HEADER TRANSFERASE 03-APR-17 5VDV
TITLE HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH COMPOUND F3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 161-521;
COMPND 5 SYNONYM: H-CGAS,2'3'-CGAMP SYNTHASE,MAB-21 DOMAIN-CONTAINING PROTEIN
COMPND 6 1;
COMPND 7 EC: 2.7.7.86;
COMPND 8 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: MB21D1, C6ORF150;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, STING, CGAMP
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.BYRNES,J.D.HALL
REVDAT 4 04-OCT-23 5VDV 1 REMARK
REVDAT 3 06-DEC-17 5VDV 1 JRNL
REVDAT 2 04-OCT-17 5VDV 1 JRNL
REVDAT 1 27-SEP-17 5VDV 0
JRNL AUTH J.HALL,E.C.RALPH,S.SHANKER,H.WANG,L.J.BYRNES,R.HORST,J.WONG,
JRNL AUTH 2 A.BRAULT,D.DUMLAO,J.F.SMITH,L.A.DAKIN,D.C.SCHMITT,
JRNL AUTH 3 J.TRUJILLO,F.VINCENT,M.GRIFFOR,A.E.AULABAUGH
JRNL TITL THE CATALYTIC MECHANISM OF CYCLIC GMP-AMP SYNTHASE (CGAS)
JRNL TITL 2 AND IMPLICATIONS FOR INNATE IMMUNITY AND INHIBITION.
JRNL REF PROTEIN SCI. V. 26 2367 2017
JRNL REFN ESSN 1469-896X
JRNL PMID 28940468
JRNL DOI 10.1002/PRO.3304
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1999
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 17350
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 887
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 55.2772 - 5.4462 1.00 2843 158 0.2005 0.2296
REMARK 3 2 5.4462 - 4.3233 1.00 2732 154 0.1836 0.2347
REMARK 3 3 4.3233 - 3.7770 1.00 2759 140 0.1894 0.2697
REMARK 3 4 3.7770 - 3.4317 1.00 2709 161 0.2093 0.2645
REMARK 3 5 3.4317 - 3.1857 1.00 2708 139 0.2471 0.3279
REMARK 3 6 3.1857 - 2.9979 1.00 2712 135 0.2749 0.3478
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.60
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 : 0.002 5518
REMARK 3 ANGLE : 0.468 7487
REMARK 3 CHIRALITY : 0.024 843
REMARK 3 PLANARITY : 0.001 1051
REMARK 3 DIHEDRAL : 11.984 1958
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5782 -3.3167 -23.9259
REMARK 3 T TENSOR
REMARK 3 T11: 0.7354 T22: 0.8401
REMARK 3 T33: 0.7223 T12: -0.0579
REMARK 3 T13: -0.1322 T23: 0.1958
REMARK 3 L TENSOR
REMARK 3 L11: 8.8204 L22: 3.1062
REMARK 3 L33: 1.5041 L12: 0.1458
REMARK 3 L13: 2.3845 L23: 0.8607
REMARK 3 S TENSOR
REMARK 3 S11: 0.8210 S12: -0.4698 S13: -2.1335
REMARK 3 S21: 0.2699 S22: -0.3948 S23: -0.3524
REMARK 3 S31: 0.6474 S32: 0.4491 S33: -0.4119
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 307 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4249 12.9135 -21.1279
REMARK 3 T TENSOR
REMARK 3 T11: 0.4993 T22: 0.9567
REMARK 3 T33: 0.7070 T12: -0.2311
REMARK 3 T13: -0.0449 T23: 0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 2.5864 L22: 4.8272
REMARK 3 L33: 3.9949 L12: -1.6598
REMARK 3 L13: 0.2189 L23: 1.1044
REMARK 3 S TENSOR
REMARK 3 S11: 0.4082 S12: -0.3892 S13: -0.1283
REMARK 3 S21: 0.3745 S22: -0.2620 S23: -0.7880
REMARK 3 S31: 0.2506 S32: 0.5767 S33: -0.1917
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 308 THROUGH 521 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4343 14.2350 -20.9383
REMARK 3 T TENSOR
REMARK 3 T11: 0.5683 T22: 0.3040
REMARK 3 T33: 0.3974 T12: -0.1485
REMARK 3 T13: 0.0524 T23: -0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 3.2507 L22: 1.6661
REMARK 3 L33: 3.4677 L12: 0.0822
REMARK 3 L13: 0.6153 L23: 0.0750
REMARK 3 S TENSOR
REMARK 3 S11: -0.0714 S12: -0.0019 S13: 0.0769
REMARK 3 S21: -0.1538 S22: 0.0091 S23: -0.0864
REMARK 3 S31: -0.0768 S32: 0.3542 S33: 0.0527
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 195 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3803 18.5103 24.3991
REMARK 3 T TENSOR
REMARK 3 T11: 0.6473 T22: 0.6852
REMARK 3 T33: 0.7313 T12: -0.1073
REMARK 3 T13: 0.2204 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 3.4232 L22: 3.7909
REMARK 3 L33: 3.6989 L12: -2.4175
REMARK 3 L13: -3.2240 L23: 1.3184
REMARK 3 S TENSOR
REMARK 3 S11: 0.9230 S12: 0.2264 S13: 1.7949
REMARK 3 S21: -0.2649 S22: -0.3862 S23: -0.8362
REMARK 3 S31: -0.8766 S32: 0.8311 S33: -0.4886
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 196 THROUGH 307 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1790 1.2533 20.5453
REMARK 3 T TENSOR
REMARK 3 T11: 0.5701 T22: 1.3739
REMARK 3 T33: 1.1211 T12: 0.2307
REMARK 3 T13: 0.0750 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.6657 L22: 4.4943
REMARK 3 L33: 2.2853 L12: 0.8875
REMARK 3 L13: -0.1520 L23: 0.1129
REMARK 3 S TENSOR
REMARK 3 S11: 0.0859 S12: 0.0366 S13: -0.1869
REMARK 3 S21: -0.0704 S22: 0.1859 S23: -0.9803
REMARK 3 S31: -0.0434 S32: 1.0057 S33: -0.2284
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 308 THROUGH 434 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.2321 2.1018 18.0469
REMARK 3 T TENSOR
REMARK 3 T11: 0.5373 T22: 0.4640
REMARK 3 T33: 0.5317 T12: 0.0871
REMARK 3 T13: 0.0258 T23: 0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 2.6150 L22: 1.0794
REMARK 3 L33: 4.6517 L12: 0.3004
REMARK 3 L13: -0.4814 L23: 0.8635
REMARK 3 S TENSOR
REMARK 3 S11: -0.0096 S12: 0.1450 S13: -0.0382
REMARK 3 S21: -0.0717 S22: 0.1283 S23: -0.3745
REMARK 3 S31: -0.1656 S32: 0.6935 S33: -0.1000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 435 THROUGH 520 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.7039 -2.0602 24.3219
REMARK 3 T TENSOR
REMARK 3 T11: 0.5909 T22: 0.3584
REMARK 3 T33: 0.4463 T12: 0.1727
REMARK 3 T13: 0.0399 T23: 0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 3.3783 L22: 1.4595
REMARK 3 L33: 4.7401 L12: 0.9658
REMARK 3 L13: -1.5849 L23: 1.1654
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: -0.1086 S13: -0.4501
REMARK 3 S21: 0.1280 S22: 0.0475 S23: 0.1721
REMARK 3 S31: 0.2754 S32: 0.4676 S33: -0.0638
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 3062
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227276.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17370
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.998
REMARK 200 RESOLUTION RANGE LOW (A) : 55.268
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.17900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.90
REMARK 200 R MERGE FOR SHELL (I) : 0.35100
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: REFMAC
REMARK 200 STARTING MODEL: 4O67
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG 3350, 0.2 M AMMONIUM
REMARK 280 CITRATE PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 108.72400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.47650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 108.72400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.47650
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 160
REMARK 465 GLY A 303
REMARK 465 GLY A 304
REMARK 465 SER A 305
REMARK 465 PRO A 306
REMARK 465 PHE A 522
REMARK 465 MET B 160
REMARK 465 ILE B 291
REMARK 465 LYS B 292
REMARK 465 ASP B 293
REMARK 465 ARG B 302
REMARK 465 GLY B 303
REMARK 465 GLY B 304
REMARK 465 SER B 305
REMARK 465 PRO B 306
REMARK 465 GLU B 366
REMARK 465 GLY B 367
REMARK 465 ASN B 368
REMARK 465 GLU B 521
REMARK 465 PHE B 522
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 171 CG CD CE NZ
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 ARG A 176 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 179 CG1 CG2 CD1
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 LEU A 195 CG CD1 CD2
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 ILE A 220 CG1 CG2 CD1
REMARK 470 ARG A 236 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 ASN A 244 CG OD1 ND2
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 ARG A 255 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 256 CG OD1 ND2
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 GLU A 259 CG CD OE1 OE2
REMARK 470 LEU A 266 CG CD1 CD2
REMARK 470 GLU A 267 CG CD OE1 OE2
REMARK 470 GLU A 269 CG CD OE1 OE2
REMARK 470 LYS A 275 CG CD CE NZ
REMARK 470 LEU A 277 CG CD1 CD2
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 ARG A 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 282 CG CD CE NZ
REMARK 470 ILE A 284 CG1 CG2 CD1
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 GLU A 286 CG CD OE1 OE2
REMARK 470 GLU A 287 CG CD OE1 OE2
REMARK 470 ASP A 290 CG OD1 OD2
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 ASP A 293 CG OD1 OD2
REMARK 470 THR A 294 OG1 CG2
REMARK 470 ASP A 295 CG OD1 OD2
REMARK 470 ARG A 300 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 301 CG CD CE NZ
REMARK 470 ARG A 302 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 ASP A 319 CG OD1 OD2
REMARK 470 LYS A 350 CG CD CE NZ
REMARK 470 LYS A 365 CG CD CE NZ
REMARK 470 GLU A 366 CG CD OE1 OE2
REMARK 470 ASN A 368 CG OD1 ND2
REMARK 470 PHE A 370 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 372 CG CD OE1 OE2
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 GLU A 385 CG CD OE1 OE2
REMARK 470 LYS A 400 CG CD CE NZ
REMARK 470 GLU A 401 CG CD OE1 OE2
REMARK 470 LYS A 407 CG CD CE NZ
REMARK 470 LYS A 411 CG CD CE NZ
REMARK 470 ASP A 426 CG OD1 OD2
REMARK 470 LYS A 428 CG CD CE NZ
REMARK 470 ASP A 431 CG OD1 OD2
REMARK 470 LYS B 164 CG CD CE NZ
REMARK 470 GLU B 170 CG CD OE1 OE2
REMARK 470 LYS B 171 CG CD CE NZ
REMARK 470 LYS B 173 CG CD CE NZ
REMARK 470 LEU B 174 CG CD1 CD2
REMARK 470 ARG B 176 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 177 CG OD1 OD2
REMARK 470 ASP B 178 CG OD1 OD2
REMARK 470 ILE B 179 CG1 CG2 CD1
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 ASP B 191 CG OD1 OD2
REMARK 470 HIS B 192 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 195 CG CD1 CD2
REMARK 470 ARG B 196 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 197 CG CD1 CD2
REMARK 470 LYS B 198 CG CD CE NZ
REMARK 470 ARG B 204 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 208 CG CD1 CD2
REMARK 470 SER B 213 OG
REMARK 470 VAL B 218 CG1 CG2
REMARK 470 ILE B 220 CG1 CG2 CD1
REMARK 470 ASN B 224 CG OD1 ND2
REMARK 470 GLU B 225 CG CD OE1 OE2
REMARK 470 ARG B 236 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 240 CG CD OE1 OE2
REMARK 470 ASN B 244 CG OD1 ND2
REMARK 470 LYS B 252 CG CD CE NZ
REMARK 470 LYS B 254 CG CD CE NZ
REMARK 470 ARG B 255 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 256 CG OD1 ND2
REMARK 470 LYS B 258 CG CD CE NZ
REMARK 470 GLU B 259 CG CD OE1 OE2
REMARK 470 LEU B 262 CG CD1 CD2
REMARK 470 LEU B 266 CG CD1 CD2
REMARK 470 GLU B 267 CG CD OE1 OE2
REMARK 470 GLU B 269 CG CD OE1 OE2
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 LEU B 277 CG CD1 CD2
REMARK 470 LYS B 279 CG CD CE NZ
REMARK 470 ARG B 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 282 CG CD CE NZ
REMARK 470 ILE B 284 CG1 CG2 CD1
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 GLU B 286 CG CD OE1 OE2
REMARK 470 GLU B 287 CG CD OE1 OE2
REMARK 470 ILE B 288 CG1 CG2 CD1
REMARK 470 ASP B 290 CG OD1 OD2
REMARK 470 THR B 294 OG1 CG2
REMARK 470 ASP B 295 CG OD1 OD2
REMARK 470 LYS B 299 CG CD CE NZ
REMARK 470 ARG B 300 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 301 CG CD CE NZ
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 LYS B 315 CG CD CE NZ
REMARK 470 LEU B 322 CG CD1 CD2
REMARK 470 LYS B 350 CG CD CE NZ
REMARK 470 GLN B 351 CG CD OE1 NE2
REMARK 470 LYS B 362 CG CD CE NZ
REMARK 470 LYS B 365 CG CD CE NZ
REMARK 470 GLU B 372 CG CD OE1 OE2
REMARK 470 GLU B 373 CG CD OE1 OE2
REMARK 470 LYS B 384 CG CD CE NZ
REMARK 470 LYS B 400 CG CD CE NZ
REMARK 470 GLU B 401 CG CD OE1 OE2
REMARK 470 LYS B 411 CG CD CE NZ
REMARK 470 GLU B 418 CG CD OE1 OE2
REMARK 470 GLU B 422 CG CD OE1 OE2
REMARK 470 ASP B 426 CG OD1 OD2
REMARK 470 LYS B 427 CG CD CE NZ
REMARK 470 LYS B 428 CG CD CE NZ
REMARK 470 LYS B 432 CG CD CE NZ
REMARK 470 LYS B 458 CG CD CE NZ
REMARK 470 ARG B 499 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 515 CG CD OE1 OE2
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 SER A 313 O HOH A 701 2.10
REMARK 500 N GLN B 238 O LYS B 252 2.12
REMARK 500 N GLN A 238 O LYS A 252 2.17
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 PHE A 203 47.96 -96.79
REMARK 500 ASN A 210 49.73 -83.32
REMARK 500 ARG A 246 -9.32 82.11
REMARK 500 LYS A 254 20.79 -142.74
REMARK 500 SER A 328 -179.20 -69.10
REMARK 500 SER A 345 161.90 88.25
REMARK 500 LYS A 428 51.86 72.49
REMARK 500 ASN A 449 77.00 -113.60
REMARK 500 PHE A 516 73.99 46.58
REMARK 500 PHE B 203 47.63 -96.85
REMARK 500 ARG B 246 -9.19 82.33
REMARK 500 LYS B 254 21.04 -141.94
REMARK 500 SER B 328 -178.96 -69.04
REMARK 500 SER B 345 161.12 89.00
REMARK 500 LYS B 428 51.88 -90.73
REMARK 500 ASN B 449 76.85 -113.73
REMARK 500 PHE B 516 74.52 46.56
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 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 390 NE2
REMARK 620 2 CYS A 396 SG 117.7
REMARK 620 3 CYS A 397 SG 90.0 116.8
REMARK 620 4 CYS A 404 SG 111.6 111.5 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 390 NE2
REMARK 620 2 CYS B 396 SG 120.2
REMARK 620 3 CYS B 397 SG 93.7 117.8
REMARK 620 4 CYS B 404 SG 106.3 112.1 104.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BV A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BV B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BV B 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VDO RELATED DB: PDB
REMARK 900 RELATED ID: 5VDP RELATED DB: PDB
REMARK 900 RELATED ID: 5VDQ RELATED DB: PDB
REMARK 900 RELATED ID: 5VDR RELATED DB: PDB
REMARK 900 RELATED ID: 5VDS RELATED DB: PDB
REMARK 900 RELATED ID: 5VDT RELATED DB: PDB
REMARK 900 RELATED ID: 5VDU RELATED DB: PDB
REMARK 900 RELATED ID: 5VDW RELATED DB: PDB
DBREF 5VDV A 161 522 UNP Q8N884 CGAS_HUMAN 161 522
DBREF 5VDV B 161 522 UNP Q8N884 CGAS_HUMAN 161 522
SEQADV 5VDV MET A 160 UNP Q8N884 EXPRESSION TAG
SEQADV 5VDV MET B 160 UNP Q8N884 EXPRESSION TAG
SEQRES 1 A 363 MET GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU
SEQRES 2 A 363 LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET
SEQRES 3 A 363 VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS
SEQRES 4 A 363 CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR
SEQRES 5 A 363 GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN
SEQRES 6 A 363 GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE
SEQRES 7 A 363 GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE
SEQRES 8 A 363 VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER
SEQRES 9 A 363 GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET
SEQRES 10 A 363 LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN
SEQRES 11 A 363 ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG
SEQRES 12 A 363 GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS
SEQRES 13 A 363 ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER
SEQRES 14 A 363 SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN
SEQRES 15 A 363 ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU
SEQRES 16 A 363 LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY
SEQRES 17 A 363 ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER
SEQRES 18 A 363 HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER
SEQRES 19 A 363 LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG
SEQRES 20 A 363 LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN
SEQRES 21 A 363 LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS
SEQRES 22 A 363 PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL
SEQRES 23 A 363 CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS
SEQRES 24 A 363 ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE
SEQRES 25 A 363 LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE
SEQRES 26 A 363 ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP
SEQRES 27 A 363 LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR
SEQRES 28 A 363 GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE
SEQRES 1 B 363 MET GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU
SEQRES 2 B 363 LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET
SEQRES 3 B 363 VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS
SEQRES 4 B 363 CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR
SEQRES 5 B 363 GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN
SEQRES 6 B 363 GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE
SEQRES 7 B 363 GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE
SEQRES 8 B 363 VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER
SEQRES 9 B 363 GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET
SEQRES 10 B 363 LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN
SEQRES 11 B 363 ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG
SEQRES 12 B 363 GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS
SEQRES 13 B 363 ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER
SEQRES 14 B 363 SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN
SEQRES 15 B 363 ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU
SEQRES 16 B 363 LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY
SEQRES 17 B 363 ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER
SEQRES 18 B 363 HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER
SEQRES 19 B 363 LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG
SEQRES 20 B 363 LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN
SEQRES 21 B 363 LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS
SEQRES 22 B 363 PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL
SEQRES 23 B 363 CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS
SEQRES 24 B 363 ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE
SEQRES 25 B 363 LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE
SEQRES 26 B 363 ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP
SEQRES 27 B 363 LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR
SEQRES 28 B 363 GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE
HET ZN A 601 1
HET 9BV A 602 38
HET ZN B 601 1
HET SO4 B 602 5
HET 9BV B 603 38
HET 9BV B 604 19
HETNAM ZN ZINC ION
HETNAM 9BV TETRAZOLO[5,1-B]QUINAZOLIN-9-OL
HETNAM SO4 SULFATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 9BV 3(C8 H5 N5 O)
FORMUL 6 SO4 O4 S 2-
FORMUL 9 HOH *66(H2 O)
HELIX 1 AA1 GLY A 161 LEU A 174 1 14
HELIX 2 AA2 SER A 175 ALA A 182 1 8
HELIX 3 AA3 ALA A 182 ASP A 200 1 19
HELIX 4 AA4 GLY A 212 HIS A 217 1 6
HELIX 5 AA5 ASN A 260 LEU A 266 5 7
HELIX 6 AA6 SER A 272 ASN A 289 1 18
HELIX 7 AA7 ILE A 340 SER A 345 1 6
HELIX 8 AA8 SER A 345 LYS A 355 1 11
HELIX 9 AA9 PHE A 379 ASN A 388 1 10
HELIX 10 AB1 ASN A 399 LYS A 403 5 5
HELIX 11 AB2 CYS A 405 PHE A 424 1 20
HELIX 12 AB3 HIS A 429 PHE A 433 5 5
HELIX 13 AB4 SER A 434 ASN A 449 1 16
HELIX 14 AB5 GLN A 451 LYS A 458 5 8
HELIX 15 AB6 ASP A 459 GLU A 478 1 20
HELIX 16 AB7 ASP A 497 ASN A 514 1 18
HELIX 17 AB8 ALA B 162 LEU B 174 1 13
HELIX 18 AB9 SER B 175 ALA B 182 1 8
HELIX 19 AC1 ALA B 182 ASP B 200 1 19
HELIX 20 AC2 ASN B 260 LEU B 266 5 7
HELIX 21 AC3 SER B 272 ASN B 289 1 18
HELIX 22 AC4 ILE B 340 SER B 345 1 6
HELIX 23 AC5 SER B 345 LYS B 355 1 11
HELIX 24 AC6 PHE B 379 ASN B 388 1 10
HELIX 25 AC7 ASN B 399 LYS B 403 5 5
HELIX 26 AC8 CYS B 405 PHE B 424 1 20
HELIX 27 AC9 HIS B 429 PHE B 433 5 5
HELIX 28 AD1 SER B 434 ASN B 449 1 16
HELIX 29 AD2 GLN B 451 LYS B 458 5 8
HELIX 30 AD3 ASP B 459 GLU B 478 1 20
HELIX 31 AD4 ASP B 497 ASN B 514 1 18
SHEET 1 AA1 7 VAL A 206 LEU A 208 0
SHEET 2 AA1 7 GLU A 225 GLU A 233 -1 O LYS A 231 N GLY A 207
SHEET 3 AA1 7 ILE A 316 SER A 326 1 O THR A 321 N PHE A 230
SHEET 4 AA1 7 PHE A 357 PRO A 361 -1 O PHE A 357 N SER A 326
SHEET 5 AA1 7 TRP A 375 SER A 378 -1 O ARG A 376 N VAL A 360
SHEET 6 AA1 7 TYR A 248 PHE A 253 -1 N TYR A 249 O TRP A 375
SHEET 7 AA1 7 ILE A 237 GLU A 241 -1 N GLN A 238 O LYS A 252
SHEET 1 AA2 5 VAL A 206 LEU A 208 0
SHEET 2 AA2 5 GLU A 225 GLU A 233 -1 O LYS A 231 N GLY A 207
SHEET 3 AA2 5 ILE A 316 SER A 326 1 O THR A 321 N PHE A 230
SHEET 4 AA2 5 VAL A 308 ILE A 312 -1 N ILE A 312 O ILE A 316
SHEET 5 AA2 5 VAL A 296 MET A 298 -1 N ILE A 297 O LEU A 311
SHEET 1 AA3 2 ALA A 364 GLU A 366 0
SHEET 2 AA3 2 GLY A 369 GLN A 371 -1 O GLN A 371 N ALA A 364
SHEET 1 AA4 7 VAL B 206 LEU B 208 0
SHEET 2 AA4 7 GLU B 225 GLU B 233 -1 O LYS B 231 N GLY B 207
SHEET 3 AA4 7 ILE B 316 SER B 326 1 O THR B 321 N PHE B 230
SHEET 4 AA4 7 PHE B 357 PRO B 361 -1 O PHE B 357 N SER B 326
SHEET 5 AA4 7 TRP B 375 SER B 378 -1 O ARG B 376 N VAL B 360
SHEET 6 AA4 7 TYR B 248 PHE B 253 -1 N TYR B 249 O TRP B 375
SHEET 7 AA4 7 ILE B 237 GLU B 241 -1 N GLN B 238 O LYS B 252
SHEET 1 AA5 5 VAL B 206 LEU B 208 0
SHEET 2 AA5 5 GLU B 225 GLU B 233 -1 O LYS B 231 N GLY B 207
SHEET 3 AA5 5 ILE B 316 SER B 326 1 O THR B 321 N PHE B 230
SHEET 4 AA5 5 VAL B 308 ILE B 312 -1 N ILE B 312 O ILE B 316
SHEET 5 AA5 5 VAL B 296 MET B 298 -1 N ILE B 297 O LEU B 311
LINK NE2 HIS A 390 ZN ZN A 601 1555 1555 2.10
LINK SG CYS A 396 ZN ZN A 601 1555 1555 2.37
LINK SG CYS A 397 ZN ZN A 601 1555 1555 2.17
LINK SG CYS A 404 ZN ZN A 601 1555 1555 2.25
LINK NE2 HIS B 390 ZN ZN B 601 1555 1555 2.09
LINK SG CYS B 396 ZN ZN B 601 1555 1555 2.28
LINK SG CYS B 397 ZN ZN B 601 1555 1555 2.20
LINK SG CYS B 404 ZN ZN B 601 1555 1555 2.30
SITE 1 AC1 4 HIS A 390 CYS A 396 CYS A 397 CYS A 404
SITE 1 AC2 8 ARG A 376 LEU A 377 TYR A 436 HIS A 437
SITE 2 AC2 8 ASN A 482 LEU A 490 HOH A 721 HOH A 728
SITE 1 AC3 4 HIS B 390 CYS B 396 CYS B 397 CYS B 404
SITE 1 AC4 5 ARG A 300 ARG B 423 GLU B 511 PRO B 517
SITE 2 AC4 5 VAL B 518
SITE 1 AC5 6 ARG B 376 SER B 434 TYR B 436 ASN B 482
SITE 2 AC5 6 HOH B 717 HOH B 722
SITE 1 AC6 5 LYS A 299 LEU A 311 ARG B 423 GLN B 507
SITE 2 AC6 5 TYR B 510
CRYST1 217.448 46.953 89.733 90.00 111.43 90.00 C 1 2 1 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 0.004599 0.000000 0.001805 0.00000
SCALE2 0.000000 0.021298 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011972 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
