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HEADER LIPID BINDING PROTEIN 24-JUL-24 9G8U
TITLE STRUCTURE OF THE LIPA:LIPB COMPLEX FROM ACINETOBACTER BAUMANNII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTONIZING LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LIPASE CHAPERONE;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: LIPASE ACTIVATOR PROTEIN,LIPASE FOLDASE,LIPASE HELPER
COMPND 10 PROTEIN,LIPASE MODULATOR;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER BAUMANNII;
SOURCE 3 ORGANISM_TAXID: 470;
SOURCE 4 STRAIN: DSM 30011;
SOURCE 5 GENE: LIP, HMPREF0010_02549;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ACINETOBACTER BAUMANNII;
SOURCE 11 ORGANISM_TAXID: 470;
SOURCE 12 STRAIN: DSM 30011;
SOURCE 13 GENE: LIFO, EA706_01485, EA722_01050, P9867_05230;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_VARIANT: STAR
KEYWDS LIPASE, SECRETION SYSTEM, BACTERIAL INFECTION, CHAPERONE COMPLEX,
KEYWDS 2 PROTEIN-PROTEIN INTERACTION, LIPID BINDING, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.R.DE OLIVEIRA SILVA,C.CONTRERAS-MARTEL,R.RODRIGUES DE MELO,
AUTHOR 2 L.ZANPHORLIN,D.M.TRINDADE,A.DESSEN
REVDAT 1 19-FEB-25 9G8U 0
JRNL AUTH Y.R.DE OLIVEIRA SILVA,C.CONTRERAS-MARTEL,
JRNL AUTH 2 R.RODRIGUES DE MELO,L.M.ZANPHORLIN,D.M.TRINDADE,A.DESSEN
JRNL TITL ARCHITECTURE OF AN EMBRACING LIPASE-FOLDASE COMPLEX OF THE
JRNL TITL 2 TYPE II SECRETION SYSTEM OF ACINETOBACTER BAUMANNII.
JRNL REF STRUCTURE 2025
JRNL REFN ISSN 0969-2126
JRNL PMID 39904335
JRNL DOI 10.1016/J.STR.2024.12.022
REMARK 2
REMARK 2 RESOLUTION. 3.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 23444
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.277
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.386
REMARK 3 FREE R VALUE TEST SET COUNT : 1966
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1578
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.5190
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.5110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4605
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 151.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.25400
REMARK 3 B22 (A**2) : 3.25400
REMARK 3 B33 (A**2) : -10.55600
REMARK 3 B12 (A**2) : 1.62700
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.147
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.456
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.659
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.817
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4702 ; 0.006 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6368 ; 1.265 ; 1.818
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 575 ; 3.121 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 28 ; 1.222 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 811 ; 6.592 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 688 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3654 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2289 ; 0.256 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3229 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 325 ; 0.112 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.198 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2306 ;13.825 ;14.813
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2879 ;21.611 ;26.639
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2396 ;15.922 ;15.250
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3489 ;24.384 ;27.883
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE NOT BEEN USED
REMARK 4
REMARK 4 9G8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-24.
REMARK 100 THE DEPOSITION ID IS D_1292140394.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-21
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 : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .97718
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20210323
REMARK 200 DATA SCALING SOFTWARE : XSCALE 20210323
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23444
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.174
REMARK 200 RESOLUTION RANGE LOW (A) : 48.296
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 19.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: POLYHEDRAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 0.1 M BIS-TRIS
REMARK 280 PROPANE (PH 7.5), 5% POLYETHYLENE GLYCOL (PEG) 400, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 93.14333
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 46.57167
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 46.57167
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 93.14333
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 23
REMARK 465 SER A 24
REMARK 465 ASN A 25
REMARK 465 ALA A 26
REMARK 465 GLU A 27
REMARK 465 GLN A 28
REMARK 465 VAL A 29
REMARK 465 LYS A 30
REMARK 465 SER A 31
REMARK 465 SER A 32
REMARK 465 MET B 42
REMARK 465 TRP B 43
REMARK 465 SER B 44
REMARK 465 HIS B 45
REMARK 465 PRO B 46
REMARK 465 GLN B 47
REMARK 465 PHE B 48
REMARK 465 GLU B 49
REMARK 465 LYS B 50
REMARK 465 GLY B 51
REMARK 465 THR B 52
REMARK 465 LEU B 53
REMARK 465 ASN B 54
REMARK 465 SER B 55
REMARK 465 PRO B 56
REMARK 465 LEU B 57
REMARK 465 ASN B 58
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 HIS A 49 -153.83 -88.80
REMARK 500 MET A 51 87.92 51.79
REMARK 500 VAL A 57 56.66 -65.91
REMARK 500 THR A 59 -66.99 -177.86
REMARK 500 TYR A 68 104.16 -57.93
REMARK 500 SER A 121 -119.55 50.52
REMARK 500 THR A 163 -61.80 -16.86
REMARK 500 PRO A 191 109.06 -48.19
REMARK 500 ALA A 242 -71.76 -98.02
REMARK 500 PRO A 249 -17.92 -44.60
REMARK 500 ASP A 266 65.94 -108.26
REMARK 500 LEU A 270 -40.93 -136.10
REMARK 500 ARG A 283 131.53 -173.59
REMARK 500 ASP A 285 30.17 -147.71
REMARK 500 ASN A 295 46.75 73.52
REMARK 500 MET A 298 11.56 48.95
REMARK 500 ALA A 302 157.93 -48.14
REMARK 500 GLN B 68 7.79 -53.07
REMARK 500 ASP B 69 37.89 -144.92
REMARK 500 GLN B 75 76.48 -102.84
REMARK 500 SER B 80 26.14 -77.41
REMARK 500 SER B 81 14.08 -158.77
REMARK 500 LEU B 122 -160.01 -114.69
REMARK 500 GLN B 145 41.32 -92.38
REMARK 500 LYS B 152 99.71 -62.96
REMARK 500 GLN B 153 7.59 -58.13
REMARK 500 ASN B 157 -5.15 -53.42
REMARK 500 TYR B 158 -64.91 -92.61
REMARK 500 PHE B 183 -35.38 -131.16
REMARK 500 SER B 184 -62.26 -26.33
REMARK 500 ASP B 202 92.51 -66.81
REMARK 500 SER B 203 38.49 -90.72
REMARK 500 ASN B 249 63.15 67.24
REMARK 500 GLN B 316 -34.43 -134.74
REMARK 500 PHE B 341 -35.39 -132.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 248 OD2
REMARK 620 2 ASP A 292 OD1 114.5
REMARK 620 3 GLN A 296 O 74.8 70.6
REMARK 620 4 ILE A 300 O 137.3 93.2 85.7
REMARK 620 N 1 2 3
DBREF 9G8U A 25 324 UNP D0CCR9 D0CCR9_ACIB2 25 324
DBREF1 9G8U B 52 343 UNP A0A0J8V187_ACIBA
DBREF2 9G8U B A0A0J8V187 52 343
SEQADV 9G8U GLY A 23 UNP D0CCR9 EXPRESSION TAG
SEQADV 9G8U SER A 24 UNP D0CCR9 EXPRESSION TAG
SEQADV 9G8U ALA A 211 UNP D0CCR9 SER 211 CONFLICT
SEQADV 9G8U ALA A 302 UNP D0CCR9 SER 302 CONFLICT
SEQADV 9G8U LEU A 304 UNP D0CCR9 PHE 304 CONFLICT
SEQADV 9G8U MET B 42 UNP A0A0J8V18 INITIATING METHIONINE
SEQADV 9G8U TRP B 43 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U SER B 44 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U HIS B 45 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U PRO B 46 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U GLN B 47 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U PHE B 48 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U GLU B 49 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U LYS B 50 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U GLY B 51 UNP A0A0J8V18 EXPRESSION TAG
SEQADV 9G8U LYS B 108 UNP A0A0J8V18 GLN 108 CONFLICT
SEQADV 9G8U SER B 149 UNP A0A0J8V18 PRO 149 CONFLICT
SEQADV 9G8U ALA B 252 UNP A0A0J8V18 VAL 252 CONFLICT
SEQRES 1 A 302 GLY SER ASN ALA GLU GLN VAL LYS SER SER PHE VAL TYR
SEQRES 2 A 302 SER THR TYR ALA GLN THR LYS TYR PRO LEU VAL PHE ASN
SEQRES 3 A 302 HIS GLY MET ALA GLY PHE ASN ARG VAL GLY THR ASP THR
SEQRES 4 A 302 LEU GLY LEU ASP TYR TRP TYR GLN ILE LEU PRO ASP LEU
SEQRES 5 A 302 ALA ARG ASN GLY GLY ASN VAL TRP ALA THR ARG VAL SER
SEQRES 6 A 302 PRO PHE ASN SER THR GLU VAL ARG GLY GLU GLN LEU ALA
SEQRES 7 A 302 GLN GLN VAL GLU GLU ILE ILE ALA ILE THR GLY LYS PRO
SEQRES 8 A 302 LYS VAL ASN LEU ILE GLY HIS SER HIS GLY GLY PRO THR
SEQRES 9 A 302 ILE ARG TYR VAL ALA GLY ILE MET PRO GLU LYS VAL ALA
SEQRES 10 A 302 SER LEU THR THR ILE GLY ALA PRO HIS LYS GLY SER PRO
SEQRES 11 A 302 MET ALA ASP VAL ILE LEU ASN VAL GLU GLY THR PRO LEU
SEQRES 12 A 302 SER GLY LEU ALA THR LEU VAL ASN TRP PHE SER ALA ALA
SEQRES 13 A 302 ILE THR TRP ALA GLY GLY LEU ASP PRO ASN SER TYR PRO
SEQRES 14 A 302 HIS ASP SER LEU ALA GLY ALA HIS SER LEU SER THR GLN
SEQRES 15 A 302 GLY SER ALA GLN PHE ASN ALA GLN PHE PRO MET GLY VAL
SEQRES 16 A 302 PRO THR THR SER CYS GLY GLU GLY ALA TYR GLN GLU LYS
SEQRES 17 A 302 GLY ILE TYR MET TYR SER PHE SER GLY ASN LYS ALA LEU
SEQRES 18 A 302 THR ASN PRO LEU ASP PRO PHE ASP ILE ALA LEU THR GLY
SEQRES 19 A 302 SER SER LEU VAL VAL ASP PRO PHE GLY ASP ASN ASP GLY
SEQRES 20 A 302 LEU VAL SER ARG CYS SER ALA LYS PHE GLY LYS THR ILE
SEQRES 21 A 302 ARG ASP ASP TYR ASN TRP ASN HIS LEU ASP GLU VAL ASN
SEQRES 22 A 302 GLN VAL MET GLY ILE ARG ALA ILE LEU ALA ALA ASP PRO
SEQRES 23 A 302 VAL SER VAL TYR ARG GLN HIS ALA ASN ARG LEU LYS LEU
SEQRES 24 A 302 GLN GLY LEU
SEQRES 1 B 302 MET TRP SER HIS PRO GLN PHE GLU LYS GLY THR LEU ASN
SEQRES 2 B 302 SER PRO LEU ASN GLU ASN THR TYR LEU SER LYS SER GLN
SEQRES 3 B 302 GLN ASP THR GLN VAL ASN CYS GLN LEU LYS ILE ASN SER
SEQRES 4 B 302 SER GLN HIS LEU VAL VAL ASN SER GLN THR ARG ASP CYS
SEQRES 5 B 302 PHE GLU TYR PHE ILE THR GLN TYR GLY GLU SER ASN LEU
SEQRES 6 B 302 GLN LYS VAL LYS THR HIS PHE GLU LYS PHE ILE GLN ASP
SEQRES 7 B 302 GLN TYR LEU GLU PRO ALA ARG SER GLN ILE ILE ASP LEU
SEQRES 8 B 302 TRP THR ARG TYR LEU LYS TYR ARG GLU GLN LEU ALA GLN
SEQRES 9 B 302 ILE GLN PRO SER GLN SER LYS GLN GLN ASP GLN ASN TYR
SEQRES 10 B 302 PHE GLN LYS VAL PHE ASN SER ILE GLN ASP ILE ARG LYS
SEQRES 11 B 302 ARG PHE PHE SER ALA SER GLU ILE GLU GLY LEU PHE SER
SEQRES 12 B 302 THR GLU ASP ILE TYR GLN ASN TYR THR LEU ASP ARG MET
SEQRES 13 B 302 LYS ILE LEU GLU ASP SER SER LEU SER GLU ILE GLU LYS
SEQRES 14 B 302 ALA LYS LYS LEU LYS GLU ARG PHE GLU GLN LEU PRO GLU
SEQRES 15 B 302 ASP TRP GLN GLU ASN LEU GLN GLU LEU SER LYS LEU ASP
SEQRES 16 B 302 ASP LEU HIS THR LEU THR LYS GLN ILE LYS ALA ARG ASN
SEQRES 17 B 302 GLY SER ALA GLU GLU LEU ARG GLN MET ARG THR ALA LEU
SEQRES 18 B 302 VAL GLY ALA GLU ALA THR GLN ARG LEU GLU THR LEU ASP
SEQRES 19 B 302 ILE GLN ARG ASN ALA TRP GLN GLN ARG VAL THR GLY TYR
SEQRES 20 B 302 LEU ASN GLN ARG ASP GLU VAL LEU HIS SER ASN MET SER
SEQRES 21 B 302 ASP SER ALA LYS LYS GLN ALA ILE GLN GLN LEU ARG GLN
SEQRES 22 B 302 GLN GLN PHE SER SER SER GLN GLU GLN LEU ARG LEU ARG
SEQRES 23 B 302 THR PHE GLU THR VAL HIS ASP GLN GLY GLY GLU LEU PRO
SEQRES 24 B 302 PHE ASN TYR
HET CA A 401 1
HET CL A 402 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 CA CA 2+
FORMUL 4 CL CL 1-
FORMUL 5 HOH *14(H2 O)
HELIX 1 AA1 ILE A 70 ASN A 77 1 8
HELIX 2 AA2 SER A 91 GLY A 111 1 21
HELIX 3 AA3 HIS A 122 MET A 134 1 13
HELIX 4 AA4 SER A 151 ASN A 159 1 9
HELIX 5 AA5 GLY A 162 ALA A 182 1 21
HELIX 6 AA6 ASP A 193 SER A 200 1 8
HELIX 7 AA7 SER A 202 ALA A 211 1 10
HELIX 8 AA8 PHE A 250 ASP A 262 1 13
HELIX 9 AA9 LEU A 291 ASN A 295 5 5
HELIX 10 AB1 ASP A 307 GLN A 322 1 16
HELIX 11 AB2 ASN B 87 THR B 99 1 13
HELIX 12 AB3 ASN B 105 TYR B 121 1 17
HELIX 13 AB4 PRO B 124 GLN B 142 1 19
HELIX 14 AB5 ASP B 155 LYS B 171 1 17
HELIX 15 AB6 SER B 175 ASP B 202 1 28
HELIX 16 AB7 SER B 206 GLU B 219 1 14
HELIX 17 AB8 PRO B 222 SER B 233 1 12
HELIX 18 AB9 SER B 233 ALA B 247 1 15
HELIX 19 AC1 SER B 251 VAL B 263 1 13
HELIX 20 AC2 GLY B 264 HIS B 297 1 34
HELIX 21 AC3 SER B 301 GLN B 315 1 15
HELIX 22 AC4 SER B 319 ASP B 334 1 16
SHEET 1 AA1 6 VAL A 81 THR A 84 0
SHEET 2 AA1 6 LEU A 45 ASN A 48 1 N PHE A 47 O THR A 84
SHEET 3 AA1 6 VAL A 115 HIS A 120 1 O ASN A 116 N VAL A 46
SHEET 4 AA1 6 VAL A 138 ILE A 144 1 O ALA A 139 N VAL A 115
SHEET 5 AA1 6 ILE A 232 PHE A 237 1 O TYR A 235 N LEU A 141
SHEET 6 AA1 6 GLN A 228 GLU A 229 -1 N GLU A 229 O ILE A 232
SHEET 1 AA2 6 VAL A 81 THR A 84 0
SHEET 2 AA2 6 LEU A 45 ASN A 48 1 N PHE A 47 O THR A 84
SHEET 3 AA2 6 VAL A 115 HIS A 120 1 O ASN A 116 N VAL A 46
SHEET 4 AA2 6 VAL A 138 ILE A 144 1 O ALA A 139 N VAL A 115
SHEET 5 AA2 6 ILE A 232 PHE A 237 1 O TYR A 235 N LEU A 141
SHEET 6 AA2 6 LYS A 280 THR A 281 1 O LYS A 280 N MET A 234
SSBOND 1 CYS A 222 CYS A 274 1555 1555 2.06
SSBOND 2 CYS B 74 CYS B 93 1555 1555 2.05
LINK OD2 ASP A 248 CA CA A 401 1555 1555 2.12
LINK OD1 ASP A 292 CA CA A 401 1555 1555 2.27
LINK O GLN A 296 CA CA A 401 1555 1555 2.87
LINK O ILE A 300 CA CA A 401 1555 1555 2.38
CISPEP 1 GLN A 296 VAL A 297 0 1.92
CISPEP 2 GLU B 123 PRO B 124 0 0.16
CRYST1 133.686 133.686 139.715 90.00 90.00 120.00 P 32 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 0.007480 0.004319 0.000000 0.00000
SCALE2 0.000000 0.008637 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007157 0.00000
TER 2221 LEU A 324
TER 4607 TYR B 343
MASTER 346 0 2 22 12 0 0 6 4621 2 9 48
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