A 113 42.63 -91.85
REMARK 500 ASN A 269 40.46 -144.88
REMARK 500 SER A 276 -35.45 -138.31
REMARK 500 LYS A 362 -45.38 82.58
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 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 76 OG1
REMARK 620 2 ASP A 77 OD1 88.0
REMARK 620 3 ASP A 78 OD1 77.5 84.2
REMARK 620 4 ASP A 316 OD2 98.6 162.1 81.0
REMARK 620 5 HOH A 501 O 141.4 96.5 64.9 68.0
REMARK 620 6 HOH A 648 O 106.4 79.7 163.3 113.8 112.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 314 OD1
REMARK 620 2 ASP A 316 OD1 66.9
REMARK 620 3 THR A 317 OG1 97.2 81.1
REMARK 620 4 AR6 A 403 O1D 96.8 138.8 139.8
REMARK 620 5 AR6 A 403 O3D 115.2 151.3 70.1 69.8
REMARK 620 6 AR6 A 403 O2D 151.9 133.9 104.2 55.1 57.7
REMARK 620 7 HOH A 501 O 158.0 91.3 75.6 102.0 82.3 48.5
REMARK 620 8 HOH A 624 O 93.3 76.0 148.6 67.2 130.5 77.8 83.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AR6 A 403
DBREF 5ZQY A 19 363 UNP Q9NX46 ARHL2_HUMAN 19 363
SEQADV 5ZQY GLY A 15 UNP Q9NX46 EXPRESSION TAG
SEQADV 5ZQY PRO A 16 UNP Q9NX46 EXPRESSION TAG
SEQADV 5ZQY GLY A 17 UNP Q9NX46 EXPRESSION TAG
SEQADV 5ZQY SER A 18 UNP Q9NX46 EXPRESSION TAG
SEQRES 1 A 349 GLY PRO GLY SER SER LEU SER ARG PHE ARG GLY CYS LEU
SEQRES 2 A 349 ALA GLY ALA LEU LEU GLY ASP CYS VAL GLY SER PHE TYR
SEQRES 3 A 349 GLU ALA HIS ASP THR VAL ASP LEU THR SER VAL LEU ARG
SEQRES 4 A 349 HIS VAL GLN SER LEU GLU PRO ASP PRO GLY THR PRO GLY
SEQRES 5 A 349 SER GLU ARG THR GLU ALA LEU TYR TYR THR ASP ASP THR
SEQRES 6 A 349 ALA MET ALA ARG ALA LEU VAL GLN SER LEU LEU ALA LYS
SEQRES 7 A 349 GLU ALA PHE ASP GLU VAL ASP MET ALA HIS ARG PHE ALA
SEQRES 8 A 349 GLN GLU TYR LYS LYS ASP PRO ASP ARG GLY TYR GLY ALA
SEQRES 9 A 349 GLY VAL VAL THR VAL PHE LYS LYS LEU LEU ASN PRO LYS
SEQRES 10 A 349 CYS ARG ASP VAL PHE GLU PRO ALA ARG ALA GLN PHE ASN
SEQRES 11 A 349 GLY LYS GLY SER TYR GLY ASN GLY GLY ALA MET ARG VAL
SEQRES 12 A 349 ALA GLY ILE SER LEU ALA TYR SER SER VAL GLN ASP VAL
SEQRES 13 A 349 GLN LYS PHE ALA ARG LEU SER ALA GLN LEU THR HIS ALA
SEQRES 14 A 349 SER SER LEU GLY TYR ASN GLY ALA ILE LEU GLN ALA LEU
SEQRES 15 A 349 ALA VAL HIS LEU ALA LEU GLN GLY GLU SER SER SER GLU
SEQRES 16 A 349 HIS PHE LEU LYS GLN LEU LEU GLY HIS MET GLU ASP LEU
SEQRES 17 A 349 GLU GLY ASP ALA GLN SER VAL LEU ASP ALA ARG GLU LEU
SEQRES 18 A 349 GLY MET GLU GLU ARG PRO TYR SER SER ARG LEU LYS LYS
SEQRES 19 A 349 ILE GLY GLU LEU LEU ASP GLN ALA SER VAL THR ARG GLU
SEQRES 20 A 349 GLU VAL VAL SER GLU LEU GLY ASN GLY ILE ALA ALA PHE
SEQRES 21 A 349 GLU SER VAL PRO THR ALA ILE TYR CYS PHE LEU ARG CYS
SEQRES 22 A 349 MET GLU PRO ASP PRO GLU ILE PRO SER ALA PHE ASN SER
SEQRES 23 A 349 LEU GLN ARG THR LEU ILE TYR SER ILE SER LEU GLY GLY
SEQRES 24 A 349 ASP THR ASP THR ILE ALA THR MET ALA GLY ALA ILE ALA
SEQRES 25 A 349 GLY ALA TYR TYR GLY MET ASP GLN VAL PRO GLU SER TRP
SEQRES 26 A 349 GLN GLN SER CYS GLU GLY TYR GLU GLU THR ASP ILE LEU
SEQRES 27 A 349 ALA GLN SER LEU HIS ARG VAL PHE GLN LYS SER
HET MG A 401 1
HET MG A 402 1
HET AR6 A 403 36
HETNAM MG MAGNESIUM ION
HETNAM AR6 [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-
HETNAM 2 AR6 OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-
HETNAM 3 AR6 TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN
HETNAM 4 AR6 PHOSPHATE
HETSYN AR6 ADENOSINE-5-DIPHOSPHORIBOSE
FORMUL 2 MG 2(MG 2+)
FORMUL 4 AR6 C15 H23 N5 O14 P2
FORMUL 5 HOH *262(H2 O)
HELIX 1 AA1 SER A 18 SER A 38 1 21
HELIX 2 AA2 PHE A 39 GLU A 41 5 3
HELIX 3 AA3 ASP A 47 SER A 57 1 11
HELIX 4 AA4 THR A 76 GLU A 93 1 18
HELIX 5 AA5 ASP A 96 ASP A 111 1 16
HELIX 6 AA6 GLY A 119 LEU A 128 1 10
HELIX 7 AA7 PHE A 136 GLN A 142 1 7
HELIX 8 AA8 ASN A 151 ARG A 156 1 6
HELIX 9 AA9 VAL A 157 TYR A 164 1 8
HELIX 10 AB1 SER A 166 LEU A 180 1 15
HELIX 11 AB2 SER A 184 GLN A 203 1 20
HELIX 12 AB3 SER A 207 GLY A 224 1 18
HELIX 13 AB4 ASP A 225 GLY A 236 1 12
HELIX 14 AB5 ARG A 240 GLN A 255 1 16
HELIX 15 AB6 THR A 259 GLY A 268 1 10
HELIX 16 AB7 ALA A 272 GLU A 275 5 4
HELIX 17 AB8 SER A 276 CYS A 287 1 12
HELIX 18 AB9 ASN A 299 LEU A 311 1 13
HELIX 19 AC1 ASP A 314 GLY A 331 1 18
HELIX 20 AC2 MET A 332 VAL A 335 5 4
HELIX 21 AC3 PRO A 336 GLN A 341 1 6
HELIX 22 AC4 GLY A 345 GLN A 361 1 17
LINK OG1 THR A 76 MG MG A 402 1555 1555 2.46
LINK OD1 ASP A 77 MG MG A 402 1555 1555 2.22
LINK OD1 ASP A 78 MG MG A 402 1555 1555 2.40
LINK OD1 ASP A 314 MG MG A 401 1555 1555 2.39
LINK OD1 ASP A 316 MG MG A 401 1555 1555 2.43
LINK OD2 ASP A 316 MG MG A 402 1555 1555 2.04
LINK OG1 THR A 317 MG MG A 401 1555 1555 2.57
LINK MG MG A 401 O1D AR6 A 403 1555 1555 2.56
LINK MG MG A 401 O3D AR6 A 403 1555 1555 2.35
LINK MG MG A 401 O2D AR6 A 403 1555 1555 2.87
LINK MG MG A 401 O HOH A 501 1555 1555 2.04
LINK MG MG A 401 O HOH A 624 1555 1555 2.51
LINK MG MG A 402 O HOH A 501 1555 1555 2.07
LINK MG MG A 402 O HOH A 648 1555 1555 2.22
SITE 1 AC1 6 ASP A 314 ASP A 316 THR A 317 AR6 A 403
SITE 2 AC1 6 HOH A 501 HOH A 624
SITE 1 AC2 7 THR A 76 ASP A 77 ASP A 78 ASP A 316
SITE 2 AC2 7 AR6 A 403 HOH A 501 HOH A 648
SITE 1 AC3 30 ASP A 77 GLY A 115 GLY A 117 ALA A 118
SITE 2 AC3 30 GLY A 119 VAL A 120 PHE A 143 GLY A 147
SITE 3 AC3 30 SER A 148 TYR A 149 GLY A 150 ASN A 151
SITE 4 AC3 30 GLY A 152 HIS A 182 ILE A 271 ASP A 314
SITE 5 AC3 30 THR A 317 MG A 401 MG A 402 HOH A 501
SITE 6 AC3 30 HOH A 506 HOH A 553 HOH A 555 HOH A 598
SITE 7 AC3 30 HOH A 606 HOH A 610 HOH A 611 HOH A 624
SITE 8 AC3 30 HOH A 656 HOH A 718
CRYST1 43.880 76.740 48.530 90.00 103.00 90.00 P 1 21 1 2
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 0.022789 0.000000 0.005261 0.00000
SCALE2 0.000000 0.013031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021148 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
