HEADER HYDROLASE 30-DEC-18 6J23
TITLE CRYSTAL STRUCTURE OF ARABIDOPSIS ADAL COMPLEXED WITH GMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE/AMP DEAMINASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ADAL, PUTATIVE ADENOSINE DEAMINASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT4G04880, T4B21.20, T4B21_20;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS M6A, N6-MAMP, ARABIDOPSIS, ZN, GMP, COMPLEX, DEAMINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.X.WU,D.ZHANG,H.B.NIE,S.L.SHEN,S.S.LI,D.J.PATEL
REVDAT 4 22-NOV-23 6J23 1 REMARK
REVDAT 3 11-SEP-19 6J23 1 JRNL
REVDAT 2 31-JUL-19 6J23 1 JRNL
REVDAT 1 27-FEB-19 6J23 0
JRNL AUTH B.WU,D.ZHANG,H.NIE,S.SHEN,Y.LI,S.LI
JRNL TITL STRUCTURE OFARABIDOPSIS THALIANA N6-METHYL-AMP DEAMINASE
JRNL TITL 2 ADAL WITH BOUND GMP AND IMP AND IMPLICATIONS
JRNL TITL 3 FORN6-METHYL-AMP RECOGNITION AND PROCESSING.
JRNL REF RNA BIOL. V. 16 1504 2019
JRNL REFN ESSN 1555-8584
JRNL PMID 31318636
JRNL DOI 10.1080/15476286.2019.1642712
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14RC2_3191
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.440
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 28180
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1422
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 27.3552 - 4.0822 0.99 3004 163 0.1460 0.1660
REMARK 3 2 4.0822 - 3.2418 1.00 2872 156 0.1523 0.2016
REMARK 3 3 3.2418 - 2.8325 1.00 2865 148 0.1683 0.2051
REMARK 3 4 2.8325 - 2.5738 0.99 2813 161 0.1777 0.2055
REMARK 3 5 2.5738 - 2.3894 1.00 2840 152 0.1676 0.2252
REMARK 3 6 2.3894 - 2.2486 1.00 2802 143 0.1759 0.2442
REMARK 3 7 2.2486 - 2.1360 0.97 2741 144 0.1920 0.2716
REMARK 3 8 2.1360 - 2.0431 0.94 2649 144 0.2109 0.2653
REMARK 3 9 2.0431 - 1.9645 0.83 2315 130 0.2144 0.2409
REMARK 3 10 1.9645 - 1.8967 0.66 1857 81 0.2334 0.3058
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.720
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 : 0.007 2782
REMARK 3 ANGLE : 0.850 3769
REMARK 3 CHIRALITY : 0.051 441
REMARK 3 PLANARITY : 0.005 474
REMARK 3 DIHEDRAL : 11.393 2336
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 6J23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010338.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-18
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 : BL19U1
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29882
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 59.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.13800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.13800
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: 6IV5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 800, 0.1 M MES PH 6.0, 0.2 M
REMARK 280 CALCIUM ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 25.69050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.48700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.26000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.48700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.69050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.26000
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 80 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 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 THR A 132
REMARK 465 ALA A 133
REMARK 465 SER A 134
REMARK 465 ASP A 135
REMARK 465 SER A 136
REMARK 465 GLN A 137
REMARK 465 LYS A 138
REMARK 465 LEU A 139
REMARK 465 HIS A 140
REMARK 465 ASN A 141
REMARK 465 ALA A 142
REMARK 465 GLY A 143
REMARK 465 ASP A 144
REMARK 465 GLY A 145
REMARK 465 ILE A 146
REMARK 465 GLY A 147
REMARK 465 VAL A 355
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 OE2 GLU A 336 O HOH A 501 1.80
REMARK 500 OD1 ASP A 276 O HOH A 502 2.05
REMARK 500 O HOH A 551 O HOH A 660 2.07
REMARK 500 OE2 GLU A 170 O HOH A 503 2.12
REMARK 500 NZ LYS A 66 O HOH A 504 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 SER A 124 -35.68 -131.07
REMARK 500 ASN A 223 76.62 -166.27
REMARK 500 HIS A 240 -82.35 86.49
REMARK 500 ASN A 295 -72.15 68.48
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 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 13 NE2
REMARK 620 2 HIS A 15 NE2 103.2
REMARK 620 3 HIS A 217 NE2 93.3 100.2
REMARK 620 4 ASN A 295 OD1 87.7 91.2 168.1
REMARK 620 5 HOH A 507 O 121.8 134.2 86.2 83.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5GP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
DBREF 6J23 A 1 355 UNP Q8LPL7 Q8LPL7_ARATH 1 355
SEQADV 6J23 ASN A 295 UNP Q8LPL7 ASP 295 ENGINEERED MUTATION
SEQRES 1 A 355 MET GLU TRP ILE GLN SER LEU PRO LYS ILE GLU LEU HIS
SEQRES 2 A 355 ALA HIS LEU ASN GLY SER ILE ARG ASP SER THR LEU LEU
SEQRES 3 A 355 GLU LEU ALA ARG VAL LEU GLY GLU LYS GLY VAL ILE VAL
SEQRES 4 A 355 PHE ALA ASP VAL GLU HIS VAL ILE GLN LYS ASN ASP ARG
SEQRES 5 A 355 SER LEU VAL GLU VAL PHE LYS LEU PHE ASP LEU ILE HIS
SEQRES 6 A 355 LYS LEU THR THR ASP HIS LYS THR VAL THR ARG ILE THR
SEQRES 7 A 355 ARG GLU VAL VAL GLU ASP PHE ALA LEU GLU ASN VAL VAL
SEQRES 8 A 355 TYR LEU GLU LEU ARG THR THR PRO LYS ARG SER ASP SER
SEQRES 9 A 355 ILE GLY MET SER LYS ARG SER TYR MET GLU ALA VAL ILE
SEQRES 10 A 355 GLN GLY LEU ARG SER VAL SER GLU VAL ASP ILE ASP PHE
SEQRES 11 A 355 VAL THR ALA SER ASP SER GLN LYS LEU HIS ASN ALA GLY
SEQRES 12 A 355 ASP GLY ILE GLY ARG LYS LYS ILE TYR VAL ARG LEU LEU
SEQRES 13 A 355 LEU SER ILE ASP ARG ARG GLU THR THR GLU SER ALA MET
SEQRES 14 A 355 GLU THR VAL LYS LEU ALA LEU GLU MET ARG ASP VAL GLY
SEQRES 15 A 355 VAL VAL GLY ILE ASP LEU SER GLY ASN PRO LEU VAL GLY
SEQRES 16 A 355 GLU TRP SER THR PHE LEU PRO ALA LEU GLN TYR ALA LYS
SEQRES 17 A 355 ASP ASN ASP LEU HIS ILE THR LEU HIS CYS GLY GLU VAL
SEQRES 18 A 355 PRO ASN PRO LYS GLU ILE GLN ALA MET LEU ASP PHE LYS
SEQRES 19 A 355 PRO HIS ARG ILE GLY HIS ALA CYS PHE PHE LYS ASP GLU
SEQRES 20 A 355 ASP TRP THR LYS LEU LYS SER PHE ARG ILE PRO VAL GLU
SEQRES 21 A 355 ILE CYS LEU THR SER ASN ILE VAL THR LYS SER ILE SER
SEQRES 22 A 355 SER ILE ASP ILE HIS HIS PHE ALA ASP LEU TYR ASN ALA
SEQRES 23 A 355 LYS HIS PRO LEU ILE LEU CYS THR ASN ASP PHE GLY VAL
SEQRES 24 A 355 PHE SER THR SER LEU SER ASN GLU TYR ALA LEU ALA VAL
SEQRES 25 A 355 ARG SER LEU GLY LEU SER LYS SER GLU THR PHE ALA LEU
SEQRES 26 A 355 ALA ARG ALA ALA ILE ASP ALA THR PHE ALA GLU ASP GLU
SEQRES 27 A 355 VAL LYS GLN GLN LEU ARG PHE ILE PHE ASP SER ALA SER
SEQRES 28 A 355 PRO GLU HIS VAL
HET 5GP A 401 24
HET ZN A 402 1
HETNAM 5GP GUANOSINE-5'-MONOPHOSPHATE
HETNAM ZN ZINC ION
FORMUL 2 5GP C10 H14 N5 O8 P
FORMUL 3 ZN ZN 2+
FORMUL 4 HOH *183(H2 O)
HELIX 1 AA1 MET A 1 LEU A 7 1 7
HELIX 2 AA2 ASN A 17 SER A 19 5 3
HELIX 3 AA3 ARG A 21 LYS A 35 1 15
HELIX 4 AA4 VAL A 39 ASN A 50 1 12
HELIX 5 AA5 SER A 53 THR A 69 1 17
HELIX 6 AA6 ASP A 70 GLU A 88 1 19
HELIX 7 AA7 SER A 102 GLY A 106 5 5
HELIX 8 AA8 SER A 108 SER A 122 1 15
HELIX 9 AA9 THR A 164 MET A 178 1 15
HELIX 10 AB1 ARG A 179 VAL A 181 5 3
HELIX 11 AB2 GLU A 196 ASN A 210 1 15
HELIX 12 AB3 ASN A 223 LYS A 234 1 12
HELIX 13 AB4 LYS A 245 ARG A 256 1 12
HELIX 14 AB5 CYS A 262 THR A 269 1 8
HELIX 15 AB6 SER A 274 HIS A 278 5 5
HELIX 16 AB7 HIS A 279 ALA A 286 1 8
HELIX 17 AB8 SER A 303 GLY A 316 1 14
HELIX 18 AB9 SER A 318 ALA A 329 1 12
HELIX 19 AC1 ILE A 330 THR A 333 5 4
HELIX 20 AC2 GLU A 336 ALA A 350 1 15
SHEET 1 AA1 4 LYS A 9 HIS A 15 0
SHEET 2 AA1 4 VAL A 90 THR A 97 1 O GLU A 94 N GLU A 11
SHEET 3 AA1 4 LYS A 150 ASP A 160 1 O TYR A 152 N VAL A 91
SHEET 4 AA1 4 ASP A 127 ASP A 129 1 N ASP A 129 O VAL A 153
SHEET 1 AA2 8 LYS A 9 HIS A 15 0
SHEET 2 AA2 8 VAL A 90 THR A 97 1 O GLU A 94 N GLU A 11
SHEET 3 AA2 8 LYS A 150 ASP A 160 1 O TYR A 152 N VAL A 91
SHEET 4 AA2 8 VAL A 183 SER A 189 1 O ASP A 187 N ILE A 159
SHEET 5 AA2 8 HIS A 213 CYS A 218 1 O THR A 215 N ILE A 186
SHEET 6 AA2 8 ARG A 237 HIS A 240 1 O GLY A 239 N CYS A 218
SHEET 7 AA2 8 VAL A 259 ILE A 261 1 O GLU A 260 N ILE A 238
SHEET 8 AA2 8 LEU A 290 LEU A 292 1 O ILE A 291 N ILE A 261
LINK NE2 HIS A 13 ZN ZN A 402 1555 1555 2.07
LINK NE2 HIS A 15 ZN ZN A 402 1555 1555 2.14
LINK NE2 HIS A 217 ZN ZN A 402 1555 1555 2.14
LINK OD1 ASN A 295 ZN ZN A 402 1555 1555 2.16
LINK ZN ZN A 402 O HOH A 507 1555 1555 2.01
SITE 1 AC1 22 HIS A 15 LEU A 16 ASN A 17 PHE A 58
SITE 2 AC1 22 PHE A 61 HIS A 65 THR A 97 THR A 98
SITE 3 AC1 22 LYS A 100 ASP A 160 GLY A 190 HIS A 217
SITE 4 AC1 22 GLU A 220 ASN A 295 ASP A 296 HOH A 507
SITE 5 AC1 22 HOH A 520 HOH A 528 HOH A 544 HOH A 586
SITE 6 AC1 22 HOH A 614 HOH A 637
SITE 1 AC2 5 HIS A 13 HIS A 15 HIS A 217 ASN A 295
SITE 2 AC2 5 HOH A 507
CRYST1 51.381 82.520 86.974 90.00 90.00 90.00 P 21 21 21 4
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 0.019462 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012118 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011498 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
