HEADER HYDROLASE INHIBITOR 06-MAR-17 5NCS
TITLE STRUCTURE OF THE NATIVE SERPIN-TYPE PROTEINASE INHIBITOR, MIROPIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERPIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: THE AMINO-TERMINAL AMINO ACID RESIDUES (GPLGS) ARE
COMPND 6 COMING FROM THE CLONING STRATEGY.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TANNERELLA FORSYTHIA;
SOURCE 3 ORGANISM_TAXID: 203275;
SOURCE 4 STRAIN: ATCC 43037 / JCM 10827 / FDC 338;
SOURCE 5 GENE: BFO_3114;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3)
KEYWDS SERPIN-TYPE PROTEINASE INHIBITOR, HYDROLASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR T.GOULAS,M.KSIAZEK,I.GARCIA-FERRER,D.MIZGALSKA,J.POTEMPA,X.GOMIS-RUTH
REVDAT 5 17-JAN-24 5NCS 1 REMARK
REVDAT 4 06-SEP-17 5NCS 1 REMARK
REVDAT 3 16-AUG-17 5NCS 1 REMARK
REVDAT 2 12-JUL-17 5NCS 1
REVDAT 1 24-MAY-17 5NCS 0
JRNL AUTH T.GOULAS,M.KSIAZEK,I.GARCIA-FERRER,A.M.SOCHAJ-GREGORCZYK,
JRNL AUTH 2 I.WALIGORSKA,M.WASYLEWSKI,J.POTEMPA,F.X.GOMIS-RUTH
JRNL TITL A STRUCTURE-DERIVED SNAP-TRAP MECHANISM OF A MULTISPECIFIC
JRNL TITL 2 SERPIN FROM THE DYSBIOTIC HUMAN ORAL MICROBIOME.
JRNL REF J. BIOL. CHEM. V. 292 10883 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28512127
JRNL DOI 10.1074/JBC.M117.786533
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 23135
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.180
REMARK 3 FREE R VALUE TEST SET COUNT : 735
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 3.1300 - 3.0000 1.00 2760 0 0.2358 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 : NULL
REMARK 3 B_SOL : NULL
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) : 58.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.09160
REMARK 3 B22 (A**2) : -10.09160
REMARK 3 B33 (A**2) : 20.18320
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 : 0.009 6011
REMARK 3 ANGLE : 1.190 8137
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL 855
REMARK 3 DIHEDRAL : NULL 2109
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|-4 - -1 A|39 - 408}
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0861 58.2895 137.2100
REMARK 3 T TENSOR
REMARK 3 T11: -0.3081 T22: 0.3182
REMARK 3 T33: -0.0721 T12: 0.0512
REMARK 3 T13: -0.0459 T23: 0.1334
REMARK 3 L TENSOR
REMARK 3 L11: 1.4026 L22: 1.0993
REMARK 3 L33: 1.9227 L12: 0.5772
REMARK 3 L13: -0.1861 L23: -0.5386
REMARK 3 S TENSOR
REMARK 3 S11: -0.0210 S12: 0.2185 S13: 0.0120
REMARK 3 S21: 0.0315 S22: 0.0257 S23: 0.0211
REMARK 3 S31: -0.0441 S32: -0.1093 S33: -0.0048
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {B|-4 - -1 B|39 - 408}
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7452 65.1578 182.6140
REMARK 3 T TENSOR
REMARK 3 T11: -0.2295 T22: -0.1565
REMARK 3 T33: -0.1719 T12: -0.0595
REMARK 3 T13: -0.0943 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 2.5950 L22: 0.7122
REMARK 3 L33: 8.8229 L12: 0.0288
REMARK 3 L13: 3.4486 L23: 0.3953
REMARK 3 S TENSOR
REMARK 3 S11: 0.0512 S12: -0.1670 S13: 0.3061
REMARK 3 S21: 0.2043 S22: -0.0703 S23: 0.0439
REMARK 3 S31: -0.0629 S32: -1.0725 S33: 0.0192
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 5NCS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200003872.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-15
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23150
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 21.50
REMARK 200 R MERGE (I) : 0.17200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 22.40
REMARK 200 R MERGE FOR SHELL (I) : 1.29500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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: 2ZV6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M DISODIUM MALONATE, PH 7.0, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 175.85500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.24500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.92750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.24500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.24500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 263.78250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.24500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.24500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.92750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.24500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.24500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 263.78250
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 175.85500
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 GLY A -5
REMARK 465 GLY B -5
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 ASN A 255 31.62 -98.52
REMARK 500 PHE A 330 64.66 -119.78
REMARK 500 SER A 373 -68.44 70.63
REMARK 500 LEU B -3 -74.66 -54.01
REMARK 500 PHE B 192 -62.89 -106.57
REMARK 500 ASN B 255 36.37 -91.39
REMARK 500 GLN B 277 50.76 -98.08
REMARK 500 PHE B 330 64.86 -119.04
REMARK 500 ILE B 333 -73.05 -81.87
REMARK 500 THR B 369 -44.91 -148.71
REMARK 500 SER B 371 59.45 -170.44
REMARK 500 SER B 373 -66.63 68.61
REMARK 500 PRO B 376 131.05 -39.58
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5NCS A 39 408 UNP G8UQY8 G8UQY8_TANFA 63 432
DBREF 5NCS B 39 408 UNP G8UQY8 G8UQY8_TANFA 63 432
SEQADV 5NCS GLY A -5 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS PRO A -4 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS LEU A -3 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS GLY A -2 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS SER A -1 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS GLN A 174 UNP G8UQY8 ARG 198 CONFLICT
SEQADV 5NCS GLY B -5 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS PRO B -4 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS LEU B -3 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS GLY B -2 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS SER B -1 UNP G8UQY8 EXPRESSION TAG
SEQADV 5NCS GLN B 174 UNP G8UQY8 ARG 198 CONFLICT
SEQRES 1 A 375 GLY PRO LEU GLY SER GLU LYS ILE GLU LYS ASP ASN ALA
SEQRES 2 A 375 PHE ALA PHE ASP LEU LEU GLN THR THR ARG LYS HIS VAL
SEQRES 3 A 375 THR GLU ALA ASN VAL PHE ILE SER PRO LEU SER VAL SER
SEQRES 4 A 375 MET ALA LEU ASN MET THR LEU ASN GLY ALA ALA GLY VAL
SEQRES 5 A 375 THR ALA ASP GLU MET LYS THR ALA LEU ARG GLU THR GLY
SEQRES 6 A 375 TYR THR MET GLU ASP ILE ASN GLU TYR SER HIS SER LEU
SEQRES 7 A 375 ARG GLU ALA LEU LEU LYS VAL ASP PRO SER THR THR ILE
SEQRES 8 A 375 GLY MET ALA ASN SER ILE TRP TYR LYS GLN GLY GLU LEU
SEQRES 9 A 375 VAL LYS GLU PRO PHE ILE LEU ALA ASN ARG THR HIS TYR
SEQRES 10 A 375 ASP ALA GLU VAL LYS ALA VAL ASP PHE SER SER PRO ALA
SEQRES 11 A 375 THR LEU PRO ALA ILE ASN GLY TRP CYS ALA GLN LYS THR
SEQRES 12 A 375 ASN ASP LYS ILE THR LYS ILE LEU ASP TYR ILE PRO GLY
SEQRES 13 A 375 ASN ALA PHE MET TYR LEU ILE ASN ALA VAL TYR PHE LYS
SEQRES 14 A 375 GLY ILE TRP VAL THR GLN PHE LYS LYS SER ASP THR LYS
SEQRES 15 A 375 ARG ALA PRO PHE ARG LYS ALA ASP GLY THR THR GLN GLU
SEQRES 16 A 375 VAL ASN MET MET ALA GLN LYS SER THR PHE GLY TYR THR
SEQRES 17 A 375 THR ASP GLU CYS CYS GLN TYR LEU GLU MET ASP TYR GLY
SEQRES 18 A 375 ASN LYS ALA PHE SER MET ILE VAL MET LEU PRO ASN GLU
SEQRES 19 A 375 GLY GLN THR THR ARG ASP VAL ILE GLU GLN LEU ASP ASN
SEQRES 20 A 375 LYS HIS TRP SER MET ILE ILE LYS GLY ILE ARG PRO THR
SEQRES 21 A 375 GLN VAL SER LEU ARG MET PRO ARG PHE LYS THR GLU CYS
SEQRES 22 A 375 LYS TYR GLY LEU GLU LYS LYS ILE LEU PRO GLU MET GLY
SEQRES 23 A 375 MET ASN VAL PRO PHE THR GLU THR ALA ASP PHE PRO GLY
SEQRES 24 A 375 ILE THR ASP ALA ALA ILE PHE ILE SER ARG VAL ILE HIS
SEQRES 25 A 375 LYS THR PHE VAL GLN VAL ASP GLU GLU GLY THR GLU ALA
SEQRES 26 A 375 ALA ALA VAL THR ALA VAL GLU MET VAL LYS THR SER SER
SEQRES 27 A 375 PRO SER THR THR PRO ILE ASN PHE HIS ILE ASN LYS PRO
SEQRES 28 A 375 PHE VAL PHE ALA ILE ARG GLU LYS SER THR GLY VAL ILE
SEQRES 29 A 375 LEU PHE ILE GLY GLU ILE GLY GLU VAL LYS GLU
SEQRES 1 B 375 GLY PRO LEU GLY SER GLU LYS ILE GLU LYS ASP ASN ALA
SEQRES 2 B 375 PHE ALA PHE ASP LEU LEU GLN THR THR ARG LYS HIS VAL
SEQRES 3 B 375 THR GLU ALA ASN VAL PHE ILE SER PRO LEU SER VAL SER
SEQRES 4 B 375 MET ALA LEU ASN MET THR LEU ASN GLY ALA ALA GLY VAL
SEQRES 5 B 375 THR ALA ASP GLU MET LYS THR ALA LEU ARG GLU THR GLY
SEQRES 6 B 375 TYR THR MET GLU ASP ILE ASN GLU TYR SER HIS SER LEU
SEQRES 7 B 375 ARG GLU ALA LEU LEU LYS VAL ASP PRO SER THR THR ILE
SEQRES 8 B 375 GLY MET ALA ASN SER ILE TRP TYR LYS GLN GLY GLU LEU
SEQRES 9 B 375 VAL LYS GLU PRO PHE ILE LEU ALA ASN ARG THR HIS TYR
SEQRES 10 B 375 ASP ALA GLU VAL LYS ALA VAL ASP PHE SER SER PRO ALA
SEQRES 11 B 375 THR LEU PRO ALA ILE ASN GLY TRP CYS ALA GLN LYS THR
SEQRES 12 B 375 ASN ASP LYS ILE THR LYS ILE LEU ASP TYR ILE PRO GLY
SEQRES 13 B 375 ASN ALA PHE MET TYR LEU ILE ASN ALA VAL TYR PHE LYS
SEQRES 14 B 375 GLY ILE TRP VAL THR GLN PHE LYS LYS SER ASP THR LYS
SEQRES 15 B 375 ARG ALA PRO PHE ARG LYS ALA ASP GLY THR THR GLN GLU
SEQRES 16 B 375 VAL ASN MET MET ALA GLN LYS SER THR PHE GLY TYR THR
SEQRES 17 B 375 THR ASP GLU CYS CYS GLN TYR LEU GLU MET ASP TYR GLY
SEQRES 18 B 375 ASN LYS ALA PHE SER MET ILE VAL MET LEU PRO ASN GLU
SEQRES 19 B 375 GLY GLN THR THR ARG ASP VAL ILE GLU GLN LEU ASP ASN
SEQRES 20 B 375 LYS HIS TRP SER MET ILE ILE LYS GLY ILE ARG PRO THR
SEQRES 21 B 375 GLN VAL SER LEU ARG MET PRO ARG PHE LYS THR GLU CYS
SEQRES 22 B 375 LYS TYR GLY LEU GLU LYS LYS ILE LEU PRO GLU MET GLY
SEQRES 23 B 375 MET ASN VAL PRO PHE THR GLU THR ALA ASP PHE PRO GLY
SEQRES 24 B 375 ILE THR ASP ALA ALA ILE PHE ILE SER ARG VAL ILE HIS
SEQRES 25 B 375 LYS THR PHE VAL GLN VAL ASP GLU GLU GLY THR GLU ALA
SEQRES 26 B 375 ALA ALA VAL THR ALA VAL GLU MET VAL LYS THR SER SER
SEQRES 27 B 375 PRO SER THR THR PRO ILE ASN PHE HIS ILE ASN LYS PRO
SEQRES 28 B 375 PHE VAL PHE ALA ILE ARG GLU LYS SER THR GLY VAL ILE
SEQRES 29 B 375 LEU PHE ILE GLY GLU ILE GLY GLU VAL LYS GLU
FORMUL 3 HOH *16(H2 O)
HELIX 1 AA1 SER A -1 HIS A 58 1 21
HELIX 2 AA2 SER A 67 ASN A 80 1 14
HELIX 3 AA3 ALA A 83 LEU A 94 1 12
HELIX 4 AA4 THR A 100 ASP A 119 1 20
HELIX 5 AA5 LYS A 139 ASP A 151 1 13
HELIX 6 AA6 ALA A 163 THR A 176 1 14
HELIX 7 AA7 LYS A 210 THR A 214 5 5
HELIX 8 AA8 THR A 270 LEU A 278 1 9
HELIX 9 AA9 ASP A 279 LYS A 288 1 10
HELIX 10 AB1 LYS A 313 GLY A 319 1 7
HELIX 11 AB2 ASN A 321 THR A 325 5 5
HELIX 12 AB3 THR A 362 LYS A 368 1 7
HELIX 13 AB4 SER B -1 HIS B 58 1 21
HELIX 14 AB5 SER B 67 ASN B 80 1 14
HELIX 15 AB6 ALA B 83 LEU B 94 1 12
HELIX 16 AB7 THR B 100 ASP B 119 1 20
HELIX 17 AB8 LYS B 139 TYR B 150 1 12
HELIX 18 AB9 ALA B 163 THR B 176 1 14
HELIX 19 AC1 LYS B 210 THR B 214 5 5
HELIX 20 AC2 THR B 270 GLN B 277 1 8
HELIX 21 AC3 ASP B 279 LYS B 288 1 10
HELIX 22 AC4 LYS B 313 GLY B 319 1 7
HELIX 23 AC5 ASN B 321 THR B 325 5 5
HELIX 24 AC6 THR B 362 LYS B 368 1 7
SHEET 1 AA1 7 VAL A 64 ILE A 66 0
SHEET 2 AA1 7 ILE A 397 ILE A 403 -1 O GLU A 402 N VAL A 64
SHEET 3 AA1 7 PHE A 385 GLU A 391 -1 N PHE A 387 O GLY A 401
SHEET 4 AA1 7 PHE A 258 PRO A 265 -1 N MET A 263 O VAL A 386
SHEET 5 AA1 7 CYS A 246 ASP A 252 -1 N GLN A 247 O LEU A 264
SHEET 6 AA1 7 THR A 226 THR A 242 -1 N THR A 241 O TYR A 248
SHEET 7 AA1 7 LYS A 215 ARG A 220 -1 N ALA A 217 O VAL A 229
SHEET 1 AA2 8 VAL A 64 ILE A 66 0
SHEET 2 AA2 8 ILE A 397 ILE A 403 -1 O GLU A 402 N VAL A 64
SHEET 3 AA2 8 PHE A 385 GLU A 391 -1 N PHE A 387 O GLY A 401
SHEET 4 AA2 8 PHE A 258 PRO A 265 -1 N MET A 263 O VAL A 386
SHEET 5 AA2 8 CYS A 246 ASP A 252 -1 N GLN A 247 O LEU A 264
SHEET 6 AA2 8 THR A 226 THR A 242 -1 N THR A 241 O TYR A 248
SHEET 7 AA2 8 ARG A 291 PRO A 300 -1 O LEU A 297 N GLN A 234
SHEET 8 AA2 8 ILE A 377 HIS A 380 1 O ILE A 377 N SER A 296
SHEET 1 AA3 5 GLU A 153 VAL A 157 0
SHEET 2 AA3 5 THR A 123 LYS A 133 1 N ILE A 130 O LYS A 155
SHEET 3 AA3 5 MET A 193 LYS A 202 -1 O LYS A 202 N THR A 123
SHEET 4 AA3 5 ARG A 342 VAL A 351 1 O ILE A 344 N ASN A 197
SHEET 5 AA3 5 PHE A 302 GLY A 309 -1 N PHE A 302 O VAL A 351
SHEET 1 AA4 2 TRP A 205 THR A 207 0
SHEET 2 AA4 2 GLY A 355 GLU A 357 1 O THR A 356 N TRP A 205
SHEET 1 AA5 7 VAL B 64 ILE B 66 0
SHEET 2 AA5 7 ILE B 397 ILE B 403 -1 O ILE B 400 N ILE B 66
SHEET 3 AA5 7 PHE B 385 GLU B 391 -1 N PHE B 387 O GLY B 401
SHEET 4 AA5 7 PHE B 258 PRO B 265 -1 N MET B 263 O VAL B 386
SHEET 5 AA5 7 CYS B 246 TYR B 253 -1 N GLN B 247 O LEU B 264
SHEET 6 AA5 7 THR B 226 THR B 242 -1 N THR B 241 O TYR B 248
SHEET 7 AA5 7 LYS B 215 ARG B 220 -1 N ALA B 217 O VAL B 229
SHEET 1 AA6 8 VAL B 64 ILE B 66 0
SHEET 2 AA6 8 ILE B 397 ILE B 403 -1 O ILE B 400 N ILE B 66
SHEET 3 AA6 8 PHE B 385 GLU B 391 -1 N PHE B 387 O GLY B 401
SHEET 4 AA6 8 PHE B 258 PRO B 265 -1 N MET B 263 O VAL B 386
SHEET 5 AA6 8 CYS B 246 TYR B 253 -1 N GLN B 247 O LEU B 264
SHEET 6 AA6 8 THR B 226 THR B 242 -1 N THR B 241 O TYR B 248
SHEET 7 AA6 8 ARG B 291 PRO B 300 -1 O VAL B 295 N SER B 236
SHEET 8 AA6 8 ILE B 377 HIS B 380 1 O ILE B 377 N SER B 296
SHEET 1 AA7 5 GLU B 153 VAL B 157 0
SHEET 2 AA7 5 THR B 123 LYS B 133 1 N ILE B 130 O LYS B 155
SHEET 3 AA7 5 MET B 193 LYS B 202 -1 O LYS B 202 N THR B 123
SHEET 4 AA7 5 ARG B 342 VAL B 351 1 O ILE B 344 N ASN B 197
SHEET 5 AA7 5 PHE B 302 GLY B 309 -1 N PHE B 302 O VAL B 351
SHEET 1 AA8 2 TRP B 205 THR B 207 0
SHEET 2 AA8 2 GLY B 355 GLU B 357 1 O THR B 356 N TRP B 205
SSBOND 1 CYS A 245 CYS A 246 1555 1555 2.09
SSBOND 2 CYS B 245 CYS B 246 1555 1555 2.07
CRYST1 78.490 78.490 351.710 90.00 90.00 90.00 P 41 21 2 16
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 0.012740 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012740 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002843 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
