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HEADER TRANSFERASE 27-MAY-25 9RC4
TITLE CRYSTAL STRUCTURE OF VIRJ DOMAIN 1 FROM BRUCELLA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VIRULENCE FACTOR FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRUCELLA ABORTUS;
SOURCE 3 ORGANISM_TAXID: 235;
SOURCE 4 GENE: NBW10_01030, NBW10_16820;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BRUCELLA, TYPE IV SECRETION, MEMBRANE, PHOSPHATIDYL GLYCEROL,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DUGELAY,S.FERRARIN,L.TERRADOT
REVDAT 1 03-SEP-25 9RC4 0
JRNL AUTH C.DUGELAY,S.FERRARIN,L.TERRADOT
JRNL TITL CRYSTAL STRUCTURE OF THE VIRULENCE PROTEIN J (VIRJ) DOMAIN 1
JRNL TITL 2 FROM BRUCELLA ABORTUS.
JRNL REF ACTA CRYSTALLOGR.,SECT.F 2025
JRNL REFN ESSN 2053-230X
JRNL PMID 40824293
JRNL DOI 10.1107/S2053230X25006697
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.2_5419
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 39667
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1910
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 38.2000 - 4.1800 0.97 2690 143 0.1495 0.1517
REMARK 3 2 4.1800 - 3.3200 0.98 2702 155 0.1560 0.1755
REMARK 3 3 3.3200 - 2.9000 0.98 2719 133 0.1879 0.1890
REMARK 3 4 2.9000 - 2.6400 0.97 2717 140 0.1940 0.2173
REMARK 3 5 2.6400 - 2.4500 0.98 2744 106 0.1853 0.2401
REMARK 3 6 2.4500 - 2.3000 0.97 2727 126 0.1839 0.1994
REMARK 3 7 2.3000 - 2.1900 0.97 2711 135 0.1762 0.2564
REMARK 3 8 2.1900 - 2.0900 0.97 2700 146 0.1794 0.2302
REMARK 3 9 2.0900 - 2.0100 0.97 2688 125 0.1905 0.2091
REMARK 3 10 2.0100 - 1.9400 0.97 2653 137 0.1865 0.2461
REMARK 3 11 1.9400 - 1.8800 0.96 2717 115 0.1898 0.2531
REMARK 3 12 1.8800 - 1.8300 0.96 2679 158 0.2006 0.2541
REMARK 3 13 1.8300 - 1.7800 0.96 2660 147 0.2355 0.2649
REMARK 3 14 1.7800 - 1.7400 0.95 2650 144 0.2816 0.3284
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.225
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.828
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.92
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.88
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 : 0.006 3260
REMARK 3 ANGLE : 0.786 4451
REMARK 3 CHIRALITY : 0.055 514
REMARK 3 PLANARITY : 0.008 597
REMARK 3 DIHEDRAL : 15.669 1199
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 9RC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1292148164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39671
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 46.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.84500
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350 16% W/V, 0.06M CITRIC ACID PH
REMARK 280 4.1, 0.04M BIS-TRIS PROPANE, VAPOR DIFFUSION, TEMPERATURE 292K
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 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 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 -6
REMARK 465 ILE A -5
REMARK 465 LYS A 215
REMARK 465 ASN A 216
REMARK 465 GLU A 217
REMARK 465 ALA A 218
REMARK 465 LEU A 219
REMARK 465 PRO A 220
REMARK 465 ILE A 221
REMARK 465 ILE A 222
REMARK 465 GLY B -6
REMARK 465 ILE B -5
REMARK 465 ASP B -4
REMARK 465 PRO B -3
REMARK 465 LYS B 215
REMARK 465 ASN B 216
REMARK 465 GLU B 217
REMARK 465 ALA B 218
REMARK 465 LEU B 219
REMARK 465 PRO B 220
REMARK 465 ILE B 221
REMARK 465 ILE B 222
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 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 93 CG1 CG2
REMARK 470 TYR A 94 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 144 CG CD OE1 OE2
REMARK 470 LYS B 32 CG CD CE NZ
REMARK 470 TYR B 94 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 150 CG OD1 OD2
REMARK 470 ARG B 183 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 212 CG CD OE1 NE2
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 GLU A 7 -124.53 57.49
REMARK 500 ARG A 133 49.28 -96.73
REMARK 500 GLU A 141 -89.88 -89.21
REMARK 500 ASN A 176 -162.81 -113.71
REMARK 500 GLU B 7 -126.10 55.97
REMARK 500 GLU B 141 -89.31 -97.71
REMARK 500 VAL B 157 -167.66 -109.86
REMARK 500 ASN B 176 -166.34 -119.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9RC4 A 0 222 UNP A0AAE9RTQ7_BRUAO
DBREF2 9RC4 A A0AAE9RTQ7 43 265
DBREF1 9RC4 B 0 222 UNP A0AAE9RTQ7_BRUAO
DBREF2 9RC4 B A0AAE9RTQ7 43 265
SEQADV 9RC4 GLY A -6 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 ILE A -5 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 ASP A -4 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 PRO A -3 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 PHE A -2 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 THR A -1 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 GLY B -6 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 ILE B -5 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 ASP B -4 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 PRO B -3 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 PHE B -2 UNP A0AAE9RTQ EXPRESSION TAG
SEQADV 9RC4 THR B -1 UNP A0AAE9RTQ EXPRESSION TAG
SEQRES 1 A 229 GLY ILE ASP PRO PHE THR PRO VAL ILE HIS ALA SER ALA
SEQRES 2 A 229 GLU ARG LEU SER ASN ILE PRO VAL TYR MET PRO LYS GLY
SEQRES 3 A 229 ASP PRO VAL GLY LEU ALA ILE LEU LEU SER ASP GLU LYS
SEQRES 4 A 229 GLY ILE GLY ASP GLN GLU ARG SER TYR MET ASP ALA MET
SEQRES 5 A 229 LEU ALA ARG ASN ILE ILE VAL MET PRO VAL GLU LEU GLY
SEQRES 6 A 229 PRO TRP ARG ALA ALA LEU ASP LYS GLU ASP GLY GLU CYS
SEQRES 7 A 229 ASN TYR LEU ASP SER ASP PHE GLU ALA ILE ALA LYS GLU
SEQRES 8 A 229 ALA LEU ARG GLY LEU ASP LEU GLY VAL TYR PHE HIS PRO
SEQRES 9 A 229 VAL LEU THR GLY ILE GLY GLN GLY ALA THR ILE ALA TYR
SEQRES 10 A 229 ALA ALA ALA SER ASP SER PRO ASP ALA THR ILE ALA GLY
SEQRES 11 A 229 ALA VAL SER LEU ASP PRO THR PRO ALA ARG THR ARG LEU
SEQRES 12 A 229 PRO SER CYS THR GLU LYS ALA GLU ALA ILE LYS GLY PRO
SEQRES 13 A 229 ASP GLY GLY PHE THR TYR SER VAL ASN ALA ALA LEU PRO
SEQRES 14 A 229 ALA PRO ALA LEU LEU ILE SER PRO PRO GLY SER PRO VAL
SEQRES 15 A 229 ASN ASN PRO VAL GLU ALA ARG ARG LYS ASN ILE ALA VAL
SEQRES 16 A 229 LEU GLN THR ALA PRO ASP PHE SER ALA ARG MET LYS MET
SEQRES 17 A 229 ALA VAL ASP ASN VAL VAL ALA MET ALA ASP GLN ASP ALA
SEQRES 18 A 229 LYS ASN GLU ALA LEU PRO ILE ILE
SEQRES 1 B 229 GLY ILE ASP PRO PHE THR PRO VAL ILE HIS ALA SER ALA
SEQRES 2 B 229 GLU ARG LEU SER ASN ILE PRO VAL TYR MET PRO LYS GLY
SEQRES 3 B 229 ASP PRO VAL GLY LEU ALA ILE LEU LEU SER ASP GLU LYS
SEQRES 4 B 229 GLY ILE GLY ASP GLN GLU ARG SER TYR MET ASP ALA MET
SEQRES 5 B 229 LEU ALA ARG ASN ILE ILE VAL MET PRO VAL GLU LEU GLY
SEQRES 6 B 229 PRO TRP ARG ALA ALA LEU ASP LYS GLU ASP GLY GLU CYS
SEQRES 7 B 229 ASN TYR LEU ASP SER ASP PHE GLU ALA ILE ALA LYS GLU
SEQRES 8 B 229 ALA LEU ARG GLY LEU ASP LEU GLY VAL TYR PHE HIS PRO
SEQRES 9 B 229 VAL LEU THR GLY ILE GLY GLN GLY ALA THR ILE ALA TYR
SEQRES 10 B 229 ALA ALA ALA SER ASP SER PRO ASP ALA THR ILE ALA GLY
SEQRES 11 B 229 ALA VAL SER LEU ASP PRO THR PRO ALA ARG THR ARG LEU
SEQRES 12 B 229 PRO SER CYS THR GLU LYS ALA GLU ALA ILE LYS GLY PRO
SEQRES 13 B 229 ASP GLY GLY PHE THR TYR SER VAL ASN ALA ALA LEU PRO
SEQRES 14 B 229 ALA PRO ALA LEU LEU ILE SER PRO PRO GLY SER PRO VAL
SEQRES 15 B 229 ASN ASN PRO VAL GLU ALA ARG ARG LYS ASN ILE ALA VAL
SEQRES 16 B 229 LEU GLN THR ALA PRO ASP PHE SER ALA ARG MET LYS MET
SEQRES 17 B 229 ALA VAL ASP ASN VAL VAL ALA MET ALA ASP GLN ASP ALA
SEQRES 18 B 229 LYS ASN GLU ALA LEU PRO ILE ILE
HET GOL A 301 6
HET GOL B 301 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *257(H2 O)
HELIX 1 AA1 GLY A 35 ARG A 48 1 14
HELIX 2 AA2 GLU A 56 LYS A 66 1 11
HELIX 3 AA3 LEU A 74 ASP A 90 1 17
HELIX 4 AA4 GLN A 104 ASP A 115 1 12
HELIX 5 AA5 ASN A 177 LYS A 184 1 8
HELIX 6 AA6 ASP A 194 ALA A 214 1 21
HELIX 7 AA7 GLY B 35 ALA B 47 1 13
HELIX 8 AA8 GLU B 56 LYS B 66 1 11
HELIX 9 AA9 LEU B 74 ASP B 90 1 17
HELIX 10 AB1 GLN B 104 ASP B 115 1 12
HELIX 11 AB2 ASN B 177 LYS B 184 1 8
HELIX 12 AB3 ASP B 194 ALA B 214 1 21
SHEET 1 AA1 2 ILE A 2 ALA A 6 0
SHEET 2 AA1 2 LEU A 9 VAL A 14 -1 O ILE A 12 N ALA A 4
SHEET 1 AA2 6 ILE A 50 VAL A 55 0
SHEET 2 AA2 6 GLY A 23 LEU A 28 1 N LEU A 27 O VAL A 55
SHEET 3 AA2 6 VAL A 98 GLY A 103 1 O VAL A 98 N LEU A 24
SHEET 4 AA2 6 GLY A 123 PRO A 129 1 O GLY A 123 N LEU A 99
SHEET 5 AA2 6 ALA A 165 SER A 169 1 O LEU A 166 N SER A 126
SHEET 6 AA2 6 VAL A 188 THR A 191 1 O VAL A 188 N LEU A 167
SHEET 1 AA3 2 ALA A 145 LYS A 147 0
SHEET 2 AA3 2 PHE A 153 TYR A 155 -1 O THR A 154 N ILE A 146
SHEET 1 AA4 2 ILE B 2 ALA B 6 0
SHEET 2 AA4 2 LEU B 9 VAL B 14 -1 O ILE B 12 N ALA B 4
SHEET 1 AA5 6 ILE B 50 VAL B 55 0
SHEET 2 AA5 6 GLY B 23 LEU B 28 1 N ALA B 25 O ILE B 51
SHEET 3 AA5 6 VAL B 98 GLY B 103 1 O THR B 100 N LEU B 28
SHEET 4 AA5 6 GLY B 123 PRO B 129 1 O GLY B 123 N LEU B 99
SHEET 5 AA5 6 ALA B 165 SER B 169 1 O LEU B 166 N SER B 126
SHEET 6 AA5 6 VAL B 188 THR B 191 1 O VAL B 188 N LEU B 167
SHEET 1 AA6 2 ALA B 145 LYS B 147 0
SHEET 2 AA6 2 PHE B 153 TYR B 155 -1 O THR B 154 N ILE B 146
SSBOND 1 CYS A 71 CYS A 139 1555 1555 2.06
SSBOND 2 CYS B 71 CYS B 139 1555 1555 2.05
CRYST1 40.638 47.235 54.124 80.92 89.06 86.14 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 0.024608 -0.001662 -0.000146 0.00000
SCALE2 0.000000 0.021219 -0.003375 0.00000
SCALE3 0.000000 0.000000 0.018711 0.00000
TER 1599 ALA A 214
TER 3186 ALA B 214
MASTER 264 0 2 12 20 0 0 6 3445 2 16 36
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