HEADER SIGNALING PROTEIN 18-MAY-15 4ZVG
TITLE CRYSTAL STRUCTURE OF GGDEF DOMAIN OF THE E. COLI DOSC - FORM III
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIGUANYLATE CYCLASE DOSC;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 297-460;
COMPND 5 SYNONYM: DGC,DIRECT OXYGEN-SENSING CYCLASE;
COMPND 6 EC: 2.7.7.65;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: DOSC, YDDV, B1490, JW5241;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXYGEN SENSING, DIGUANYLATE CYCLASE, CYCLIC-DI-GMP, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,T.R.M.BARENDS,I.SCHLICHTING
REVDAT 2 10-JAN-24 4ZVG 1 REMARK
REVDAT 1 11-NOV-15 4ZVG 0
JRNL AUTH M.TARNAWSKI,T.R.BARENDS,I.SCHLICHTING
JRNL TITL STRUCTURAL ANALYSIS OF AN OXYGEN-REGULATED DIGUANYLATE
JRNL TITL 2 CYCLASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 2158 2015
JRNL REFN ESSN 1399-0047
JRNL PMID 26527135
JRNL DOI 10.1107/S139900471501545X
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 18580
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 929
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 48.6215 - 4.2078 0.99 2699 143 0.1747 0.1916
REMARK 3 2 4.2078 - 3.3401 0.99 2575 135 0.1872 0.2392
REMARK 3 3 3.3401 - 2.9179 0.99 2557 135 0.2200 0.2648
REMARK 3 4 2.9179 - 2.6512 0.98 2502 131 0.2402 0.3319
REMARK 3 5 2.6512 - 2.4612 0.97 2459 130 0.2469 0.3024
REMARK 3 6 2.4612 - 2.3161 0.96 2448 129 0.2689 0.3423
REMARK 3 7 2.3161 - 2.2001 0.96 2411 126 0.2885 0.3372
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.220
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 : 0.008 2702
REMARK 3 ANGLE : 1.132 3642
REMARK 3 CHIRALITY : 0.047 411
REMARK 3 PLANARITY : 0.006 469
REMARK 3 DIHEDRAL : 11.758 1022
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 4ZVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97627
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18580
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.78300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.540
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: 4ZVE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE, 22%
REMARK 280 (W/V) PEG 3350, VAPOR DIFFUSION, 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 26.89000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.81000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.46500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.81000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.89000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.46500
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 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 GLU A 462
REMARK 465 HIS A 463
REMARK 465 HIS A 464
REMARK 465 HIS A 465
REMARK 465 HIS A 466
REMARK 465 HIS A 467
REMARK 465 HIS A 468
REMARK 465 MET B 297
REMARK 465 GLU B 462
REMARK 465 HIS B 463
REMARK 465 HIS B 464
REMARK 465 HIS B 465
REMARK 465 HIS B 466
REMARK 465 HIS B 467
REMARK 465 HIS B 468
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 ARG B 372 O HOH B 501 2.06
REMARK 500 OD2 ASP B 298 O HOH B 502 2.15
REMARK 500 NH1 ARG B 307 O HOH B 503 2.15
REMARK 500 O HOH B 519 O HOH B 524 2.16
REMARK 500 O HOH A 539 O HOH A 540 2.18
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 386 171.77 -59.79
REMARK 500 ARG A 450 -175.74 66.64
REMARK 500 ARG B 450 -177.77 61.39
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4ZVG A 297 460 UNP P0AA89 DOSC_ECOLI 297 460
DBREF 4ZVG B 297 460 UNP P0AA89 DOSC_ECOLI 297 460
SEQADV 4ZVG LEU A 461 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG GLU A 462 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS A 463 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS A 464 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS A 465 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS A 466 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS A 467 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS A 468 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG LEU B 461 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG GLU B 462 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS B 463 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS B 464 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS B 465 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS B 466 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS B 467 UNP P0AA89 EXPRESSION TAG
SEQADV 4ZVG HIS B 468 UNP P0AA89 EXPRESSION TAG
SEQRES 1 A 172 MET ASP VAL LEU THR LYS LEU LEU ASN ARG ARG PHE LEU
SEQRES 2 A 172 PRO THR ILE PHE LYS ARG GLU ILE ALA HIS ALA ASN ARG
SEQRES 3 A 172 THR GLY THR PRO LEU SER VAL LEU ILE ILE ASP VAL ASP
SEQRES 4 A 172 LYS PHE LYS GLU ILE ASN ASP THR TRP GLY HIS ASN THR
SEQRES 5 A 172 GLY ASP GLU ILE LEU ARG LYS VAL SER GLN ALA PHE TYR
SEQRES 6 A 172 ASP ASN VAL ARG SER SER ASP TYR VAL PHE ARG TYR GLY
SEQRES 7 A 172 GLY ASP GLU PHE ILE ILE VAL LEU THR GLU ALA SER GLU
SEQRES 8 A 172 ASN GLU THR LEU ARG THR ALA GLU ARG ILE ARG SER ARG
SEQRES 9 A 172 VAL GLU LYS THR LYS LEU LYS ALA ALA ASN GLY GLU ASP
SEQRES 10 A 172 ILE ALA LEU SER LEU SER ILE GLY ALA ALA MET PHE ASN
SEQRES 11 A 172 GLY HIS PRO ASP TYR GLU ARG LEU ILE GLN ILE ALA ASP
SEQRES 12 A 172 GLU ALA LEU TYR ILE ALA LYS ARG ARG GLY ARG ASN ARG
SEQRES 13 A 172 VAL GLU LEU TRP LYS ALA SER LEU LEU GLU HIS HIS HIS
SEQRES 14 A 172 HIS HIS HIS
SEQRES 1 B 172 MET ASP VAL LEU THR LYS LEU LEU ASN ARG ARG PHE LEU
SEQRES 2 B 172 PRO THR ILE PHE LYS ARG GLU ILE ALA HIS ALA ASN ARG
SEQRES 3 B 172 THR GLY THR PRO LEU SER VAL LEU ILE ILE ASP VAL ASP
SEQRES 4 B 172 LYS PHE LYS GLU ILE ASN ASP THR TRP GLY HIS ASN THR
SEQRES 5 B 172 GLY ASP GLU ILE LEU ARG LYS VAL SER GLN ALA PHE TYR
SEQRES 6 B 172 ASP ASN VAL ARG SER SER ASP TYR VAL PHE ARG TYR GLY
SEQRES 7 B 172 GLY ASP GLU PHE ILE ILE VAL LEU THR GLU ALA SER GLU
SEQRES 8 B 172 ASN GLU THR LEU ARG THR ALA GLU ARG ILE ARG SER ARG
SEQRES 9 B 172 VAL GLU LYS THR LYS LEU LYS ALA ALA ASN GLY GLU ASP
SEQRES 10 B 172 ILE ALA LEU SER LEU SER ILE GLY ALA ALA MET PHE ASN
SEQRES 11 B 172 GLY HIS PRO ASP TYR GLU ARG LEU ILE GLN ILE ALA ASP
SEQRES 12 B 172 GLU ALA LEU TYR ILE ALA LYS ARG ARG GLY ARG ASN ARG
SEQRES 13 B 172 VAL GLU LEU TRP LYS ALA SER LEU LEU GLU HIS HIS HIS
SEQRES 14 B 172 HIS HIS HIS
FORMUL 3 HOH *78(H2 O)
HELIX 1 AA1 ASP A 298 LEU A 303 5 6
HELIX 2 AA2 PHE A 308 GLY A 324 1 17
HELIX 3 AA3 LYS A 336 GLY A 345 1 10
HELIX 4 AA4 GLY A 345 ASP A 362 1 18
HELIX 5 AA5 SER A 386 THR A 404 1 19
HELIX 6 AA6 ASP A 430 ARG A 448 1 19
HELIX 7 AA7 ASP B 298 LYS B 302 5 5
HELIX 8 AA8 PHE B 308 GLY B 324 1 17
HELIX 9 AA9 LYS B 336 GLY B 345 1 10
HELIX 10 AB1 GLY B 345 ASP B 362 1 18
HELIX 11 AB2 SER B 386 THR B 404 1 19
HELIX 12 AB3 ASP B 430 ARG B 448 1 19
SHEET 1 AA1 6 LEU A 304 ASN A 305 0
SHEET 2 AA1 6 TYR A 369 ARG A 372 1 O VAL A 370 N LEU A 304
SHEET 3 AA1 6 GLU A 377 THR A 383 -1 O ILE A 379 N PHE A 371
SHEET 4 AA1 6 LEU A 327 VAL A 334 -1 N ILE A 332 O PHE A 378
SHEET 5 AA1 6 LEU A 418 MET A 424 -1 O SER A 419 N ASP A 333
SHEET 6 AA1 6 ARG A 452 LEU A 455 1 O GLU A 454 N ALA A 422
SHEET 1 AA2 6 LEU B 304 ASN B 305 0
SHEET 2 AA2 6 TYR B 369 ARG B 372 1 O VAL B 370 N LEU B 304
SHEET 3 AA2 6 GLU B 377 THR B 383 -1 O ILE B 379 N PHE B 371
SHEET 4 AA2 6 LEU B 327 VAL B 334 -1 N ILE B 332 O PHE B 378
SHEET 5 AA2 6 LEU B 418 MET B 424 -1 O GLY B 421 N ILE B 331
SHEET 6 AA2 6 ARG B 452 LEU B 455 1 O GLU B 454 N ALA B 422
CRYST1 53.780 58.930 113.620 90.00 90.00 90.00 P 21 21 21 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 0.018594 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016969 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008801 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
