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HEADER IMMUNE SYSTEM 17-NOV-22 8F6V
TITLE CRYSTAL STRUCTURE OF NANOBODY VHH108 BOUND TO ITS ANTIGEN PA14 CIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NANOBODY VHH108;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 7 CHAIN: D, C;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS;
SOURCE 3 ORGANISM_TAXID: 30538;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: DE3 RIL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PA14;
SOURCE 11 ORGANISM_TAXID: 652611;
SOURCE 12 GENE: PA2394;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PDPM73
KEYWDS PSEUDOMONAS AERUGINOSA, NANOBODY VHH, IMMUNOGLOBULIN DOMAIN, CFTR
KEYWDS 2 INHIBITORY FACTOR (CIF), IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.SIMARD,D.R.MADDEN
REVDAT 1 13-MAR-24 8F6V 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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 48020
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2417
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 44.2300 - 5.9100 0.99 2752 108 0.1525 0.1599
REMARK 3 2 5.9100 - 4.6900 1.00 2606 232 0.1427 0.1696
REMARK 3 3 4.6900 - 4.1000 1.00 2735 119 0.1315 0.1560
REMARK 3 4 4.1000 - 3.7300 1.00 2703 121 0.1627 0.1936
REMARK 3 5 3.7300 - 3.4600 1.00 2739 122 0.1740 0.2177
REMARK 3 6 3.4600 - 3.2500 1.00 2731 124 0.1980 0.1990
REMARK 3 7 3.2500 - 3.0900 1.00 2679 122 0.2034 0.2338
REMARK 3 8 3.0900 - 2.9600 0.99 2604 250 0.2190 0.2546
REMARK 3 9 2.9600 - 2.8400 0.98 2656 123 0.2221 0.3109
REMARK 3 10 2.8400 - 2.7500 0.99 2677 119 0.2156 0.2752
REMARK 3 11 2.7400 - 2.6600 0.98 2657 122 0.2341 0.2590
REMARK 3 12 2.6600 - 2.5800 0.99 2703 119 0.2432 0.2421
REMARK 3 13 2.5800 - 2.5200 0.99 2679 122 0.2509 0.2635
REMARK 3 14 2.5200 - 2.4500 0.99 2587 239 0.2553 0.2938
REMARK 3 15 2.4500 - 2.4000 0.99 2682 126 0.2663 0.3059
REMARK 3 16 2.4000 - 2.3500 1.00 2697 122 0.2851 0.3395
REMARK 3 17 2.3500 - 2.3000 1.00 2716 127 0.2906 0.3460
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) : 0.279
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.575
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.77
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 : 0.009 6740
REMARK 3 ANGLE : 0.977 9141
REMARK 3 CHIRALITY : 0.060 960
REMARK 3 PLANARITY : 0.008 1204
REMARK 3 DIHEDRAL : 14.124 2449
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1285 -21.7277 -9.9987
REMARK 3 T TENSOR
REMARK 3 T11: 0.4380 T22: 0.4678
REMARK 3 T33: 0.4868 T12: -0.0502
REMARK 3 T13: 0.0418 T23: -0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 3.2938 L22: 2.1674
REMARK 3 L33: 2.1028 L12: 0.3733
REMARK 3 L13: -0.0964 L23: -0.3522
REMARK 3 S TENSOR
REMARK 3 S11: 0.0286 S12: -0.0587 S13: 0.6208
REMARK 3 S21: -0.1596 S22: 0.0108 S23: -0.3027
REMARK 3 S31: -0.4207 S32: 0.4736 S33: -0.0448
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6794 22.9347 10.7186
REMARK 3 T TENSOR
REMARK 3 T11: 0.6628 T22: 0.4915
REMARK 3 T33: 0.5633 T12: 0.0066
REMARK 3 T13: 0.0002 T23: -0.1107
REMARK 3 L TENSOR
REMARK 3 L11: 2.4001 L22: 2.2720
REMARK 3 L33: 1.8721 L12: 0.8544
REMARK 3 L13: -0.1011 L23: -0.8275
REMARK 3 S TENSOR
REMARK 3 S11: -0.0542 S12: -0.3099 S13: 0.1226
REMARK 3 S21: 0.2640 S22: 0.0162 S23: -0.5550
REMARK 3 S31: -0.5094 S32: 0.2874 S33: 0.0285
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1964 -35.3219 -7.6052
REMARK 3 T TENSOR
REMARK 3 T11: 0.3975 T22: 0.3539
REMARK 3 T33: 0.4402 T12: -0.0228
REMARK 3 T13: -0.0880 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 1.7307 L22: 1.6208
REMARK 3 L33: 1.2507 L12: -0.5212
REMARK 3 L13: -0.3400 L23: 0.1216
REMARK 3 S TENSOR
REMARK 3 S11: 0.0632 S12: 0.0578 S13: -0.3786
REMARK 3 S21: -0.0648 S22: 0.0072 S23: 0.2734
REMARK 3 S31: 0.2114 S32: -0.1349 S33: -0.0663
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1209 -2.4612 8.1646
REMARK 3 T TENSOR
REMARK 3 T11: 0.3669 T22: 0.4823
REMARK 3 T33: 0.3892 T12: 0.0597
REMARK 3 T13: 0.0565 T23: 0.0701
REMARK 3 L TENSOR
REMARK 3 L11: 1.5386 L22: 2.1425
REMARK 3 L33: 1.0512 L12: -0.3335
REMARK 3 L13: 0.0055 L23: 0.3313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0253 S12: -0.1791 S13: -0.0610
REMARK 3 S21: 0.1905 S22: 0.0808 S23: 0.4545
REMARK 3 S31: -0.1103 S32: -0.3662 S33: -0.0575
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 8F6V 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_1000270070.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.979312
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 : 48028
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 44.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.08607
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.78330
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.280
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, 8E1B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS I CONDITION G2 (COMPOSITION
REMARK 280 BY MOLECULAR DIMENSIONS STOCK SOLUTIONS WITH CATALOGUE NUMBERS
REMARK 280 LISTED AT END) 20% (V/V) ETHYLENE GLYCOL, 10% (W/V) PEG8000, 20
REMARK 280 MM SODIUM FORMATE, 20 MM AMMONIUM ACETATE, 20 MM SODIUM CITRATE
REMARK 280 TRIBASIC DIHYDRATE, 20 MM POTASSIUM SODIUM TARTRATE TETRAHYDRATE,
REMARK 280 20 MM SODIUM OXAMATE, 100 MM IMIDAZOLE/MES MONOHYDRATE (ACID)
REMARK 280 PH 6.5 STOCK MIXTURES LISTED BELOW WITH CATALOGUE NUMBER IN
REMARK 280 BRACKETS. 30% (V/V) PRECIPITANT MIX 2 [MD2-100-82], 100 MM
REMARK 280 CARBOXYLIC ACIDS MIX [MD2-100-76], 100 MM BUFFER SYSTEM 1 PH 6.5
REMARK 280 [MD2-100-100], VAPOR DIFFUSION, TEMPERATURE 292.8K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 65.66233
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 131.32467
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 98.49350
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 164.15583
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 32.83117
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 APPLY THE FOLLOWING TO CHAINS: A, D, B, C
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 GLU A 3
REMARK 465 SER A 127
REMARK 465 GLY A 128
REMARK 465 GLN A 129
REMARK 465 ALA A 130
REMARK 465 GLY A 131
REMARK 465 GLN A 132
REMARK 465 ALA D 25
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 SER B 126
REMARK 465 SER B 127
REMARK 465 GLY B 128
REMARK 465 GLN B 129
REMARK 465 ALA B 130
REMARK 465 GLY B 131
REMARK 465 GLN B 132
REMARK 465 ALA C 25
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 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 LEU A 13 CG CD1 CD2
REMARK 480 LYS A 44 CE NZ
REMARK 480 LYS D 45 CE NZ
REMARK 480 LYS B 44 CE NZ
REMARK 480 GLU B 62 CG CD OE1 OE2
REMARK 480 GLU B 89 CG CD OE1 OE2
REMARK 480 GLU C 212 CD OE1 OE2
REMARK 480 ARG C 217 CD 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 THR A 104 -101.87 -116.30
REMARK 500 ASP D 42 54.20 38.89
REMARK 500 ASP D 129 -130.27 63.02
REMARK 500 TRP D 298 57.92 -94.08
REMARK 500 THR B 104 -101.46 -111.70
REMARK 500 THR C 99 -74.49 -79.81
REMARK 500 ASP C 129 -138.35 62.60
REMARK 500 TRP C 298 59.13 -93.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 3KD2 CONTAINS CIF PROTEIN
REMARK 900 RELATED ID: 8E1B RELATED DB: PDB
REMARK 900 8E1B CONTAINS NANOBODY VHH108
DBREF 8F6V A 1 132 PDB 8F6V 8F6V 1 132
DBREF1 8F6V D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8F6V D A0A0M3KL26 1 301
DBREF 8F6V B 1 132 PDB 8F6V 8F6V 1 132
DBREF1 8F6V C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 8F6V C A0A0M3KL26 1 301
SEQRES 1 A 132 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 A 132 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS GLU ALA
SEQRES 3 A 132 THR GLY ASN PHE ASP ASP ARG GLY ILE GLY TRP PHE ARG
SEQRES 4 A 132 GLN ALA PRO GLY LYS GLU ARG GLU GLY ILE ALA CYS ILE
SEQRES 5 A 132 THR THR ARG GLY ARG THR HIS TYR ALA GLU SER VAL GLU
SEQRES 6 A 132 GLY ARG PHE THR ILE SER THR ASP ILE ALA ASN ASN ALA
SEQRES 7 A 132 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 A 132 ALA VAL TYR TYR CYS ALA LYS ALA ILE ARG LEU THR THR
SEQRES 9 A 132 ASP ARG THR GLN CYS VAL ALA PHE PRO GLY VAL SER TRP
SEQRES 10 A 132 GLY ARG GLY THR GLN VAL THR VAL SER SER GLY GLN ALA
SEQRES 11 A 132 GLY GLN
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 132 MET ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU
SEQRES 2 B 132 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS GLU ALA
SEQRES 3 B 132 THR GLY ASN PHE ASP ASP ARG GLY ILE GLY TRP PHE ARG
SEQRES 4 B 132 GLN ALA PRO GLY LYS GLU ARG GLU GLY ILE ALA CYS ILE
SEQRES 5 B 132 THR THR ARG GLY ARG THR HIS TYR ALA GLU SER VAL GLU
SEQRES 6 B 132 GLY ARG PHE THR ILE SER THR ASP ILE ALA ASN ASN ALA
SEQRES 7 B 132 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 B 132 ALA VAL TYR TYR CYS ALA LYS ALA ILE ARG LEU THR THR
SEQRES 9 B 132 ASP ARG THR GLN CYS VAL ALA PHE PRO GLY VAL SER TRP
SEQRES 10 B 132 GLY ARG GLY THR GLN VAL THR VAL SER SER GLY GLN ALA
SEQRES 11 B 132 GLY GLN
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
FORMUL 5 HOH *267(H2 O)
HELIX 1 AA1 LYS A 87 THR A 91 5 5
HELIX 2 AA2 THR D 66 HIS D 71 5 6
HELIX 3 AA3 LEU D 73 LYS D 79 1 7
HELIX 4 AA4 SER D 102 GLN D 116 1 15
HELIX 5 AA5 ASP D 129 ASN D 134 1 6
HELIX 6 AA6 THR D 135 ASN D 142 1 8
HELIX 7 AA7 ASP D 158 PHE D 164 5 7
HELIX 8 AA8 TRP D 176 ALA D 183 1 8
HELIX 9 AA9 ARG D 186 ALA D 193 1 8
HELIX 10 AB1 LYS D 195 HIS D 207 1 13
HELIX 11 AB2 SER D 215 LYS D 228 1 14
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 LYS D 281 1 8
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 LYS B 87 THR B 91 5 5
HELIX 18 AB9 THR C 66 HIS C 71 5 6
HELIX 19 AC1 GLN C 72 LYS C 79 1 8
HELIX 20 AC2 SER C 102 SER C 118 1 17
HELIX 21 AC3 ASP C 129 ASN C 142 1 14
HELIX 22 AC4 ASP C 158 PHE C 164 5 7
HELIX 23 AC5 TRP C 176 ALA C 183 1 8
HELIX 24 AC6 ARG C 186 ALA C 193 1 8
HELIX 25 AC7 LYS C 195 HIS C 207 1 13
HELIX 26 AC8 SER C 215 LYS C 228 1 14
HELIX 27 AC9 LYS C 228 ALA C 241 1 14
HELIX 28 AD1 ALA C 241 ALA C 253 1 13
HELIX 29 AD2 THR C 274 LYS C 281 1 8
HELIX 30 AD3 TRP C 298 CYS C 303 1 6
HELIX 31 AD4 CYS C 303 ARG C 317 1 15
SHEET 1 AA1 4 LEU A 6 SER A 9 0
SHEET 2 AA1 4 LEU A 20 ALA A 26 -1 O GLU A 25 N VAL A 7
SHEET 3 AA1 4 ALA A 78 MET A 83 -1 O MET A 83 N LEU A 20
SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82
SHEET 1 AA2 4 GLY A 12 VAL A 14 0
SHEET 2 AA2 4 THR A 121 VAL A 125 1 O THR A 124 N VAL A 14
SHEET 3 AA2 4 ALA A 92 THR A 103 -1 N TYR A 94 O THR A 121
SHEET 4 AA2 4 THR A 107 ALA A 111 -1 O VAL A 110 N ILE A 100
SHEET 1 AA312 THR A 58 TYR A 60 0
SHEET 2 AA312 GLU A 47 ILE A 52 -1 N CYS A 51 O HIS A 59
SHEET 3 AA312 ILE A 35 GLN A 40 -1 N TRP A 37 O ALA A 50
SHEET 4 AA312 ALA A 92 THR A 103 -1 O TYR A 95 N PHE A 38
SHEET 5 AA312 ASP C 286 LEU C 292 1 O VAL C 287 N THR A 103
SHEET 6 AA312 THR C 261 GLY C 266 1 N THR C 261 O ASP C 286
SHEET 7 AA312 ILE C 146 MET C 152 1 N TYR C 151 O MET C 262
SHEET 8 AA312 PHE C 123 HIS C 128 1 N LEU C 125 O VAL C 150
SHEET 9 AA312 LEU C 56 VAL C 60 1 N MET C 58 O ASP C 124
SHEET 10 AA312 THR C 82 PRO C 86 1 O ILE C 84 N VAL C 57
SHEET 11 AA312 VAL C 44 GLY C 51 -1 N GLY C 51 O VAL C 83
SHEET 12 AA312 PHE C 34 VAL C 41 -1 N ARG C 39 O LEU C 46
SHEET 1 AA412 PHE D 34 VAL D 41 0
SHEET 2 AA412 VAL D 44 GLY D 52 -1 O VAL D 44 N VAL D 41
SHEET 3 AA412 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA412 LEU D 56 VAL D 60 1 N VAL D 57 O ILE D 84
SHEET 5 AA412 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 AA412 ILE D 146 MET D 152 1 O VAL D 150 N ALA D 127
SHEET 7 AA412 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA412 ASP D 286 LEU D 292 1 O GLU D 288 N THR D 263
SHEET 9 AA412 ALA B 92 THR B 103 1 O THR B 103 N VAL D 287
SHEET 10 AA412 ILE B 35 GLN B 40 -1 N PHE B 38 O TYR B 95
SHEET 11 AA412 ARG B 46 ILE B 52 -1 O ALA B 50 N TRP B 37
SHEET 12 AA412 THR B 58 TYR B 60 -1 O HIS B 59 N CYS B 51
SHEET 1 AA5 4 GLY B 12 LEU B 13 0
SHEET 2 AA5 4 THR B 121 THR B 124 1 O THR B 124 N GLY B 12
SHEET 3 AA5 4 ALA B 92 THR B 103 -1 N TYR B 94 O THR B 121
SHEET 4 AA5 4 THR B 107 ALA B 111 -1 O VAL B 110 N ILE B 100
SHEET 1 AA6 2 PHE D 167 THR D 168 0
SHEET 2 AA6 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SHEET 1 AA7 4 LEU B 6 SER B 9 0
SHEET 2 AA7 4 LEU B 20 ALA B 26 -1 O SER B 23 N SER B 9
SHEET 3 AA7 4 ALA B 78 MET B 83 -1 O MET B 83 N LEU B 20
SHEET 4 AA7 4 PHE B 68 ASP B 73 -1 N ASP B 73 O ALA B 78
SHEET 1 AA8 2 PHE C 167 THR C 168 0
SHEET 2 AA8 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SSBOND 1 CYS A 24 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 51 CYS A 109 1555 1555 2.07
SSBOND 3 CYS D 295 CYS D 303 1555 1555 2.05
SSBOND 4 CYS B 24 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 51 CYS B 109 1555 1555 2.06
SSBOND 6 CYS C 295 CYS C 303 1555 1555 2.02
CRYST1 98.995 98.995 196.987 90.00 90.00 120.00 P 61 12
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 0.010102 0.005832 0.000000 0.00000
SCALE2 0.000000 0.011664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005076 0.00000
TER 933 SER A 126
TER 3293 ARG D 319
TER 4220 VAL B 125
TER 6569 ARG C 319
MASTER 389 0 0 31 44 0 0 6 6821 4 12 70
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