HEADER TRANSFERASE 24-JUL-18 6H5F
TITLE LTGA DISORDERED HELIX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS NM422;
SOURCE 3 ORGANISM_TAXID: 1095701;
SOURCE 4 GENE: NMB1949;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: GOLD
KEYWDS PEPTIDOGLYCAN, ANTIBIOTIC RESISTANCE, ENZYME HUB, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.H.WILLIAMS
REVDAT 4 17-JAN-24 6H5F 1 REMARK
REVDAT 3 05-AUG-20 6H5F 1 JRNL
REVDAT 2 04-SEP-19 6H5F 1 COMPND SOURCE DBREF
REVDAT 1 28-AUG-19 6H5F 0
SPRSDE 28-AUG-19 6H5F 4YP4
JRNL AUTH A.H.WILLIAMS,R.WHEELER,A.E.DEGHMANE,I.SANTECCHIA,R.E.SCHAUB,
JRNL AUTH 2 S.HICHAM,M.MOYA NILGES,C.MALOSSE,J.CHAMOT-ROOKE,A.HAOUZ,
JRNL AUTH 3 J.P.DILLARD,W.P.ROBINS,M.K.TAHA,I.GOMPERTS BONECA
JRNL TITL DEFECTIVE LYTIC TRANSGLYCOSYLASE DISRUPTS CELL MORPHOGENESIS
JRNL TITL 2 BY HINDERING CELL WALL DE-O-ACETYLATION INNEISSERIA
JRNL TITL 3 MENINGITIDIS.
JRNL REF ELIFE V. 9 2020
JRNL REFN ESSN 2050-084X
JRNL PMID 32022687
JRNL DOI 10.7554/ELIFE.51247
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 40497
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 49.0738 - 4.8074 1.00 2974 153 0.1667 0.1886
REMARK 3 2 4.8074 - 3.8162 1.00 2836 148 0.1514 0.2203
REMARK 3 3 3.8162 - 3.3340 1.00 2810 147 0.1812 0.2228
REMARK 3 4 3.3340 - 3.0292 1.00 2785 143 0.2112 0.2871
REMARK 3 5 3.0292 - 2.8121 0.99 2762 157 0.2289 0.3423
REMARK 3 6 2.8121 - 2.6463 0.99 2764 141 0.2216 0.2646
REMARK 3 7 2.6463 - 2.5138 0.99 2749 145 0.2178 0.2873
REMARK 3 8 2.5138 - 2.4044 0.99 2720 136 0.2162 0.2924
REMARK 3 9 2.4044 - 2.3118 0.99 2752 140 0.2174 0.2932
REMARK 3 10 2.3118 - 2.2320 0.98 2691 149 0.2154 0.3051
REMARK 3 11 2.2320 - 2.1622 0.99 2715 134 0.2395 0.2907
REMARK 3 12 2.1622 - 2.1004 0.98 2702 139 0.2702 0.3025
REMARK 3 13 2.1004 - 2.0451 0.98 2674 157 0.2947 0.3541
REMARK 3 14 2.0451 - 1.9952 0.92 2564 110 0.3274 0.3582
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.970
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 4478
REMARK 3 ANGLE : 0.963 6065
REMARK 3 CHIRALITY : 0.038 645
REMARK 3 PLANARITY : 0.004 807
REMARK 3 DIHEDRAL : 14.242 1655
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 6H5F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200011068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40499
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.955
REMARK 200 RESOLUTION RANGE LOW (A) : 49.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 7.740
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
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 (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.06300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.470
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: 4YIB
REMARK 200
REMARK 200 REMARK: RECTANGULAR IN SHAPE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 33% (W/V) PEG 6000, 0.01 M TRI SODIUM
REMARK 280 CITRATE., PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K, VAPOR DIFFUSION, SITTING DROP
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 33.41100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.15650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.12800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.15650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.41100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.12800
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 MET A 1
REMARK 465 TYR A 2
REMARK 465 LEU A 3
REMARK 465 PRO A 4
REMARK 465 SER A 5
REMARK 465 MET A 6
REMARK 465 LYS A 7
REMARK 465 HIS A 8
REMARK 465 SER A 9
REMARK 465 LEU A 10
REMARK 465 PRO A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 LEU A 16
REMARK 465 VAL A 17
REMARK 465 LEU A 18
REMARK 465 ALA A 19
REMARK 465 ALA A 20
REMARK 465 CYS A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 ASN A 25
REMARK 465 THR A 26
REMARK 465 LEU A 27
REMARK 465 PRO A 28
REMARK 465 ALA A 29
REMARK 465 GLY A 30
REMARK 465 LYS A 31
REMARK 465 THR A 32
REMARK 465 PRO A 33
REMARK 465 ALA A 34
REMARK 465 ASP A 35
REMARK 465 ASN A 36
REMARK 465 ILE A 37
REMARK 465 GLU A 38
REMARK 465 THR A 39
REMARK 465 ALA A 40
REMARK 465 MET A 501
REMARK 465 PRO A 502
REMARK 465 ALA A 503
REMARK 465 THR A 504
REMARK 465 ALA A 505
REMARK 465 ARG A 506
REMARK 465 GLU A 507
REMARK 465 ILE A 508
REMARK 465 ALA A 509
REMARK 465 GLY A 510
REMARK 465 LYS A 511
REMARK 465 ILE A 512
REMARK 465 GLY A 513
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 ARG A 55 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 361 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 515 CG OD1 OD2
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 ALA A 165 O HOH A 701 2.13
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 48 40.40 -141.89
REMARK 500 LYS A 74 31.74 72.97
REMARK 500 PRO A 153 154.99 -48.62
REMARK 500 THR A 205 -145.35 -92.08
REMARK 500 LEU A 213 1.54 -65.43
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6H5F A 1 616 UNP Q9JXP1 Q9JXP1_NEIMB 1 616
SEQRES 1 A 616 MET TYR LEU PRO SER MET LYS HIS SER LEU PRO LEU LEU
SEQRES 2 A 616 ALA ALA LEU VAL LEU ALA ALA CYS SER SER THR ASN THR
SEQRES 3 A 616 LEU PRO ALA GLY LYS THR PRO ALA ASP ASN ILE GLU THR
SEQRES 4 A 616 ALA ASP LEU SER ALA SER VAL PRO THR ARG PRO ALA GLU
SEQRES 5 A 616 PRO GLU ARG LYS THR LEU ALA ASP TYR GLY GLY TYR PRO
SEQRES 6 A 616 SER ALA LEU ASP ALA VAL LYS GLN LYS ASN ASP ALA ALA
SEQRES 7 A 616 VAL ALA ALA TYR LEU GLU ASN ALA GLY ASP SER ALA MET
SEQRES 8 A 616 ALA GLU ASN VAL ARG ASN GLU TRP LEU LYS SER LEU GLY
SEQRES 9 A 616 ALA ARG ARG GLN TRP THR LEU PHE ALA GLN GLU TYR ALA
SEQRES 10 A 616 LYS LEU GLU PRO ALA GLY ARG ALA GLN GLU VAL GLU CYS
SEQRES 11 A 616 TYR ALA ASP SER SER ARG ASN ASP TYR THR ARG ALA ALA
SEQRES 12 A 616 GLU LEU VAL LYS ASN THR GLY LYS LEU PRO SER GLY CYS
SEQRES 13 A 616 THR LYS LEU LEU GLU GLN ALA ALA ALA SER GLY LEU LEU
SEQRES 14 A 616 ASP GLY ASN ASP ALA TRP ARG ARG VAL ARG GLY LEU LEU
SEQRES 15 A 616 ALA GLY ARG GLN THR THR ASP ALA ARG ASN LEU ALA ALA
SEQRES 16 A 616 ALA LEU GLY SER PRO PHE ASP GLY GLY THR GLN GLY SER
SEQRES 17 A 616 ARG GLU TYR ALA LEU LEU ASN VAL ILE GLY LYS GLU ALA
SEQRES 18 A 616 ARG LYS SER PRO ASN ALA ALA ALA LEU LEU SER GLU MET
SEQRES 19 A 616 GLU SER GLY LEU SER LEU GLU GLN ARG SER PHE ALA TRP
SEQRES 20 A 616 GLY VAL LEU GLY HIS TYR GLN SER GLN ASN LEU ASN VAL
SEQRES 21 A 616 PRO ALA ALA LEU ASP TYR TYR GLY LYS VAL ALA ASP ARG
SEQRES 22 A 616 ARG GLN LEU THR ASP ASP GLN ILE GLU TRP TYR ALA ARG
SEQRES 23 A 616 ALA ALA LEU ARG ALA ARG ARG TRP ASP GLU LEU ALA SER
SEQRES 24 A 616 VAL ILE SER HIS MET PRO GLU LYS LEU GLN LYS SER PRO
SEQRES 25 A 616 THR TRP LEU TYR TRP LEU ALA ARG SER ARG ALA ALA THR
SEQRES 26 A 616 GLY ASN THR GLN GLU ALA GLU LYS LEU TYR LYS GLN ALA
SEQRES 27 A 616 ALA ALA THR GLY ARG ASN PHE TYR ALA VAL LEU ALA GLY
SEQRES 28 A 616 GLU GLU LEU GLY ARG LYS ILE ASP THR ARG ASN ASN VAL
SEQRES 29 A 616 PRO ASP ALA GLY LYS ASN SER VAL ARG ARG MET ALA GLU
SEQRES 30 A 616 ASP GLY ALA VAL LYS ARG ALA LEU VAL LEU PHE GLN ASN
SEQRES 31 A 616 SER GLN SER ALA GLY ASP ALA LYS MET ARG ARG GLN ALA
SEQRES 32 A 616 GLN ALA GLU TRP ARG PHE ALA THR ARG GLY PHE ASP GLU
SEQRES 33 A 616 ASP LYS LEU LEU THR ALA ALA GLN THR ALA PHE ASP HIS
SEQRES 34 A 616 GLY PHE TYR ASP MET ALA VAL ASN SER ALA GLU ARG THR
SEQRES 35 A 616 ASP ARG LYS LEU ASN TYR THR LEU ARG TYR ILE SER PRO
SEQRES 36 A 616 PHE LYS ASP THR VAL ILE ARG HIS ALA GLN ASN VAL ASN
SEQRES 37 A 616 VAL ASP PRO ALA TRP VAL TYR GLY LEU ILE ARG GLN GLU
SEQRES 38 A 616 SER ARG PHE VAL ILE GLY ALA GLN SER ARG VAL GLY ALA
SEQRES 39 A 616 GLN GLY LEU MET GLN VAL MET PRO ALA THR ALA ARG GLU
SEQRES 40 A 616 ILE ALA GLY LYS ILE GLY MET ASP ALA ALA GLN LEU TYR
SEQRES 41 A 616 THR ALA ASP GLY ASN ILE ARG MET GLY THR TRP TYR MET
SEQRES 42 A 616 ALA ASP THR LYS ARG ARG LEU GLN ASN ASN GLU VAL LEU
SEQRES 43 A 616 ALA THR ALA GLY TYR ASN ALA GLY PRO GLY ARG ALA ARG
SEQRES 44 A 616 ARG TRP GLN ALA ASP THR PRO LEU GLU GLY ALA VAL TYR
SEQRES 45 A 616 ALA GLU THR ILE PRO PHE SER GLU THR ARG ASP TYR VAL
SEQRES 46 A 616 LYS LYS VAL MET ALA ASN ALA ALA TYR TYR ALA ALA LEU
SEQRES 47 A 616 PHE GLY ALA PRO HIS ILE PRO LEU LYS GLN ARG MET GLY
SEQRES 48 A 616 ILE VAL PRO ALA ARG
FORMUL 2 HOH *271(H2 O)
HELIX 1 AA1 PRO A 53 LYS A 74 1 22
HELIX 2 AA2 ASN A 75 ASN A 85 1 11
HELIX 3 AA3 SER A 89 ARG A 106 1 18
HELIX 4 AA4 GLN A 108 ALA A 117 1 10
HELIX 5 AA5 LYS A 118 LEU A 119 5 2
HELIX 6 AA6 GLU A 120 ARG A 124 5 5
HELIX 7 AA7 ALA A 125 ARG A 136 1 12
HELIX 8 AA8 ARG A 141 VAL A 146 1 6
HELIX 9 AA9 PRO A 153 SER A 166 1 14
HELIX 10 AB1 ASP A 170 GLY A 184 1 15
HELIX 11 AB2 GLN A 186 LEU A 197 1 12
HELIX 12 AB3 THR A 205 LEU A 213 1 9
HELIX 13 AB4 LEU A 213 GLY A 218 1 6
HELIX 14 AB5 GLU A 220 SER A 224 5 5
HELIX 15 AB6 ASN A 226 GLU A 235 1 10
HELIX 16 AB7 SER A 236 LEU A 238 5 3
HELIX 17 AB8 SER A 239 ASN A 257 1 19
HELIX 18 AB9 ASN A 259 LYS A 269 1 11
HELIX 19 AC1 ASP A 272 LEU A 276 5 5
HELIX 20 AC2 THR A 277 ALA A 291 1 15
HELIX 21 AC3 ARG A 293 HIS A 303 1 11
HELIX 22 AC4 PRO A 305 LYS A 310 1 6
HELIX 23 AC5 SER A 311 THR A 325 1 15
HELIX 24 AC6 ASN A 327 ALA A 340 1 14
HELIX 25 AC7 ASN A 344 LEU A 354 1 11
HELIX 26 AC8 GLY A 368 ALA A 376 1 9
HELIX 27 AC9 ASP A 378 SER A 393 1 16
HELIX 28 AD1 ASP A 396 THR A 411 1 16
HELIX 29 AD2 ASP A 415 HIS A 429 1 15
HELIX 30 AD3 PHE A 431 GLU A 440 1 10
HELIX 31 AD4 ASN A 447 TYR A 452 1 6
HELIX 32 AD5 PHE A 456 VAL A 467 1 12
HELIX 33 AD6 ASP A 470 SER A 482 1 13
HELIX 34 AD7 ASP A 515 TYR A 520 5 6
HELIX 35 AD8 THR A 521 LEU A 540 1 20
HELIX 36 AD9 ASN A 543 GLY A 554 1 12
HELIX 37 AE1 GLY A 554 TRP A 561 1 8
HELIX 38 AE2 GLY A 569 THR A 575 1 7
HELIX 39 AE3 PHE A 578 PHE A 599 1 22
HELIX 40 AE4 PRO A 605 GLY A 611 1 7
SHEET 1 AA1 2 LEU A 567 GLU A 568 0
SHEET 2 AA1 2 ILE A 612 VAL A 613 -1 O VAL A 613 N LEU A 567
SSBOND 1 CYS A 130 CYS A 156 1555 1555 2.12
CRYST1 66.822 72.256 122.313 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 0.014965 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013840 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
