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HEADER IMMUNE SYSTEM 17-NOV-22 8F6U
TITLE CRYSTAL STRUCTURE OF NANOBODY VHH113 BOUND TO ITS ANTIGEN PA14 CIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: D, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: NANOBODY VHH113;
COMPND 7 CHAIN: B, A;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PA14;
SOURCE 3 ORGANISM_TAXID: 652611;
SOURCE 4 GENE: PA2394;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDPM73;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: VICUGNA PACOS;
SOURCE 12 ORGANISM_TAXID: 30538;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 15 EXPRESSION_SYSTEM_VARIANT: DE3 RIL;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PCOMB3X
KEYWDS PSEUDOMONAS AERUGINOSA, NANOBODY VHH, IMMUNOGLOBULIN DOMAIN, CFTR
KEYWDS 2 INHIBITORY FACTOR (CIF), IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.SIMARD,N.M.TAHER,A.K.MISHRA,D.R.MADDEN
REVDAT 1 13-MAR-24 8F6U 0
JRNL AUTH A.R.SIMARD,D.R.MADDEN
JRNL TITL CRYSTAL STRUCTURE OF NANOBODY VHH113 BOUND TO ITS ANTIGEN
JRNL TITL 2 PA14 CIF
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.VASYLIEVA,S.KITAMURA,J.DONG,B.BARNYCH,K.L.HVORECNY,
REMARK 1 AUTH 2 D.R.MADDEN,S.J.GEE,D.W.WOLAN,C.MORISSEAU,B.D.HAMMOCK
REMARK 1 TITL NANOBODY-BASED BINDING ASSAY FOR THE DISCOVERY OF POTENT
REMARK 1 TITL 2 INHIBITORS OF CFTR INHIBITORY FACTOR (CIF).
REMARK 1 REF ANAL CHIM ACTA V.1057 106 2019
REMARK 1 REFN ISSN 1873-4324
REMARK 1 PMID 30832908
REMARK 1 DOI 10.1016/J.ACA.2018.12.060
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,
REMARK 1 AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,
REMARK 1 AUTH 3 P.H.ZWART,P.D.ADAMS
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR D BIOL V. 68 352 2012
REMARK 1 REF 2 CRYSTALLOGR
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 22505256
REMARK 1 DOI 10.1107/S0907444912001308
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 124297
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 : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 6228
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 46.4900 - 5.2800 0.99 4088 317 0.1774 0.1811
REMARK 3 2 5.2800 - 4.1900 0.99 4228 25 0.1344 0.1852
REMARK 3 3 4.1900 - 3.6600 0.99 3927 296 0.1471 0.1612
REMARK 3 4 3.6600 - 3.3300 1.00 3920 288 0.1560 0.1683
REMARK 3 5 3.3300 - 3.0900 0.99 4117 97 0.1666 0.1689
REMARK 3 6 3.0900 - 2.9100 0.99 3912 261 0.1836 0.1996
REMARK 3 7 2.9100 - 2.7600 0.99 3921 217 0.1818 0.2122
REMARK 3 8 2.7600 - 2.6400 0.99 3986 180 0.1774 0.2014
REMARK 3 9 2.6400 - 2.5400 0.99 3935 209 0.1771 0.1961
REMARK 3 10 2.5400 - 2.4500 0.99 3929 219 0.1812 0.2333
REMARK 3 11 2.4500 - 2.3800 0.99 3929 208 0.1787 0.1885
REMARK 3 12 2.3800 - 2.3100 0.99 3948 205 0.1708 0.2094
REMARK 3 13 2.3100 - 2.2500 0.99 3917 204 0.1712 0.1935
REMARK 3 14 2.2500 - 2.1900 0.99 3932 211 0.1722 0.1799
REMARK 3 15 2.1900 - 2.1400 0.99 3884 224 0.1760 0.1934
REMARK 3 16 2.1400 - 2.1000 0.99 3944 180 0.1810 0.2356
REMARK 3 17 2.1000 - 2.0500 0.99 3915 222 0.1864 0.2098
REMARK 3 18 2.0500 - 2.0200 0.99 3901 210 0.1919 0.2104
REMARK 3 19 2.0200 - 1.9800 0.99 3930 189 0.1945 0.2051
REMARK 3 20 1.9800 - 1.9500 0.99 3871 238 0.1952 0.2359
REMARK 3 21 1.9500 - 1.9100 0.99 3919 166 0.2124 0.2313
REMARK 3 22 1.9100 - 1.8900 0.99 3911 209 0.2269 0.2641
REMARK 3 23 1.8900 - 1.8600 0.99 3891 220 0.2460 0.2971
REMARK 3 24 1.8600 - 1.8300 0.99 3895 203 0.2573 0.2710
REMARK 3 25 1.8300 - 1.8100 0.99 3894 210 0.2580 0.2985
REMARK 3 26 1.8100 - 1.7800 0.99 3912 209 0.2548 0.2871
REMARK 3 27 1.7800 - 1.7600 0.98 3845 218 0.2648 0.3057
REMARK 3 28 1.7600 - 1.7400 0.99 3891 192 0.2844 0.2712
REMARK 3 29 1.7400 - 1.7200 0.99 3897 220 0.3018 0.3763
REMARK 3 30 1.7200 - 1.7000 0.98 3880 181 0.3142 0.3408
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) : 0.192
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.409
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.61
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 6812
REMARK 3 ANGLE : 0.839 9259
REMARK 3 CHIRALITY : 0.055 965
REMARK 3 PLANARITY : 0.008 1221
REMARK 3 DIHEDRAL : 12.868 2439
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: ATOMS MODELED WITH ZERO OCCUPANCY COULD
REMARK 3 NOT BE PLACED WITH CONFIDENCE AND WERE SELECTED FOR ZERO-
REMARK 3 OCCUPANCY FLAGGING AFTER MANUAL INSPECTION OF THE 2FO-FC MAP AT
REMARK 3 A 0.5-SIGMA CUTOFF.
REMARK 4
REMARK 4 8F6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1000270064.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS-II
REMARK 200 BEAMLINE : 17-ID-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979339
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 124313
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.10670
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 1.64600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.260
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: 3KD2, 8E1C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM POTASSIUM BROMIDE, 200 MM
REMARK 280 POTASSIUM THIOCYANATE, 100 MM SODIUM ACETATE PH 5, 3% (W/V)
REMARK 280 GAMMA-PGA (NA+ FORM, LM), 10% (W/V) PEG 2000 MME, PH 5.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 292.8K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 53.37650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.37650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 57.59250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 92.97050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 57.59250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 92.97050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.37650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 57.59250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 92.97050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.37650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 57.59250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 92.97050
REMARK 290 SMTRY3 8 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, B, C, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 402 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 271 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 329 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 331 LIES ON A SPECIAL POSITION.
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 D 318
REMARK 465 ARG D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 VAL B 4
REMARK 465 GLN B 5
REMARK 465 GLY B 130
REMARK 465 GLN B 131
REMARK 465 ALA B 132
REMARK 465 GLY B 133
REMARK 465 GLN B 134
REMARK 465 HIS B 135
REMARK 465 HIS B 136
REMARK 465 HIS B 137
REMARK 465 HIS B 138
REMARK 465 HIS B 139
REMARK 465 HIS B 140
REMARK 465 GLY B 141
REMARK 465 ALA B 142
REMARK 465 TYR B 143
REMARK 465 PRO B 144
REMARK 465 TYR B 145
REMARK 465 ASP B 146
REMARK 465 VAL B 147
REMARK 465 PRO B 148
REMARK 465 ASP B 149
REMARK 465 TYR B 150
REMARK 465 ALA B 151
REMARK 465 SER B 152
REMARK 465 GLY B 153
REMARK 465 SER B 154
REMARK 465 ALA C 25
REMARK 465 ARG C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLY A 130
REMARK 465 GLN A 131
REMARK 465 ALA A 132
REMARK 465 GLY A 133
REMARK 465 GLN A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 GLY A 141
REMARK 465 ALA A 142
REMARK 465 TYR A 143
REMARK 465 PRO A 144
REMARK 465 TYR A 145
REMARK 465 ASP A 146
REMARK 465 VAL A 147
REMARK 465 PRO A 148
REMARK 465 ASP A 149
REMARK 465 TYR A 150
REMARK 465 ALA A 151
REMARK 465 SER A 152
REMARK 465 GLY A 153
REMARK 465 SER A 154
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN D 53 CD OE1 NE2
REMARK 480 GLU D 212 CG CD OE1 OE2
REMARK 480 LYS C 45 CE NZ
REMARK 480 ARG C 121 NE CZ NH1 NH2
REMARK 480 GLU C 212 CG CD OE1 OE2
REMARK 480 GLU C 285 CD OE1 OE2
REMARK 480 ARG C 309 NE CZ NH1 NH2
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 ASP D 129 -131.82 57.07
REMARK 500 TRP D 298 68.73 -100.69
REMARK 500 ASP C 129 -131.86 58.00
REMARK 500 ALA C 154 147.97 -176.91
REMARK 500 ALA A 97 165.80 175.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 338 DISTANCE = 5.86 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 3KD2 CONTAINS CIF
REMARK 900 RELATED ID: 8E2N RELATED DB: PDB
REMARK 900 8E2N CONTAINS NANOBODY VHH113
REMARK 900 RELATED ID: 8ELN RELATED DB: PDB
REMARK 900 8ELN CONTAINS CIF CO-CRYSTALIZED WITH RELATED NANOBODY VHH222
REMARK 900 RELATED ID: 8EVD RELATED DB: PDB
REMARK 900 8EVD CONTAINS CIF CO-CRYSTALIZED WITH RELATED NANOBODY VHH101
REMARK 900 RELATED ID: 8EE2 RELATED DB: PDB
REMARK 900 8EE2 ONTAINS CIF CO-CRYSTALIZED WITH RELATED NANOBODY VHH219
DBREF1 8F6U D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8F6U D A0A0M3KL26 1 301
DBREF 8F6U B 1 154 PDB 8F6U 8F6U 1 154
DBREF1 8F6U C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8F6U C A0A0M3KL26 1 301
DBREF 8F6U A 1 154 PDB 8F6U 8F6U 1 154
SEQRES 1 D 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 D 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 D 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 D 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 D 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 D 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 D 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 D 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 D 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 D 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 D 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 D 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 D 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 D 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 D 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 D 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 D 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 D 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 D 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 D 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 D 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 D 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 D 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 D 301 HIS HIS
SEQRES 1 B 154 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 B 154 VAL PRO ALA GLY GLY SER LEU ARG LEU SER CYS THR THR
SEQRES 3 B 154 SER GLU ARG ALA PHE ARG SER ASN ALA MET GLY TRP PHE
SEQRES 4 B 154 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 B 154 VAL SER VAL LEU SER TRP SER GLY ASP SER ALA VAL VAL
SEQRES 6 B 154 ALA ASP SER VAL ALA GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 B 154 ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 B 154 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 B 154 SER ASP ILE GLY ALA LEU GLN SER GLY ALA SER SER TRP
SEQRES 10 B 154 SER TRP GLY HIS GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 B 154 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 B 154 PRO TYR ASP VAL PRO ASP TYR ALA SER GLY SER
SEQRES 1 C 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 C 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 C 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 C 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 C 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 C 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 C 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 C 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 C 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 C 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 C 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 C 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 C 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 C 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 C 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 C 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 C 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 C 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 C 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 C 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 C 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 C 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 C 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 C 301 HIS HIS
SEQRES 1 A 154 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 A 154 VAL PRO ALA GLY GLY SER LEU ARG LEU SER CYS THR THR
SEQRES 3 A 154 SER GLU ARG ALA PHE ARG SER ASN ALA MET GLY TRP PHE
SEQRES 4 A 154 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA
SEQRES 5 A 154 VAL SER VAL LEU SER TRP SER GLY ASP SER ALA VAL VAL
SEQRES 6 A 154 ALA ASP SER VAL ALA GLY ARG PHE THR ILE PHE ARG ASP
SEQRES 7 A 154 ASN ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU
SEQRES 8 A 154 LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN GLY ALA
SEQRES 9 A 154 SER ASP ILE GLY ALA LEU GLN SER GLY ALA SER SER TRP
SEQRES 10 A 154 SER TRP GLY HIS GLY THR GLN VAL THR VAL SER SER GLY
SEQRES 11 A 154 GLN ALA GLY GLN HIS HIS HIS HIS HIS HIS GLY ALA TYR
SEQRES 12 A 154 PRO TYR ASP VAL PRO ASP TYR ALA SER GLY SER
FORMUL 5 HOH *784(H2 O)
HELIX 1 AA1 THR D 66 HIS D 71 5 6
HELIX 2 AA2 LEU D 73 ALA D 78 1 6
HELIX 3 AA3 SER D 102 SER D 118 1 17
HELIX 4 AA4 ASP D 129 ASN D 134 1 6
HELIX 5 AA5 THR D 135 ASN D 142 1 8
HELIX 6 AA6 ASP D 158 PHE D 164 5 7
HELIX 7 AA7 TRP D 176 ALA D 183 1 8
HELIX 8 AA8 ARG D 186 ALA D 193 1 8
HELIX 9 AA9 LYS D 195 HIS D 207 1 13
HELIX 10 AB1 ASN D 210 PHE D 214 5 5
HELIX 11 AB2 SER D 215 ALA D 227 1 13
HELIX 12 AB3 LYS D 228 ALA D 241 1 14
HELIX 13 AB4 ALA D 241 ALA D 253 1 13
HELIX 14 AB5 THR D 274 ALA D 282 1 9
HELIX 15 AB6 TRP D 298 CYS D 303 1 6
HELIX 16 AB7 CYS D 303 ARG D 317 1 15
HELIX 17 AB8 SER B 27 SER B 33 1 7
HELIX 18 AB9 LYS B 92 THR B 96 5 5
HELIX 19 AC1 ASP B 106 GLY B 113 1 8
HELIX 20 AC2 THR C 66 HIS C 71 5 6
HELIX 21 AC3 LEU C 73 ALA C 78 1 6
HELIX 22 AC4 SER C 102 SER C 118 1 17
HELIX 23 AC5 ASP C 129 ASN C 134 1 6
HELIX 24 AC6 THR C 135 ASN C 142 1 8
HELIX 25 AC7 ASP C 158 PHE C 164 5 7
HELIX 26 AC8 TRP C 176 ALA C 183 1 8
HELIX 27 AC9 ARG C 186 ALA C 193 1 8
HELIX 28 AD1 LYS C 195 HIS C 207 1 13
HELIX 29 AD2 ASN C 210 PHE C 214 5 5
HELIX 30 AD3 SER C 215 ALA C 227 1 13
HELIX 31 AD4 LYS C 228 ALA C 241 1 14
HELIX 32 AD5 ALA C 241 ALA C 253 1 13
HELIX 33 AD6 THR C 274 LYS C 281 1 8
HELIX 34 AD7 TRP C 298 CYS C 303 1 6
HELIX 35 AD8 CYS C 303 SER C 316 1 14
HELIX 36 AD9 SER A 27 SER A 33 1 7
HELIX 37 AE1 ASN A 79 LYS A 81 5 3
HELIX 38 AE2 LYS A 92 THR A 96 5 5
HELIX 39 AE3 ASP A 106 GLY A 113 1 8
SHEET 1 AA1 8 GLU D 35 VAL D 41 0
SHEET 2 AA1 8 VAL D 44 GLY D 52 -1 O LYS D 50 N GLU D 35
SHEET 3 AA1 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA1 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA1 8 PHE D 123 HIS D 128 1 O ASP D 124 N LEU D 56
SHEET 6 AA1 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA1 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA1 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA2 2 PHE D 167 THR D 168 0
SHEET 2 AA2 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SHEET 1 AA3 4 VAL B 7 SER B 9 0
SHEET 2 AA3 4 LEU B 20 THR B 25 -1 O THR B 25 N VAL B 7
SHEET 3 AA3 4 THR B 83 MET B 88 -1 O MET B 88 N LEU B 20
SHEET 4 AA3 4 PHE B 73 ASP B 78 -1 N PHE B 76 O TYR B 85
SHEET 1 AA4 6 GLY B 12 PRO B 15 0
SHEET 2 AA4 6 THR B 123 SER B 128 1 O THR B 126 N VAL B 14
SHEET 3 AA4 6 ALA B 97 ALA B 104 -1 N TYR B 99 O THR B 123
SHEET 4 AA4 6 ALA B 35 GLN B 41 -1 N PHE B 39 O TYR B 100
SHEET 5 AA4 6 GLU B 48 VAL B 53 -1 O GLU B 48 N ARG B 40
SHEET 6 AA4 6 ALA B 63 VAL B 65 -1 O VAL B 64 N ALA B 52
SHEET 1 AA5 8 PHE C 34 VAL C 41 0
SHEET 2 AA5 8 VAL C 44 GLY C 52 -1 O LEU C 46 N ARG C 39
SHEET 3 AA5 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA5 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA5 8 PHE C 123 HIS C 128 1 O ASP C 124 N LEU C 56
SHEET 6 AA5 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
SHEET 7 AA5 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA5 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA6 2 PHE C 167 THR C 168 0
SHEET 2 AA6 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 AA7 4 VAL A 7 SER A 9 0
SHEET 2 AA7 4 LEU A 20 THR A 25 -1 O SER A 23 N SER A 9
SHEET 3 AA7 4 THR A 83 MET A 88 -1 O MET A 88 N LEU A 20
SHEET 4 AA7 4 PHE A 73 ASP A 78 -1 N ASP A 78 O THR A 83
SHEET 1 AA8 6 LEU A 13 PRO A 15 0
SHEET 2 AA8 6 THR A 123 SER A 128 1 O THR A 126 N VAL A 14
SHEET 3 AA8 6 ALA A 97 ALA A 104 -1 N TYR A 99 O THR A 123
SHEET 4 AA8 6 ALA A 35 GLN A 41 -1 N ALA A 35 O ALA A 104
SHEET 5 AA8 6 GLU A 48 VAL A 53 -1 O ALA A 51 N TRP A 38
SHEET 6 AA8 6 ALA A 63 VAL A 65 -1 O VAL A 64 N ALA A 52
SSBOND 1 CYS D 295 CYS D 303 1555 1555 2.02
SSBOND 2 CYS B 24 CYS B 101 1555 1555 2.04
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.21
SSBOND 4 CYS A 24 CYS A 101 1555 1555 2.02
CRYST1 115.185 185.941 106.753 90.00 90.00 90.00 C 2 2 21 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 0.008682 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009367 0.00000
TER 2373 ARG D 317
TER 3303 SER B 129
TER 5682 GLY C 318
TER 6624 SER A 129
MASTER 416 0 0 39 40 0 0 6 7311 4 8 72
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