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HEADER HYDROLASE 31-JAN-17 5UNO
TITLE CRYSTAL STRUCTURE OF HIP1 (RV2224C)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 50-520;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: N-TERMINAL 6XHIS TAG WITH LINKER AND THROMBIN
COMPND 8 RECOGNITION CLEAVAGE SITE.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: ATCC 25618 / H37RV;
SOURCE 5 ATCC: 25618;
SOURCE 6 GENE: CAEA, RV2224C, MTCY427.05C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS SERINE PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.NAFFIN-OLIVOS,A.DAAB,A.WHITE,N.GOLDFARB,A.C.MILNE,D.LIU,B.M.DUNN,
AUTHOR 2 J.RENGARAJAN,G.A.PETSKO,D.RINGE
REVDAT 1 12-APR-17 5UNO 0
JRNL AUTH J.L.NAFFIN-OLIVOS,A.DAAB,A.WHITE,N.E.GOLDFARB,A.C.MILNE,
JRNL AUTH 2 D.LIU,J.BAIKOVITZ,B.M.DUNN,J.RENGARAJAN,G.A.PETSKO,D.RINGE
JRNL TITL STRUCTURE DETERMINATION OF MYCOBACTERIUM TUBERCULOSIS SERINE
JRNL TITL 2 PROTEASE HIP1 (RV2224C).
JRNL REF BIOCHEMISTRY 2017
JRNL REFN ISSN 1520-4995
JRNL PMID 28346784
JRNL DOI 10.1021/ACS.BIOCHEM.6B01066
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 25248
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2002
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 33.0853 - 6.2604 1.00 1777 160 0.1847 0.2240
REMARK 3 2 6.2604 - 4.9745 1.00 1692 145 0.2050 0.2268
REMARK 3 3 4.9745 - 4.3473 1.00 1675 143 0.1828 0.2001
REMARK 3 4 4.3473 - 3.9505 1.00 1682 146 0.1948 0.2241
REMARK 3 5 3.9505 - 3.6677 1.00 1666 145 0.1953 0.2123
REMARK 3 6 3.6677 - 3.4517 1.00 1657 144 0.2197 0.2637
REMARK 3 7 3.4517 - 3.2790 1.00 1650 137 0.2333 0.2888
REMARK 3 8 3.2790 - 3.1364 1.00 1651 140 0.2333 0.2943
REMARK 3 9 3.1364 - 3.0157 1.00 1641 141 0.2275 0.2668
REMARK 3 10 3.0157 - 2.9117 1.00 1643 143 0.2419 0.3105
REMARK 3 11 2.9117 - 2.8207 1.00 1654 141 0.2272 0.2779
REMARK 3 12 2.8207 - 2.7402 1.00 1629 138 0.2202 0.2816
REMARK 3 13 2.7402 - 2.6681 1.00 1633 140 0.2458 0.2707
REMARK 3 14 2.6681 - 2.6030 0.97 1596 139 0.2708 0.3263
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.58
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 : 0.009 3587
REMARK 3 ANGLE : 1.100 4883
REMARK 3 CHIRALITY : 0.046 537
REMARK 3 PLANARITY : 0.006 659
REMARK 3 DIHEDRAL : 13.871 1314
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 5UNO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000212315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25285
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 33.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 15.10
REMARK 200 R MERGE (I) : 0.17900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.90900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (W/V) PEG3350, 0.1 M NAACETATE PH
REMARK 280 5.6, 0.2 M (NH4)2SO4, 10% (V/V) GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.74600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 85.49200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 85.49200
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.74600
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 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 29
REMARK 465 GLY A 30
REMARK 465 SER A 31
REMARK 465 SER A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 HIS A 37
REMARK 465 HIS A 38
REMARK 465 SER A 39
REMARK 465 SER A 40
REMARK 465 GLY A 41
REMARK 465 LEU A 42
REMARK 465 VAL A 43
REMARK 465 PRO A 44
REMARK 465 ARG A 45
REMARK 465 GLY A 46
REMARK 465 SER A 47
REMARK 465 HIS A 48
REMARK 465 MET A 49
REMARK 465 SER A 57
REMARK 465 SER A 58
REMARK 465 ASN A 59
REMARK 465 PRO A 60
REMARK 465 GLN A 61
REMARK 465 VAL A 62
REMARK 465 LYS A 63
REMARK 465 ILE A 64
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 51 CG CD OE1 OE2
REMARK 480 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 128 CG CD CE NZ
REMARK 480 ARG A 321 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 323 CD CE NZ
REMARK 480 LYS A 423 CG CD CE NZ
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 PRO A 82 45.96 -69.40
REMARK 500 ASP A 83 4.57 -160.55
REMARK 500 ALA A 145 -112.19 57.46
REMARK 500 CYS A 153 -53.41 -128.37
REMARK 500 SER A 228 -114.43 57.42
REMARK 500 ARG A 318 74.70 -114.46
REMARK 500 THR A 488 76.24 -112.93
REMARK 500 THR A 491 164.42 77.44
REMARK 500 VAL A 492 -20.74 -159.64
REMARK 500 ILE A 509 -61.96 -91.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UOH RELATED DB: PDB
DBREF 5UNO A 50 520 UNP P9WHR3 CAEA_MYCTU 50 520
SEQADV 5UNO MET A 29 UNP P9WHR3 INITIATING METHIONINE
SEQADV 5UNO GLY A 30 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO SER A 31 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO SER A 32 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO HIS A 33 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO HIS A 34 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO HIS A 35 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO HIS A 36 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO HIS A 37 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO HIS A 38 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO SER A 39 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO SER A 40 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO GLY A 41 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO LEU A 42 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO VAL A 43 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO PRO A 44 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO ARG A 45 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO GLY A 46 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO SER A 47 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO HIS A 48 UNP P9WHR3 EXPRESSION TAG
SEQADV 5UNO MET A 49 UNP P9WHR3 EXPRESSION TAG
SEQRES 1 A 492 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 492 LEU VAL PRO ARG GLY SER HIS MET VAL GLU TRP THR PRO
SEQRES 3 A 492 CYS ARG SER SER ASN PRO GLN VAL LYS ILE PRO GLY GLY
SEQRES 4 A 492 ALA LEU CYS GLY LYS LEU ALA VAL PRO VAL ASP TYR ASP
SEQRES 5 A 492 ARG PRO ASP GLY ASP VAL ALA ALA LEU ALA LEU ILE ARG
SEQRES 6 A 492 PHE PRO ALA THR GLY ASP LYS ILE GLY SER LEU VAL ILE
SEQRES 7 A 492 ASN PRO GLY GLY PRO GLY GLU SER GLY ILE GLU ALA ALA
SEQRES 8 A 492 LEU GLY VAL PHE GLN THR LEU PRO LYS ARG VAL HIS GLU
SEQRES 9 A 492 ARG PHE ASP LEU VAL GLY PHE ASP PRO ARG GLY VAL ALA
SEQRES 10 A 492 SER SER ARG PRO ALA ILE TRP CYS ASN SER ASP ALA ASP
SEQRES 11 A 492 ASN ASP ARG LEU ARG ALA GLU PRO GLN VAL ASP TYR SER
SEQRES 12 A 492 ARG GLU GLY VAL ALA HIS ILE GLU ASN GLU THR LYS GLN
SEQRES 13 A 492 PHE VAL GLY ARG CYS VAL ASP LYS MET GLY LYS ASN PHE
SEQRES 14 A 492 LEU ALA HIS VAL GLY THR VAL ASN VAL ALA LYS ASP LEU
SEQRES 15 A 492 ASP ALA ILE ARG ALA ALA LEU GLY ASP ASP LYS LEU THR
SEQRES 16 A 492 TYR LEU GLY TYR SER TYR GLY THR ARG ILE GLY SER ALA
SEQRES 17 A 492 TYR ALA GLU GLU PHE PRO GLN ARG VAL ARG ALA MET ILE
SEQRES 18 A 492 LEU ASP GLY ALA VAL ASP PRO ASN ALA ASP PRO ILE GLU
SEQRES 19 A 492 ALA GLU LEU ARG GLN ALA LYS GLY PHE GLN ASP ALA PHE
SEQRES 20 A 492 ASN ASN TYR ALA ALA ASP CYS ALA LYS ASN ALA GLY CYS
SEQRES 21 A 492 PRO LEU GLY ALA ASP PRO ALA LYS ALA VAL GLU VAL TYR
SEQRES 22 A 492 HIS SER LEU VAL ASP PRO LEU VAL ASP PRO ASP ASN PRO
SEQRES 23 A 492 ARG ILE SER ARG PRO ALA ARG THR LYS ASP PRO ARG GLY
SEQRES 24 A 492 LEU SER TYR SER ASP ALA ILE VAL GLY THR ILE MET ALA
SEQRES 25 A 492 LEU TYR SER PRO ASN LEU TRP GLN HIS LEU THR ASP GLY
SEQRES 26 A 492 LEU SER GLU LEU VAL ASP ASN ARG GLY ASP THR LEU LEU
SEQRES 27 A 492 ALA LEU ALA ASP MET TYR MET ARG ARG ASP SER HIS GLY
SEQRES 28 A 492 ARG TYR ASN ASN SER GLY ASP ALA ARG VAL ALA ILE ASN
SEQRES 29 A 492 CYS VAL ASP GLN PRO PRO VAL THR ASP ARG ASP LYS VAL
SEQRES 30 A 492 ILE ASP GLU ASP ARG ARG ALA ARG GLU ILE ALA PRO PHE
SEQRES 31 A 492 MET SER TYR GLY LYS PHE THR GLY ASP ALA PRO LEU GLY
SEQRES 32 A 492 THR CYS ALA PHE TRP PRO VAL PRO PRO THR SER GLN PRO
SEQRES 33 A 492 HIS ALA VAL SER ALA PRO GLY LEU VAL PRO THR VAL VAL
SEQRES 34 A 492 VAL SER THR THR HIS ASP PRO ALA THR PRO TYR LYS ALA
SEQRES 35 A 492 GLY VAL ASP LEU ALA ASN GLN LEU ARG GLY SER LEU LEU
SEQRES 36 A 492 THR PHE ASP GLY THR GLN HIS THR VAL VAL PHE GLN GLY
SEQRES 37 A 492 ASP SER CYS ILE ASP GLU TYR VAL THR ALA TYR LEU ILE
SEQRES 38 A 492 GLY GLY THR THR PRO PRO SER GLY ALA LYS CYS
HELIX 1 AA1 SER A 114 LEU A 126 1 13
HELIX 2 AA2 PRO A 127 ARG A 133 1 7
HELIX 3 AA3 SER A 155 GLU A 165 1 11
HELIX 4 AA4 SER A 171 ALA A 199 1 29
HELIX 5 AA5 GLY A 202 LEU A 217 1 16
HELIX 6 AA6 TYR A 229 PHE A 241 1 13
HELIX 7 AA7 ASP A 259 ALA A 283 1 25
HELIX 8 AA8 ASP A 293 ALA A 295 5 3
HELIX 9 AA9 LYS A 296 ASP A 306 1 11
HELIX 10 AB1 PRO A 307 VAL A 309 5 3
HELIX 11 AB2 SER A 329 LEU A 341 1 13
HELIX 12 AB3 TYR A 342 ASN A 345 5 4
HELIX 13 AB4 LEU A 346 ASP A 359 1 14
HELIX 14 AB5 GLY A 362 ARG A 374 1 13
HELIX 15 AB6 ASN A 383 GLN A 396 1 14
HELIX 16 AB7 ASP A 401 ALA A 416 1 16
HELIX 17 AB8 PRO A 417 SER A 420 5 4
HELIX 18 AB9 GLY A 431 TRP A 436 5 6
HELIX 19 AC1 PRO A 467 ARG A 479 1 13
HELIX 20 AC2 ASP A 497 GLY A 510 1 14
SHEET 1 AA110 THR A 53 PRO A 54 0
SHEET 2 AA110 LEU A 69 PRO A 76 -1 O CYS A 70 N THR A 53
SHEET 3 AA110 VAL A 86 PHE A 94 -1 O ALA A 87 N VAL A 75
SHEET 4 AA110 PHE A 134 ASP A 140 -1 O LEU A 136 N PHE A 94
SHEET 5 AA110 GLY A 102 ASN A 107 1 N LEU A 104 O ASP A 135
SHEET 6 AA110 LEU A 222 TYR A 227 1 O TYR A 227 N ASN A 107
SHEET 7 AA110 VAL A 245 ASP A 251 1 O ILE A 249 N TYR A 224
SHEET 8 AA110 VAL A 456 THR A 460 1 O VAL A 458 N LEU A 250
SHEET 9 AA110 SER A 481 PHE A 485 1 O SER A 481 N VAL A 457
SHEET 10 AA110 LYS A 519 CYS A 520 1 O CYS A 520 N THR A 484
SSBOND 1 CYS A 55 CYS A 70 1555 1555 2.04
SSBOND 2 CYS A 153 CYS A 189 1555 1555 2.04
SSBOND 3 CYS A 282 CYS A 288 1555 1555 2.07
SSBOND 4 CYS A 393 CYS A 433 1555 1555 2.03
SSBOND 5 CYS A 499 CYS A 520 1555 1555 2.05
CISPEP 1 GLY A 110 PRO A 111 0 -0.63
CISPEP 2 ARG A 148 PRO A 149 0 -4.34
CRYST1 104.483 104.483 128.238 90.00 90.00 120.00 P 31 2 1 6
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 0.009571 0.005526 0.000000 0.00000
SCALE2 0.000000 0.011052 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007798 0.00000
TER 3502 CYS A 520
MASTER 290 0 0 20 10 0 0 6 3501 1 10 38
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