HEADER OXIDOREDUCTASE 11-NOV-15 5EPF
TITLE CRYSTAL STRUCTURE OF PEROXIDOXIN BCPB FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXIREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 ATCC: 25618;
SOURCE 7 GENE: LH57_08785;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: MYTUD.00904.A.B1
KEYWDS MYCOBACTERIUM TUBERCULOSIS, PEROXIDOXIN, BCPB, STRUCTURAL GENOMICS,
KEYWDS 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 27-SEP-23 5EPF 1 REMARK
REVDAT 1 02-DEC-15 5EPF 0
JRNL AUTH J.ABENDROTH,S.J.MAYCLIN,D.D.LORIMER,T.E.EDWARDS
JRNL TITL CRYSTAL STRUCTURE OF PEROXIDOXIN BCPB FROM MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.35 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 35886
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.310
REMARK 3 FREE R VALUE TEST SET COUNT : 1904
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 50.0000 - 3.2527 1.00 2634 138 0.1531 0.1868
REMARK 3 2 3.2527 - 2.5821 1.00 2499 147 0.1535 0.1962
REMARK 3 3 2.5821 - 2.2558 1.00 2475 143 0.1503 0.1622
REMARK 3 4 2.2558 - 2.0496 1.00 2476 127 0.1409 0.1570
REMARK 3 5 2.0496 - 1.9027 0.99 2405 153 0.1408 0.1868
REMARK 3 6 1.9027 - 1.7906 0.99 2422 146 0.1394 0.1817
REMARK 3 7 1.7906 - 1.7009 0.99 2426 137 0.1234 0.1596
REMARK 3 8 1.7009 - 1.6268 0.99 2392 131 0.1171 0.1550
REMARK 3 9 1.6268 - 1.5642 0.99 2380 145 0.1134 0.1499
REMARK 3 10 1.5642 - 1.5102 0.99 2397 138 0.1154 0.1664
REMARK 3 11 1.5102 - 1.4630 0.98 2383 106 0.1126 0.1487
REMARK 3 12 1.4630 - 1.4212 0.98 2386 126 0.1115 0.1592
REMARK 3 13 1.4212 - 1.3838 0.98 2351 131 0.1309 0.1525
REMARK 3 14 1.3838 - 1.3500 0.98 2356 136 0.1489 0.1785
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.68
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 : 0.008 1279
REMARK 3 ANGLE : 0.945 1744
REMARK 3 CHIRALITY : 0.093 199
REMARK 3 PLANARITY : 0.007 228
REMARK 3 DIHEDRAL : 13.988 491
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 5EPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215309.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-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 : 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) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35895
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 11.00
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.840
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 ENTRY 3DRN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MYCROLYTIC MCSG1 E6: 20% PEG 3350,
REMARK 280 200MM POTASSIUM SULPHATE ; MYTUD.00904.A.B1.PW37743 AT 18.3 MG/
REMARK 280 ML, CRYO: 20% EG, 1 STEP; TRAY: 266501E6; PUCK: QMK2-10, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 27.81000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.81000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.07000
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: 490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 ALA A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 GLY A 162
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 LYS A 118 CG CD CE NZ
REMARK 470 ARG A 160 CG CD NE CZ NH1 NH2
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 HOH A 307 O HOH A 400 2.13
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 CYS A 52 CB CYS A 52 SG -0.098
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 MET A 48 -3.76 78.29
REMARK 500 ASP A 100 70.66 -105.21
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 SO4 A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-MYTUD.00904.A RELATED DB: TARGETTRACK
DBREF 5EPF A 9 162 UNP I6X1R8 I6X1R8_MYCTU 1 154
SEQADV 5EPF MET A 1 UNP I6X1R8 INITIATING METHIONINE
SEQADV 5EPF ALA A 2 UNP I6X1R8 EXPRESSION TAG
SEQADV 5EPF HIS A 3 UNP I6X1R8 EXPRESSION TAG
SEQADV 5EPF HIS A 4 UNP I6X1R8 EXPRESSION TAG
SEQADV 5EPF HIS A 5 UNP I6X1R8 EXPRESSION TAG
SEQADV 5EPF HIS A 6 UNP I6X1R8 EXPRESSION TAG
SEQADV 5EPF HIS A 7 UNP I6X1R8 EXPRESSION TAG
SEQADV 5EPF HIS A 8 UNP I6X1R8 EXPRESSION TAG
SEQRES 1 A 162 MET ALA HIS HIS HIS HIS HIS HIS MET LYS THR GLY ASP
SEQRES 2 A 162 THR VAL ALA ASP PHE GLU LEU PRO ASP GLN THR GLY THR
SEQRES 3 A 162 PRO ARG ARG LEU SER VAL LEU LEU SER ASP GLY PRO VAL
SEQRES 4 A 162 VAL LEU PHE PHE TYR PRO ALA ALA MET THR PRO GLY CYS
SEQRES 5 A 162 THR LYS GLU ALA CYS HIS PHE ARG ASP LEU ALA LYS GLU
SEQRES 6 A 162 PHE ALA GLU VAL ARG ALA SER ARG VAL GLY ILE SER THR
SEQRES 7 A 162 ASP PRO VAL ARG LYS GLN ALA LYS PHE ALA GLU VAL ARG
SEQRES 8 A 162 ARG PHE ASP TYR PRO LEU LEU SER ASP ALA GLN GLY THR
SEQRES 9 A 162 VAL ALA ALA GLN PHE GLY VAL LYS ARG GLY LEU LEU GLY
SEQRES 10 A 162 LYS LEU MET PRO VAL LYS ARG THR THR PHE VAL ILE ASP
SEQRES 11 A 162 THR ASP ARG LYS VAL LEU ASP VAL ILE SER SER GLU PHE
SEQRES 12 A 162 SER MET ASP ALA HIS ALA ASP LYS ALA LEU ALA THR LEU
SEQRES 13 A 162 ARG ALA ILE ARG SER GLY
HET SO4 A 200 5
HET SO4 A 201 5
HET EDO A 202 4
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 EDO C2 H6 O2
FORMUL 5 HOH *253(H2 O)
HELIX 1 AA1 LEU A 30 LEU A 34 1 5
HELIX 2 AA2 THR A 49 LEU A 62 1 14
HELIX 3 AA3 LEU A 62 VAL A 69 1 8
HELIX 4 AA4 PRO A 80 ARG A 92 1 13
HELIX 5 AA5 GLY A 103 GLY A 110 1 8
HELIX 6 AA6 ASP A 146 ILE A 159 1 14
SHEET 1 AA1 2 GLU A 19 PRO A 21 0
SHEET 2 AA1 2 PRO A 27 ARG A 29 -1 O ARG A 28 N LEU A 20
SHEET 1 AA2 5 LEU A 97 SER A 99 0
SHEET 2 AA2 5 SER A 72 SER A 77 1 N GLY A 75 O LEU A 98
SHEET 3 AA2 5 VAL A 39 PHE A 43 1 N VAL A 40 O VAL A 74
SHEET 4 AA2 5 THR A 125 ILE A 129 -1 O ILE A 129 N VAL A 39
SHEET 5 AA2 5 VAL A 135 ILE A 139 -1 O LEU A 136 N VAL A 128
SHEET 1 AA3 2 ARG A 113 LEU A 115 0
SHEET 2 AA3 2 LYS A 118 MET A 120 -1 O MET A 120 N ARG A 113
SITE 1 AC1 8 ARG A 60 ARG A 91 ARG A 92 LYS A 134
SITE 2 AC1 8 HOH A 309 HOH A 366 HOH A 397 HOH A 451
SITE 1 AC2 5 ALA A 63 ARG A 113 HOH A 306 HOH A 374
SITE 2 AC2 5 HOH A 425
SITE 1 AC3 5 PRO A 80 VAL A 81 ARG A 82 HOH A 404
SITE 2 AC3 5 HOH A 418
CRYST1 55.620 72.140 40.170 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 0.017979 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013862 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024894 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
