HEADER HEME-BINDING PROTEIN 18-JUL-11 3SZ6
TITLE ISDX1, AN ANTHRAX HEMOPHORE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 26-146;
COMPND 5 SYNONYM: IRON TRANSPORT-ASSOCIATED DOMAIN PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 1392;
SOURCE 5 GENE: BAS4443, BA_4788, GBAA_4788;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IG FOLD, HEMOPHORE, HEME-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.B.POOR,A.W.MARESSO,F.MURPHY,C.HE
REVDAT 2 28-FEB-24 3SZ6 1 REMARK
REVDAT 1 28-MAR-12 3SZ6 0
JRNL AUTH M.T.EKWOROMADU,C.B.POOR,C.P.OWENS,M.A.BALDERAS,M.FABIAN,
JRNL AUTH 2 J.S.OLSON,F.MURPHY,E.BALKABASI,E.S.HONSA,C.HE,C.W.GOULDING,
JRNL AUTH 3 A.W.MARESSO
JRNL TITL DIFFERENTIAL FUNCTION OF LIP RESIDUES IN THE MECHANISM AND
JRNL TITL 2 BIOLOGY OF AN ANTHRAX HEMOPHORE.
JRNL REF PLOS PATHOG. V. 8 02559 2012
JRNL REFN ISSN 1553-7366
JRNL PMID 22412371
JRNL DOI 10.1371/JOURNAL.PPAT.1002559
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 22863
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.120
REMARK 3 FREE R VALUE TEST SET COUNT : 2314
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 25.5768 - 4.6209 0.98 1309 146 0.2179 0.2249
REMARK 3 2 4.6209 - 3.6712 0.99 1315 149 0.1683 0.1821
REMARK 3 3 3.6712 - 3.2081 0.99 1340 154 0.1995 0.2131
REMARK 3 4 3.2081 - 2.9153 0.98 1291 143 0.2147 0.2244
REMARK 3 5 2.9153 - 2.7066 0.97 1302 142 0.2375 0.2624
REMARK 3 6 2.7066 - 2.5471 0.96 1294 139 0.2349 0.2638
REMARK 3 7 2.5471 - 2.4197 0.95 1252 152 0.2188 0.2554
REMARK 3 8 2.4197 - 2.3144 0.95 1272 137 0.2223 0.2529
REMARK 3 9 2.3144 - 2.2254 0.94 1259 146 0.1979 0.2573
REMARK 3 10 2.2254 - 2.1486 0.96 1259 145 0.2052 0.2327
REMARK 3 11 2.1486 - 2.0815 0.94 1270 132 0.2035 0.2687
REMARK 3 12 2.0815 - 2.0220 0.94 1256 135 0.2031 0.2462
REMARK 3 13 2.0220 - 1.9688 0.90 1169 144 0.2112 0.2584
REMARK 3 14 1.9688 - 1.9208 0.85 1113 144 0.2092 0.2895
REMARK 3 15 1.9208 - 1.8771 0.76 1033 114 0.2415 0.3176
REMARK 3 16 1.8771 - 1.8372 0.70 921 96 0.2857 0.3767
REMARK 3 17 1.8372 - 1.8004 0.65 894 96 0.2845 0.3512
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.46
REMARK 3 B_SOL : 61.86
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.400
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) : 6.34990
REMARK 3 B22 (A**2) : 1.22530
REMARK 3 B33 (A**2) : -7.57520
REMARK 3 B12 (A**2) : 1.86660
REMARK 3 B13 (A**2) : -3.01070
REMARK 3 B23 (A**2) : -6.47710
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 : 0.002 1951
REMARK 3 ANGLE : 0.566 2632
REMARK 3 CHIRALITY : 0.038 295
REMARK 3 PLANARITY : 0.002 333
REMARK 3 DIHEDRAL : 8.939 747
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4001 6.4654 2.0083
REMARK 3 T TENSOR
REMARK 3 T11: 0.1476 T22: 0.1991
REMARK 3 T33: 0.1264 T12: 0.0195
REMARK 3 T13: 0.0035 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.9096 L22: 1.0411
REMARK 3 L33: 1.8453 L12: -0.4783
REMARK 3 L13: -1.0033 L23: -0.0750
REMARK 3 S TENSOR
REMARK 3 S11: 0.0374 S12: 0.2103 S13: -0.0491
REMARK 3 S21: -0.1561 S22: -0.0901 S23: 0.0094
REMARK 3 S31: -0.0119 S32: -0.2255 S33: 0.0553
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4469 18.3866 -17.0553
REMARK 3 T TENSOR
REMARK 3 T11: 0.2246 T22: 0.2031
REMARK 3 T33: 0.1640 T12: 0.0152
REMARK 3 T13: 0.0084 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.7070 L22: 0.9070
REMARK 3 L33: 2.4926 L12: 0.4413
REMARK 3 L13: 1.6329 L23: 0.2199
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: -0.2573 S13: 0.0683
REMARK 3 S21: 0.2351 S22: -0.0740 S23: 0.0803
REMARK 3 S31: 0.1949 S32: -0.3673 S33: 0.1073
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 3SZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24541
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M NACL, 0.1 M CITRIC ACID (PH 3.5) ,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 ASP A 26
REMARK 465 ALA A 27
REMARK 465 LYS A 28
REMARK 465 ALA A 29
REMARK 465 ALA A 30
REMARK 465 ASP B 26
REMARK 465 ALA B 27
REMARK 465 LYS B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
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 ASP B 48 O HOH B 169 2.17
REMARK 500 O HOH B 206 O HOH B 210 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET B 55 N MET B 55 CA -0.138
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 ILE A 133 -1.92 -51.27
REMARK 500 ASN A 135 105.05 -56.60
REMARK 500 ASN B 135 49.35 -88.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 147
DBREF 3SZ6 A 26 146 UNP Q81L44 Q81L44_BACAN 26 146
DBREF 3SZ6 B 26 146 UNP Q81L44 Q81L44_BACAN 26 146
SEQRES 1 A 121 ASP ALA LYS ALA ALA THR LYS LEU ALA ASP GLY LYS TYR
SEQRES 2 A 121 ASN ILE ALA PHE THR VAL TRP LYS GLY ASP LYS ASP GLU
SEQRES 3 A 121 SER SER ARG MET ASN ARG TYR PHE GLU SER PRO ALA THR
SEQRES 4 A 121 LEU THR VAL LYS ASN GLY LYS GLN TYR VAL SER PHE LYS
SEQRES 5 A 121 VAL LYS ASP SER THR SER ILE LYS SER PHE GLN VAL GLU
SEQRES 6 A 121 LYS ASP GLY GLN PHE VAL GLU THR THR VAL LEU SER GLU
SEQRES 7 A 121 ASN LYS LYS ASP ASN THR ARG VAL VAL GLU PHE GLU VAL
SEQRES 8 A 121 ALA ASP LEU SER LYS LYS LEU ASN GLY LYS VAL LYS ILE
SEQRES 9 A 121 ASN ILE PRO ILE ILE ASN TYR ASN ALA SER TYR ASP ILE
SEQRES 10 A 121 ARG PHE VAL PHE
SEQRES 1 B 121 ASP ALA LYS ALA ALA THR LYS LEU ALA ASP GLY LYS TYR
SEQRES 2 B 121 ASN ILE ALA PHE THR VAL TRP LYS GLY ASP LYS ASP GLU
SEQRES 3 B 121 SER SER ARG MET ASN ARG TYR PHE GLU SER PRO ALA THR
SEQRES 4 B 121 LEU THR VAL LYS ASN GLY LYS GLN TYR VAL SER PHE LYS
SEQRES 5 B 121 VAL LYS ASP SER THR SER ILE LYS SER PHE GLN VAL GLU
SEQRES 6 B 121 LYS ASP GLY GLN PHE VAL GLU THR THR VAL LEU SER GLU
SEQRES 7 B 121 ASN LYS LYS ASP ASN THR ARG VAL VAL GLU PHE GLU VAL
SEQRES 8 B 121 ALA ASP LEU SER LYS LYS LEU ASN GLY LYS VAL LYS ILE
SEQRES 9 B 121 ASN ILE PRO ILE ILE ASN TYR ASN ALA SER TYR ASP ILE
SEQRES 10 B 121 ARG PHE VAL PHE
HET CL A 1 1
HET CL B 1 1
HET GOL B 147 6
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CL 2(CL 1-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *161(H2 O)
HELIX 1 1 SER A 53 PHE A 59 5 7
HELIX 2 2 ASP A 80 THR A 82 5 3
HELIX 3 3 SER B 53 TYR B 58 5 6
HELIX 4 4 ASP B 80 THR B 82 5 3
SHEET 1 A 5 GLY A 36 ILE A 40 0
SHEET 2 A 5 ALA A 63 LYS A 68 -1 O LEU A 65 N TYR A 38
SHEET 3 A 5 LYS A 71 VAL A 78 -1 O SER A 75 N THR A 64
SHEET 4 A 5 THR A 109 GLU A 115 -1 O ARG A 110 N VAL A 78
SHEET 5 A 5 THR A 99 ASN A 104 -1 N ASN A 104 O THR A 109
SHEET 1 B 5 THR A 43 LYS A 46 0
SHEET 2 B 5 ASN A 137 VAL A 145 -1 O ARG A 143 N TRP A 45
SHEET 3 B 5 LEU A 123 ASN A 130 -1 N VAL A 127 O TYR A 140
SHEET 4 B 5 ILE A 84 GLU A 90 -1 N GLN A 88 O LYS A 126
SHEET 5 B 5 PHE A 95 GLU A 97 -1 O VAL A 96 N VAL A 89
SHEET 1 C 5 GLY B 36 ILE B 40 0
SHEET 2 C 5 ALA B 63 LYS B 68 -1 O LEU B 65 N TYR B 38
SHEET 3 C 5 LYS B 71 VAL B 78 -1 O SER B 75 N THR B 64
SHEET 4 C 5 THR B 109 GLU B 115 -1 O ARG B 110 N VAL B 78
SHEET 5 C 5 THR B 99 ASN B 104 -1 N ASN B 104 O THR B 109
SHEET 1 D 5 THR B 43 LYS B 46 0
SHEET 2 D 5 TYR B 136 VAL B 145 -1 O ARG B 143 N TRP B 45
SHEET 3 D 5 LEU B 123 ILE B 131 -1 N ILE B 129 O ALA B 138
SHEET 4 D 5 ILE B 84 LYS B 91 -1 N LYS B 85 O LYS B 128
SHEET 5 D 5 GLN B 94 GLU B 97 -1 O GLN B 94 N LYS B 91
CISPEP 1 SER A 61 PRO A 62 0 2.31
CISPEP 2 SER B 61 PRO B 62 0 4.21
SITE 1 AC1 3 LYS A 122 ARG A 143 ALA B 41
SITE 1 AC2 2 ALA A 41 ARG B 143
SITE 1 AC3 9 LYS B 85 SER B 86 PHE B 87 GLU B 97
SITE 2 AC3 9 THR B 98 VAL B 100 ARG B 110 VAL B 112
SITE 3 AC3 9 HOH B 191
CRYST1 36.637 43.659 47.408 99.24 96.53 107.35 P 1 2
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 0.027295 0.008529 0.004977 0.00000
SCALE2 0.000000 0.023997 0.005027 0.00000
SCALE3 0.000000 0.000000 0.021692 0.00000
(ATOM LINES ARE NOT SHOWN.)
END