HEADER TRANSFERASE 27-SEP-09 3K1D
TITLE CRYSTAL STRUCTURE OF GLYCOGEN BRANCHING ENZYME SYNONYM: 1,4-ALPHA-D-
TITLE 2 GLUCAN:1,4-ALPHA-D-GLUCAN 6-GLUCOSYL-TRANSFERASE FROM MYCOBACTERIUM
TITLE 3 TUBERCULOSIS H37RV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,4-ALPHA-GLUCAN-BRANCHING ENZYME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 10-731;
COMPND 5 SYNONYM: GLYCOGEN-BRANCHING ENZYME, BE, 1,4-ALPHA-D-GLUCAN:1,4-ALPHA-
COMPND 6 D-GLUCAN 6-GLUCOSYL-TRANSFERASE;
COMPND 7 EC: 2.4.1.18;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: GLGB, RV1326C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET29A
KEYWDS MYCOBACTERIUM TUBERCULOSIS H37RV, MESOPHILIC HUMAN PATHOGEN, GLGB
KEYWDS 2 RV1326C GENE, GLYCOSYL TRANSFERASE, N-TERMINAL SANDWIC, GLYCOGEN
KEYWDS 3 BIOSYNTHESIS, GLYCOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.PAL,S.KUMAR,K.SWAMINATHAN
REVDAT 3 01-NOV-23 3K1D 1 REMARK
REVDAT 2 19-FEB-14 3K1D 1 JRNL VERSN
REVDAT 1 05-MAY-10 3K1D 0
JRNL AUTH K.PAL,S.KUMAR,S.SHARMA,S.K.GARG,M.S.ALAM,H.E.XU,P.AGRAWAL,
JRNL AUTH 2 K.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF FULL-LENGTH MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 H37RV GLYCOGEN BRANCHING ENZYME: INSIGHTS OF N-TERMINAL
JRNL TITL 3 BETA-SANDWICH IN SUBSTRATE SPECIFICITY AND ENZYMATIC
JRNL TITL 4 ACTIVITY
JRNL REF J.BIOL.CHEM. V. 285 20897 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20444687
JRNL DOI 10.1074/JBC.M110.121707
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.K.GARG,M.S.ALAM,K.V.KISHAN,P.AGRAWAL
REMARK 1 TITL EXPRESSION AND CHARACTERIZATION OF ALPHA-(1,4)-GLUCAN
REMARK 1 TITL 2 BRANCHING ENZYME RV1326C OF MYCOBACTERIUM TUBERCULOSIS H37RV
REMARK 1 REF PROTEIN EXPR.PURIF. V. 51 198 2007
REMARK 1 REFN ISSN 1046-5928
REMARK 1 PMID 17005418
REMARK 1 DOI 10.1016/J.PEP.2006.08.005
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1996027.230
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36160
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1800
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.48
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5627
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 298
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5724
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.07000
REMARK 3 B22 (A**2) : -2.58000
REMARK 3 B33 (A**2) : -5.49000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 37.02
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3K1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : C (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36272
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.330
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 14.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.17500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.76000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB CODE 1M7X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.50, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 54.68650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.43050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.68650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.43050
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 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 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 HIS A 11 38.90 -86.61
REMARK 500 ASP A 40 -53.49 70.50
REMARK 500 ASP A 41 -76.02 -157.02
REMARK 500 ARG A 49 85.36 -153.77
REMARK 500 VAL A 55 -73.69 -111.45
REMARK 500 VAL A 56 131.43 60.13
REMARK 500 PHE A 64 83.39 -38.85
REMARK 500 SER A 65 -114.52 -168.27
REMARK 500 LEU A 66 140.66 75.62
REMARK 500 HIS A 68 10.90 -175.84
REMARK 500 ASP A 70 -163.52 47.75
REMARK 500 SER A 71 49.78 -104.65
REMARK 500 ALA A 77 -124.23 63.93
REMARK 500 LEU A 78 137.09 58.80
REMARK 500 PRO A 79 -155.69 -50.56
REMARK 500 PHE A 80 148.19 55.42
REMARK 500 ASP A 82 -64.57 70.71
REMARK 500 LEU A 83 -71.02 65.22
REMARK 500 ILE A 84 92.29 60.84
REMARK 500 ASP A 85 145.80 63.70
REMARK 500 TYR A 86 -160.07 -168.49
REMARK 500 THR A 139 -139.36 -90.26
REMARK 500 ALA A 153 72.95 -164.79
REMARK 500 ASN A 169 17.82 -155.02
REMARK 500 LEU A 186 137.60 -175.84
REMARK 500 ASP A 233 19.60 -141.56
REMARK 500 ARG A 276 -62.99 -97.51
REMARK 500 PRO A 294 119.61 -31.23
REMARK 500 VAL A 343 69.71 -115.01
REMARK 500 ALA A 353 -113.92 -100.99
REMARK 500 ARG A 356 55.59 34.62
REMARK 500 PRO A 368 152.05 -41.78
REMARK 500 LYS A 369 -160.73 -69.79
REMARK 500 GLU A 372 -120.43 -69.56
REMARK 500 GLN A 373 -161.07 57.89
REMARK 500 LEU A 374 60.86 -102.43
REMARK 500 THR A 378 90.92 51.15
REMARK 500 ASP A 420 159.72 -30.99
REMARK 500 TYR A 421 149.65 168.40
REMARK 500 SER A 422 135.49 47.91
REMARK 500 VAL A 432 -105.78 -86.83
REMARK 500 HIS A 433 -86.17 57.33
REMARK 500 ASN A 598 40.28 -98.72
REMARK 500 TRP A 622 -9.45 -151.25
REMARK 500 ASP A 638 56.58 -116.92
REMARK 500 HIS A 692 32.30 79.00
REMARK 500 ASP A 706 48.64 -91.13
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3K1D A 10 731 UNP Q10625 GLGB_MYCTU 10 731
SEQRES 1 A 722 GLU HIS LEU ALA PRO GLU PRO ALA GLU MET ALA ARG LEU
SEQRES 2 A 722 VAL ALA GLY THR HIS HIS ASN PRO HIS GLY ILE LEU GLY
SEQRES 3 A 722 ALA HIS GLU TYR ASP ASP HIS THR VAL ILE ARG ALA PHE
SEQRES 4 A 722 ARG PRO HIS ALA VAL GLU VAL VAL ALA LEU VAL GLY LYS
SEQRES 5 A 722 ASP ARG PHE SER LEU GLN HIS LEU ASP SER GLY LEU PHE
SEQRES 6 A 722 ALA VAL ALA LEU PRO PHE VAL ASP LEU ILE ASP TYR ARG
SEQRES 7 A 722 LEU GLN VAL THR TYR GLU GLY CYS GLU PRO HIS THR VAL
SEQRES 8 A 722 ALA ASP ALA TYR ARG PHE LEU PRO THR LEU GLY GLU VAL
SEQRES 9 A 722 ASP LEU HIS LEU PHE ALA GLU GLY ARG HIS GLU ARG LEU
SEQRES 10 A 722 TRP GLU VAL LEU GLY ALA HIS PRO ARG SER PHE THR THR
SEQRES 11 A 722 ALA ASP GLY VAL VAL SER GLY VAL SER PHE ALA VAL TRP
SEQRES 12 A 722 ALA PRO ASN ALA LYS GLY VAL SER LEU ILE GLY GLU PHE
SEQRES 13 A 722 ASN GLY TRP ASN GLY HIS GLU ALA PRO MET ARG VAL LEU
SEQRES 14 A 722 GLY PRO SER GLY VAL TRP GLU LEU PHE TRP PRO ASP PHE
SEQRES 15 A 722 PRO CYS ASP GLY LEU TYR LYS PHE ARG VAL HIS GLY ALA
SEQRES 16 A 722 ASP GLY VAL VAL THR ASP ARG ALA ASP PRO PHE ALA PHE
SEQRES 17 A 722 GLY THR GLU VAL PRO PRO GLN THR ALA SER ARG VAL THR
SEQRES 18 A 722 SER SER ASP TYR THR TRP GLY ASP ASP ASP TRP MET ALA
SEQRES 19 A 722 GLY ARG ALA LEU ARG ASN PRO VAL ASN GLU ALA MET SER
SEQRES 20 A 722 THR TYR GLU VAL HIS LEU GLY SER TRP ARG PRO GLY LEU
SEQRES 21 A 722 SER TYR ARG GLN LEU ALA ARG GLU LEU THR ASP TYR ILE
SEQRES 22 A 722 VAL ASP GLN GLY PHE THR HIS VAL GLU LEU LEU PRO VAL
SEQRES 23 A 722 ALA GLU HIS PRO PHE ALA GLY SER TRP GLY TYR GLN VAL
SEQRES 24 A 722 THR SER TYR TYR ALA PRO THR SER ARG PHE GLY THR PRO
SEQRES 25 A 722 ASP ASP PHE ARG ALA LEU VAL ASP ALA LEU HIS GLN ALA
SEQRES 26 A 722 GLY ILE GLY VAL ILE VAL ASP TRP VAL PRO ALA HIS PHE
SEQRES 27 A 722 PRO LYS ASP ALA TRP ALA LEU GLY ARG PHE ASP GLY THR
SEQRES 28 A 722 PRO LEU TYR GLU HIS SER ASP PRO LYS ARG GLY GLU GLN
SEQRES 29 A 722 LEU ASP TRP GLY THR TYR VAL PHE ASP PHE GLY ARG PRO
SEQRES 30 A 722 GLU VAL ARG ASN PHE LEU VAL ALA ASN ALA LEU TYR TRP
SEQRES 31 A 722 LEU GLN GLU PHE HIS ILE ASP GLY LEU ARG VAL ASP ALA
SEQRES 32 A 722 VAL ALA SER MET LEU TYR LEU ASP TYR SER ARG PRO GLU
SEQRES 33 A 722 GLY GLY TRP THR PRO ASN VAL HIS GLY GLY ARG GLU ASN
SEQRES 34 A 722 LEU GLU ALA VAL GLN PHE LEU GLN GLU MET ASN ALA THR
SEQRES 35 A 722 ALA HIS LYS VAL ALA PRO GLY ILE VAL THR ILE ALA GLU
SEQRES 36 A 722 GLU SER THR PRO TRP SER GLY VAL THR ARG PRO THR ASN
SEQRES 37 A 722 ILE GLY GLY LEU GLY PHE SER MET LYS TRP ASN MET GLY
SEQRES 38 A 722 TRP MET HIS ASP THR LEU ASP TYR VAL SER ARG ASP PRO
SEQRES 39 A 722 VAL TYR ARG SER TYR HIS HIS HIS GLU MET THR PHE SER
SEQRES 40 A 722 MET LEU TYR ALA PHE SER GLU ASN TYR VAL LEU PRO LEU
SEQRES 41 A 722 SER HIS ASP GLU VAL VAL HIS GLY LYS GLY THR LEU TRP
SEQRES 42 A 722 GLY ARG MET PRO GLY ASN ASN HIS VAL LYS ALA ALA GLY
SEQRES 43 A 722 LEU ARG SER LEU LEU ALA TYR GLN TRP ALA HIS PRO GLY
SEQRES 44 A 722 LYS GLN LEU LEU PHE MET GLY GLN GLU PHE GLY GLN ARG
SEQRES 45 A 722 ALA GLU TRP SER GLU GLN ARG GLY LEU ASP TRP PHE GLN
SEQRES 46 A 722 LEU ASP GLU ASN GLY PHE SER ASN GLY ILE GLN ARG LEU
SEQRES 47 A 722 VAL ARG ASP ILE ASN ASP ILE TYR ARG CYS HIS PRO ALA
SEQRES 48 A 722 LEU TRP SER LEU ASP THR THR PRO GLU GLY TYR SER TRP
SEQRES 49 A 722 ILE ASP ALA ASN ASP SER ALA ASN ASN VAL LEU SER PHE
SEQRES 50 A 722 MET ARG TYR GLY SER ASP GLY SER VAL LEU ALA CYS VAL
SEQRES 51 A 722 PHE ASN PHE ALA GLY ALA GLU HIS ARG ASP TYR ARG LEU
SEQRES 52 A 722 GLY LEU PRO ARG ALA GLY ARG TRP ARG GLU VAL LEU ASN
SEQRES 53 A 722 THR ASP ALA THR ILE TYR HIS GLY SER GLY ILE GLY ASN
SEQRES 54 A 722 LEU GLY GLY VAL ASP ALA THR ASP ASP PRO TRP HIS GLY
SEQRES 55 A 722 ARG PRO ALA SER ALA VAL LEU VAL LEU PRO PRO THR SER
SEQRES 56 A 722 ALA LEU TRP LEU THR PRO ALA
FORMUL 2 HOH *323(H2 O)
HELIX 1 1 GLU A 15 GLY A 25 1 11
HELIX 2 2 ASN A 29 LEU A 34 1 6
HELIX 3 3 ASP A 102 PHE A 106 5 5
HELIX 4 4 GLY A 111 GLU A 120 1 10
HELIX 5 5 ARG A 125 VAL A 129 5 5
HELIX 6 6 PHE A 165 GLY A 167 5 3
HELIX 7 7 GLY A 179 SER A 181 5 3
HELIX 8 8 ASP A 238 ALA A 246 1 9
HELIX 9 9 LEU A 247 ARG A 248 5 2
HELIX 10 10 ASN A 249 GLU A 253 5 5
HELIX 11 11 SER A 270 GLY A 286 1 17
HELIX 12 12 PHE A 300 TRP A 304 5 5
HELIX 13 13 SER A 316 GLY A 319 5 4
HELIX 14 14 THR A 320 ALA A 334 1 15
HELIX 15 15 ARG A 385 PHE A 403 1 19
HELIX 16 16 VAL A 413 TYR A 418 1 6
HELIX 17 17 ASN A 438 ALA A 456 1 19
HELIX 18 18 PRO A 475 GLY A 479 5 5
HELIX 19 19 ASN A 488 ARG A 501 1 14
HELIX 20 20 ASP A 502 TYR A 508 5 7
HELIX 21 21 HIS A 509 PHE A 515 1 7
HELIX 22 22 SER A 516 TYR A 519 5 4
HELIX 23 23 SER A 530 VAL A 534 5 5
HELIX 24 24 THR A 540 MET A 545 1 6
HELIX 25 25 ASN A 548 HIS A 566 1 19
HELIX 26 26 GLY A 575 GLY A 579 5 5
HELIX 27 27 ASP A 591 GLU A 597 5 7
HELIX 28 28 PHE A 600 HIS A 618 1 19
HELIX 29 29 PRO A 619 TRP A 622 5 4
HELIX 30 30 THR A 627 GLU A 629 5 3
HELIX 31 31 ALA A 688 HIS A 692 5 5
SHEET 1 A 3 GLY A 35 GLU A 38 0
SHEET 2 A 3 THR A 43 PHE A 48 -1 O VAL A 44 N HIS A 37
SHEET 3 A 3 LEU A 73 ALA A 75 -1 O PHE A 74 N ALA A 47
SHEET 1 B 3 ALA A 57 LEU A 58 0
SHEET 2 B 3 ARG A 87 VAL A 90 -1 O ARG A 87 N LEU A 58
SHEET 3 B 3 HIS A 98 VAL A 100 -1 O VAL A 100 N LEU A 88
SHEET 1 C 4 GLY A 131 THR A 138 0
SHEET 2 C 4 VAL A 143 TRP A 152 -1 O VAL A 144 N PHE A 137
SHEET 3 C 4 VAL A 183 PRO A 189 -1 O TRP A 184 N VAL A 151
SHEET 4 C 4 ARG A 176 VAL A 177 -1 N ARG A 176 O GLU A 185
SHEET 1 D 3 GLY A 158 GLY A 163 0
SHEET 2 D 3 LEU A 196 HIS A 202 -1 O ARG A 200 N SER A 160
SHEET 3 D 3 VAL A 208 ARG A 211 -1 O THR A 209 N VAL A 201
SHEET 1 E 3 GLY A 158 GLY A 163 0
SHEET 2 E 3 LEU A 196 HIS A 202 -1 O ARG A 200 N SER A 160
SHEET 3 E 3 SER A 227 ARG A 228 -1 O SER A 227 N TYR A 197
SHEET 1 F 9 SER A 256 VAL A 260 0
SHEET 2 F 9 HIS A 289 LEU A 292 1 O GLU A 291 N VAL A 260
SHEET 3 F 9 GLY A 337 TRP A 342 1 O ILE A 339 N LEU A 292
SHEET 4 F 9 GLY A 407 VAL A 410 1 O ARG A 409 N TRP A 342
SHEET 5 F 9 VAL A 460 ALA A 463 1 O ILE A 462 N LEU A 408
SHEET 6 F 9 MET A 485 TRP A 487 1 O TRP A 487 N ALA A 463
SHEET 7 F 9 TYR A 525 LEU A 529 1 O VAL A 526 N LYS A 486
SHEET 8 F 9 LYS A 569 PHE A 573 1 O LYS A 569 N LEU A 527
SHEET 9 F 9 SER A 256 VAL A 260 1 N THR A 257 O LEU A 572
SHEET 1 G 2 ALA A 296 GLU A 297 0
SHEET 2 G 2 SER A 310 PRO A 314 -1 O ALA A 313 N GLU A 297
SHEET 1 H 8 TYR A 631 ASP A 638 0
SHEET 2 H 8 VAL A 643 TYR A 649 -1 O MET A 647 N SER A 632
SHEET 3 H 8 VAL A 655 ASN A 661 -1 O PHE A 660 N LEU A 644
SHEET 4 H 8 SER A 724 PRO A 730 -1 O LEU A 728 N ALA A 657
SHEET 5 H 8 GLY A 678 ASN A 685 -1 N ARG A 681 O THR A 729
SHEET 6 H 8 GLY A 701 THR A 705 -1 O ALA A 704 N GLY A 678
SHEET 7 H 8 ALA A 714 LEU A 720 -1 O SER A 715 N THR A 705
SHEET 8 H 8 HIS A 667 LEU A 674 -1 N LEU A 674 O ALA A 714
CISPEP 1 PRO A 222 PRO A 223 0 -0.88
CRYST1 109.373 156.861 48.021 90.00 90.00 90.00 P 21 21 2 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 0.009143 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006375 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020824 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
