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HEADER CELL ADHESION 05-MAY-09 3HC7
TITLE CRYSTAL STRUCTURE OF LYSIN B FROM MYCOBACTERIOPHAGE D29
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENE 12 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GP12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM PHAGE D29;
SOURCE 3 ORGANISM_TAXID: 28369;
SOURCE 4 GENE: 12, GP12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLAM3
KEYWDS ALPHA/BETA SANDWICH, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.SUN,J.C.SACCHETTINI
REVDAT 2 25-AUG-09 3HC7 1 JRNL
REVDAT 1 21-JUL-09 3HC7 0
JRNL AUTH K.PAYNE,Q.SUN,J.SACCHETTINI,G.F.HATFULL
JRNL TITL MYCOBACTERIOPHAGE LYSIN B IS A NOVEL
JRNL TITL 2 MYCOLYLARABINOGALACTAN ESTERASE
JRNL REF MOL.MICROBIOL. V. 73 367 2009
JRNL REFN ISSN 0950-382X
JRNL PMID 19555454
JRNL DOI 10.1111/J.1365-2958.2009.06775.X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 19777
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1978
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 35.5780 - 6.6040 0.87 579 0 0.2260 0.0000
REMARK 3 2 6.6040 - 5.2470 0.90 549 0 0.2100 0.0000
REMARK 3 3 5.2470 - 4.5860 0.90 551 0 0.1770 0.0000
REMARK 3 4 4.5860 - 4.1670 0.90 537 0 0.1520 0.0000
REMARK 3 5 4.1670 - 3.8690 0.90 524 0 0.1580 0.0000
REMARK 3 6 3.8690 - 3.6410 0.90 536 0 0.1540 0.0000
REMARK 3 7 3.6410 - 3.4590 0.90 528 0 0.1750 0.0000
REMARK 3 8 3.4590 - 3.3080 0.90 514 0 0.1960 0.0000
REMARK 3 9 3.3080 - 3.1810 0.90 534 0 0.1730 0.0000
REMARK 3 10 3.1810 - 3.0710 0.90 529 0 0.1990 0.0000
REMARK 3 11 3.0710 - 2.9750 0.90 513 0 0.1880 0.0000
REMARK 3 12 2.9750 - 2.8900 0.90 521 0 0.1910 0.0000
REMARK 3 13 2.8900 - 2.8140 0.90 524 0 0.2060 0.0000
REMARK 3 14 2.8140 - 2.7460 0.90 514 0 0.2030 0.0000
REMARK 3 15 2.7460 - 2.6830 0.89 521 0 0.2080 0.0000
REMARK 3 16 2.6830 - 2.6260 0.90 513 0 0.1940 0.0000
REMARK 3 17 2.6260 - 2.5740 0.89 497 0 0.1930 0.0000
REMARK 3 18 2.5740 - 2.5250 0.89 527 0 0.2070 0.0000
REMARK 3 19 2.5250 - 2.4800 0.90 511 0 0.2050 0.0000
REMARK 3 20 2.4800 - 2.4380 0.89 522 0 0.2100 0.0000
REMARK 3 21 2.4380 - 2.3990 0.90 501 0 0.2200 0.0000
REMARK 3 22 2.3990 - 2.3620 0.90 511 0 0.2150 0.0000
REMARK 3 23 2.3620 - 2.3270 0.89 507 0 0.2310 0.0000
REMARK 3 24 2.3270 - 2.2940 0.89 519 0 0.2440 0.0000
REMARK 3 25 2.2940 - 2.2630 0.85 482 0 0.2730 0.0000
REMARK 3 26 2.2630 - 2.2340 0.89 512 0 0.2900 0.0000
REMARK 3 27 2.2340 - 2.2060 0.87 483 0 0.2720 0.0000
REMARK 3 28 2.2060 - 2.1790 0.89 503 0 0.2440 0.0000
REMARK 3 29 2.1790 - 2.1540 0.89 516 0 0.2680 0.0000
REMARK 3 30 2.1540 - 2.1300 0.89 509 0 0.2600 0.0000
REMARK 3 31 2.1300 - 2.1070 0.89 494 0 0.2770 0.0000
REMARK 3 32 2.1070 - 2.0850 0.89 522 0 0.3000 0.0000
REMARK 3 33 2.0850 - 2.0630 0.89 485 0 0.2990 0.0000
REMARK 3 34 2.0630 - 2.0430 0.77 436 0 0.2910 0.0000
REMARK 3 35 2.0430 - 2.0230 0.35 202 0 0.2670 0.0000
REMARK 3 36 2.0230 - 2.0000 0.13 73 0 0.2620 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 82.08
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.51200
REMARK 3 B22 (A**2) : -1.51200
REMARK 3 B33 (A**2) : 3.02400
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.004 NULL
REMARK 3 ANGLE : 0.635 NULL
REMARK 3 CHIRALITY : 0.051 NULL
REMARK 3 PLANARITY : 0.003 NULL
REMARK 3 DIHEDRAL : 9.597 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: NONE
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5080 18.9103 22.0644
REMARK 3 T TENSOR
REMARK 3 T11: 0.4638 T22: 0.2726
REMARK 3 T33: 0.1290 T12: 0.1943
REMARK 3 T13: -0.0104 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 2.1864 L22: 3.7345
REMARK 3 L33: 0.7645 L12: -2.1560
REMARK 3 L13: -0.5771 L23: 1.0531
REMARK 3 S TENSOR
REMARK 3 S11: 0.6922 S12: 0.5277 S13: -0.0389
REMARK 3 S21: -1.0313 S22: -0.6163 S23: -0.0235
REMARK 3 S31: -0.2592 S32: -0.2555 S33: -0.0696
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 3HC7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB052955.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMETER. ADJUSTABLE
REMARK 200 FOCUSING MIRRORS IN K-B
REMARK 200 GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21027
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS PH8, 20% PEG1000, 100MM
REMARK 280 CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 34.81500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 46.26500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.26500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.22250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.26500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.26500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 17.40750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.26500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.26500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.22250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.26500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.26500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 17.40750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 34.81500
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2001 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2028 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2030 LIES ON A SPECIAL POSITION.
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 ILE A 254
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 TYR A 73 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 172 CG CD CE NZ
REMARK 470 GLU A 173 CG CD OE1 OE2
REMARK 470 GLU A 206 CD OE1 OE2
REMARK 470 ARG A 231 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 249 CG CD OE1 OE2
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 82 -117.84 51.13
REMARK 500 TRP A 131 -153.47 -151.55
REMARK 500 GLN A 209 -51.69 73.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2054 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A2083 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH A2090 DISTANCE = 6.16 ANGSTROMS
DBREF 3HC7 A 1 254 UNP O64205 VG12_BPMD2 1 254
SEQRES 1 A 254 MET SER LYS PRO TRP LEU PHE THR VAL HIS GLY THR GLY
SEQRES 2 A 254 GLN PRO ASP PRO LEU GLY PRO GLY LEU PRO ALA ASP THR
SEQRES 3 A 254 ALA ARG ASP VAL LEU ASP ILE TYR ARG TRP GLN PRO ILE
SEQRES 4 A 254 GLY ASN TYR PRO ALA ALA ALA PHE PRO MET TRP PRO SER
SEQRES 5 A 254 VAL GLU LYS GLY VAL ALA GLU LEU ILE LEU GLN ILE GLU
SEQRES 6 A 254 LEU LYS LEU ASP ALA ASP PRO TYR ALA ASP PHE ALA MET
SEQRES 7 A 254 ALA GLY TYR SER GLN GLY ALA ILE VAL VAL GLY GLN VAL
SEQRES 8 A 254 LEU LYS HIS HIS ILE LEU PRO PRO THR GLY ARG LEU HIS
SEQRES 9 A 254 ARG PHE LEU HIS ARG LEU LYS LYS VAL ILE PHE TRP GLY
SEQRES 10 A 254 ASN PRO MET ARG GLN LYS GLY PHE ALA HIS SER ASP GLU
SEQRES 11 A 254 TRP ILE HIS PRO VAL ALA ALA PRO ASP THR LEU GLY ILE
SEQRES 12 A 254 LEU GLU ASP ARG LEU GLU ASN LEU GLU GLN TYR GLY PHE
SEQRES 13 A 254 GLU VAL ARG ASP TYR ALA HIS ASP GLY ASP MET TYR ALA
SEQRES 14 A 254 SER ILE LYS GLU ASP ASP LEU HIS GLU TYR GLU VAL ALA
SEQRES 15 A 254 ILE GLY ARG ILE VAL MET LYS ALA SER GLY PHE ILE GLY
SEQRES 16 A 254 GLY ARG ASP SER VAL VAL ALA GLN LEU ILE GLU LEU GLY
SEQRES 17 A 254 GLN ARG PRO ILE THR GLU GLY ILE ALA LEU ALA GLY ALA
SEQRES 18 A 254 ILE ILE ASP ALA LEU THR PHE PHE ALA ARG SER ARG MET
SEQRES 19 A 254 GLY ASP LYS TRP PRO HIS LEU TYR ASN ARG TYR PRO ALA
SEQRES 20 A 254 VAL GLU PHE LEU ARG GLN ILE
FORMUL 2 HOH *121(H2 O)
HELIX 1 1 GLY A 21 ARG A 28 1 8
HELIX 2 2 MET A 49 ASP A 71 1 23
HELIX 3 3 SER A 82 ILE A 96 1 15
HELIX 4 4 LEU A 103 HIS A 108 5 6
HELIX 5 5 ASN A 150 TYR A 154 5 5
HELIX 6 6 ASP A 166 SER A 170 5 5
HELIX 7 7 ASP A 174 LEU A 176 5 3
HELIX 8 8 GLU A 178 ALA A 190 1 13
HELIX 9 9 SER A 199 GLY A 208 1 10
HELIX 10 10 PRO A 211 ARG A 231 1 21
HELIX 11 11 ARG A 244 ARG A 252 1 9
SHEET 1 A 5 ARG A 35 PRO A 38 0
SHEET 2 A 5 TRP A 5 VAL A 9 1 N LEU A 6 O GLN A 37
SHEET 3 A 5 PHE A 76 TYR A 81 1 O ALA A 79 N PHE A 7
SHEET 4 A 5 LEU A 110 TRP A 116 1 O ILE A 114 N MET A 78
SHEET 5 A 5 GLU A 157 TYR A 161 1 O ARG A 159 N VAL A 113
SHEET 1 B 2 THR A 140 LEU A 141 0
SHEET 2 B 2 ILE A 171 LYS A 172 -1 O ILE A 171 N LEU A 141
CISPEP 1 PHE A 47 PRO A 48 0 -0.68
CRYST1 92.530 92.530 69.630 90.00 90.00 90.00 P 43 21 2 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 0.010807 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010807 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014362 0.00000
TER 1974 GLN A 253
MASTER 328 0 0 11 7 0 0 6 2094 1 0 20
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