HEADER STRUCTURAL PROTEIN 04-FEB-24 8RWF TITLE DOMAINS 1 AND 2 OF BACILLUS ANTHRACIS SAP S-LAYER IN COMPLEX WITH TITLE 2 NB692 COMPND MOL_ID: 1; COMPND 2 MOLECULE: S-LAYER PROTEIN SAP; COMPND 3 CHAIN: A, B, D; COMPND 4 SYNONYM: SURFACE ARRAY PROTEIN,SURFACE LAYER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SAP BINDING NANOBODY 692; COMPND 8 CHAIN: C, E, G; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS; SOURCE 3 ORGANISM_TAXID: 1392; SOURCE 4 GENE: SAP, BA_0885, GBAA_0885, BAS0841; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 9 ORGANISM_TAXID: 9844; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS S-LAYER, NANOBODY, ANTHRAX, STRUCTURAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.SOGUES,H.REMAUT REVDAT 1 20-NOV-24 8RWF 0 JRNL AUTH A.SOGUES,H.REMAUT JRNL TITL MOLECULAR DYNAMICS AND MACHINE LEARNING STRATIFY JRNL TITL 2 MOTION-DEPENDENT ACTIVITY PROFILES OF S-LAYER DESTABILIZING JRNL TITL 3 NANOBODIES JRNL REF TO BE PUBLISHED 2024 JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.11 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21_5207 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) : 3.11 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 106.63 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 22681 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.224 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.285 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 1143 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1106.6300 - 6.2300 1.00 2886 167 0.1897 0.2615 REMARK 3 2 6.2300 - 4.9400 1.00 2724 136 0.1917 0.2579 REMARK 3 3 4.9400 - 4.3200 1.00 2690 148 0.1717 0.2247 REMARK 3 4 4.3200 - 3.9200 1.00 2652 155 0.2020 0.2499 REMARK 3 5 3.9200 - 3.6400 1.00 2649 143 0.2400 0.3355 REMARK 3 6 3.6400 - 3.4300 1.00 2656 141 0.2583 0.3175 REMARK 3 7 3.4300 - 3.2600 1.00 2629 136 0.2966 0.3754 REMARK 3 8 3.2600 - 3.1100 1.00 2652 117 0.3188 0.3794 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) : 0.496 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.171 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.99 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.02 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 6517 REMARK 3 ANGLE : 1.171 8795 REMARK 3 CHIRALITY : 0.063 1050 REMARK 3 PLANARITY : 0.007 1120 REMARK 3 DIHEDRAL : 15.077 2391 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 : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 216 through 285 or REMARK 3 (resid 286 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 287 REMARK 3 through 384)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 216 through 285 or REMARK 3 (resid 286 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 287 REMARK 3 through 384)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 1 through 18 or REMARK 3 (resid 19 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 20 REMARK 3 through 103 or (resid 104 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 105 through 118)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 1 through 42 or REMARK 3 (resid 43 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 44 REMARK 3 through 118)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "G" and (resid 1 through 18 or REMARK 3 (resid 19 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 20 REMARK 3 through 42 or (resid 43 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 44 through 103 or (resid 104 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 105 through 118)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8RWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1292136345. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-JAN-22 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 : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9179 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22681 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.110 REMARK 200 RESOLUTION RANGE LOW (A) : 106.630 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 26.60 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.22 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.22 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL 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 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.16 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CHLORIDE, 0.1 M HEPES REMARK 280 (PH 7.5) AND 25% V/V GLYCEROL ETHOXYLATE, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 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 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 26.63350 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 106.63200 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 106.63200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.95025 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 106.63200 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 106.63200 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 13.31675 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 106.63200 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 106.63200 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.95025 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 106.63200 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 106.63200 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 13.31675 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 26.63350 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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 APPLY THE FOLLOWING TO CHAINS: A, G 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E 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 MSE A 208 REMARK 465 HIS A 209 REMARK 465 HIS A 210 REMARK 465 HIS A 211 REMARK 465 HIS A 212 REMARK 465 HIS A 213 REMARK 465 HIS A 214 REMARK 465 GLU A 215 REMARK 465 MSE B 208 REMARK 465 HIS B 209 REMARK 465 HIS B 210 REMARK 465 HIS B 211 REMARK 465 HIS B 212 REMARK 465 HIS B 213 REMARK 465 HIS B 214 REMARK 465 GLU B 215 REMARK 465 HIS C 119 REMARK 465 HIS C 120 REMARK 465 HIS C 121 REMARK 465 HIS C 122 REMARK 465 HIS C 123 REMARK 465 HIS C 124 REMARK 465 MSE D 208 REMARK 465 HIS D 209 REMARK 465 HIS D 210 REMARK 465 HIS D 211 REMARK 465 HIS D 212 REMARK 465 HIS D 213 REMARK 465 HIS D 214 REMARK 465 GLU D 215 REMARK 465 HIS E 119 REMARK 465 HIS E 120 REMARK 465 HIS E 121 REMARK 465 HIS E 122 REMARK 465 HIS E 123 REMARK 465 HIS E 124 REMARK 465 HIS G 119 REMARK 465 HIS G 120 REMARK 465 HIS G 121 REMARK 465 HIS G 122 REMARK 465 HIS G 123 REMARK 465 HIS G 124 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 286 CG CD CE NZ REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 ARG E 19 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 104 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 E 205 O HOH E 213 1.82 REMARK 500 O ILE C 28 O HOH C 201 1.97 REMARK 500 O HOH B 401 O HOH B 411 1.98 REMARK 500 O LYS E 43 O HOH E 201 2.10 REMARK 500 O HOH A 423 O HOH G 215 2.12 REMARK 500 O ILE B 345 O HOH B 401 2.13 REMARK 500 OE2 GLU D 303 O HOH D 401 2.14 REMARK 500 OD2 ASP A 368 O HOH A 401 2.17 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 LYS A 263 16.30 59.76 REMARK 500 VAL A 287 -50.70 -130.33 REMARK 500 GLU A 343 2.26 -69.33 REMARK 500 SER B 230 31.14 -81.12 REMARK 500 LYS B 231 149.98 -177.41 REMARK 500 LYS B 263 19.75 59.22 REMARK 500 VAL B 287 -54.54 -132.48 REMARK 500 ASN C 32 -125.45 -82.94 REMARK 500 VAL C 48 -60.03 -105.41 REMARK 500 LEU C 102 -81.55 -119.42 REMARK 500 LYS D 263 16.23 57.25 REMARK 500 VAL D 287 -52.96 -128.84 REMARK 500 ASP D 312 9.86 59.58 REMARK 500 ASP E 33 124.03 83.40 REMARK 500 VAL E 48 -61.42 -105.21 REMARK 500 ASP G 33 133.30 90.58 REMARK 500 THR G 90 106.06 -59.78 REMARK 500 REMARK 500 REMARK: NULL DBREF 8RWF A 215 384 UNP P49051 SLAP1_BACAN 215 384 DBREF 8RWF B 215 384 UNP P49051 SLAP1_BACAN 215 384 DBREF 8RWF C 1 124 PDB 8RWF 8RWF 1 124 DBREF 8RWF D 215 384 UNP P49051 SLAP1_BACAN 215 384 DBREF 8RWF E 1 124 PDB 8RWF 8RWF 1 124 DBREF 8RWF G 1 124 PDB 8RWF 8RWF 1 124 SEQADV 8RWF MSE A 208 UNP P49051 INITIATING METHIONINE SEQADV 8RWF HIS A 209 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS A 210 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS A 211 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS A 212 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS A 213 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS A 214 UNP P49051 EXPRESSION TAG SEQADV 8RWF MSE B 208 UNP P49051 INITIATING METHIONINE SEQADV 8RWF HIS B 209 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS B 210 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS B 211 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS B 212 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS B 213 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS B 214 UNP P49051 EXPRESSION TAG SEQADV 8RWF MSE D 208 UNP P49051 INITIATING METHIONINE SEQADV 8RWF HIS D 209 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS D 210 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS D 211 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS D 212 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS D 213 UNP P49051 EXPRESSION TAG SEQADV 8RWF HIS D 214 UNP P49051 EXPRESSION TAG SEQRES 1 A 177 MSE HIS HIS HIS HIS HIS HIS GLU SER ALA LYS ALA VAL SEQRES 2 A 177 THR THR GLN LYS VAL GLU VAL LYS PHE SER LYS ALA VAL SEQRES 3 A 177 GLU LYS LEU THR LYS GLU ASP ILE LYS VAL THR ASN LYS SEQRES 4 A 177 ALA ASN ASN ASP LYS VAL LEU VAL LYS GLU VAL THR LEU SEQRES 5 A 177 SER GLU ASP LYS LYS SER ALA THR VAL GLU LEU TYR SER SEQRES 6 A 177 ASN LEU ALA ALA LYS GLN THR TYR THR VAL ASP VAL ASN SEQRES 7 A 177 LYS VAL GLY LYS THR GLU VAL ALA VAL GLY SER LEU GLU SEQRES 8 A 177 ALA LYS THR ILE GLU MSE ALA ASP GLN THR VAL VAL ALA SEQRES 9 A 177 ASP GLU PRO THR ALA LEU GLN PHE THR VAL LYS ASP GLU SEQRES 10 A 177 ASN GLY THR GLU VAL VAL SER PRO GLU GLY ILE GLU PHE SEQRES 11 A 177 VAL THR PRO ALA ALA GLU LYS ILE ASN ALA LYS GLY GLU SEQRES 12 A 177 ILE THR LEU ALA LYS GLY THR SER THR THR VAL LYS ALA SEQRES 13 A 177 VAL TYR LYS LYS ASP GLY LYS VAL VAL ALA GLU SER LYS SEQRES 14 A 177 GLU VAL LYS VAL SER ALA GLU GLY SEQRES 1 B 177 MSE HIS HIS HIS HIS HIS HIS GLU SER ALA LYS ALA VAL SEQRES 2 B 177 THR THR GLN LYS VAL GLU VAL LYS PHE SER LYS ALA VAL SEQRES 3 B 177 GLU LYS LEU THR LYS GLU ASP ILE LYS VAL THR ASN LYS SEQRES 4 B 177 ALA ASN ASN ASP LYS VAL LEU VAL LYS GLU VAL THR LEU SEQRES 5 B 177 SER GLU ASP LYS LYS SER ALA THR VAL GLU LEU TYR SER SEQRES 6 B 177 ASN LEU ALA ALA LYS GLN THR TYR THR VAL ASP VAL ASN SEQRES 7 B 177 LYS VAL GLY LYS THR GLU VAL ALA VAL GLY SER LEU GLU SEQRES 8 B 177 ALA LYS THR ILE GLU MSE ALA ASP GLN THR VAL VAL ALA SEQRES 9 B 177 ASP GLU PRO THR ALA LEU GLN PHE THR VAL LYS ASP GLU SEQRES 10 B 177 ASN GLY THR GLU VAL VAL SER PRO GLU GLY ILE GLU PHE SEQRES 11 B 177 VAL THR PRO ALA ALA GLU LYS ILE ASN ALA LYS GLY GLU SEQRES 12 B 177 ILE THR LEU ALA LYS GLY THR SER THR THR VAL LYS ALA SEQRES 13 B 177 VAL TYR LYS LYS ASP GLY LYS VAL VAL ALA GLU SER LYS SEQRES 14 B 177 GLU VAL LYS VAL SER ALA GLU GLY SEQRES 1 C 124 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 124 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 124 SER ILE PHE ARG ILE ASN ASP MET GLY TRP TYR ARG GLN SEQRES 4 C 124 ALA THR GLY LYS GLN ARG GLU LEU VAL ALA VAL ILE THR SEQRES 5 C 124 SER GLY GLY SER ALA ASN TYR ALA ASP SER VAL LYS GLY SEQRES 6 C 124 ARG PHE SER ILE SER ARG ASP ASN ALA LYS LYS ALA VAL SEQRES 7 C 124 TYR LEU ARG MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 C 124 VAL TYR TYR CYS ASN ALA ASP PHE GLY THR LEU GLY ARG SEQRES 9 C 124 TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 C 124 SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 177 MSE HIS HIS HIS HIS HIS HIS GLU SER ALA LYS ALA VAL SEQRES 2 D 177 THR THR GLN LYS VAL GLU VAL LYS PHE SER LYS ALA VAL SEQRES 3 D 177 GLU LYS LEU THR LYS GLU ASP ILE LYS VAL THR ASN LYS SEQRES 4 D 177 ALA ASN ASN ASP LYS VAL LEU VAL LYS GLU VAL THR LEU SEQRES 5 D 177 SER GLU ASP LYS LYS SER ALA THR VAL GLU LEU TYR SER SEQRES 6 D 177 ASN LEU ALA ALA LYS GLN THR TYR THR VAL ASP VAL ASN SEQRES 7 D 177 LYS VAL GLY LYS THR GLU VAL ALA VAL GLY SER LEU GLU SEQRES 8 D 177 ALA LYS THR ILE GLU MSE ALA ASP GLN THR VAL VAL ALA SEQRES 9 D 177 ASP GLU PRO THR ALA LEU GLN PHE THR VAL LYS ASP GLU SEQRES 10 D 177 ASN GLY THR GLU VAL VAL SER PRO GLU GLY ILE GLU PHE SEQRES 11 D 177 VAL THR PRO ALA ALA GLU LYS ILE ASN ALA LYS GLY GLU SEQRES 12 D 177 ILE THR LEU ALA LYS GLY THR SER THR THR VAL LYS ALA SEQRES 13 D 177 VAL TYR LYS LYS ASP GLY LYS VAL VAL ALA GLU SER LYS SEQRES 14 D 177 GLU VAL LYS VAL SER ALA GLU GLY SEQRES 1 E 124 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 124 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 124 SER ILE PHE ARG ILE ASN ASP MET GLY TRP TYR ARG GLN SEQRES 4 E 124 ALA THR GLY LYS GLN ARG GLU LEU VAL ALA VAL ILE THR SEQRES 5 E 124 SER GLY GLY SER ALA ASN TYR ALA ASP SER VAL LYS GLY SEQRES 6 E 124 ARG PHE SER ILE SER ARG ASP ASN ALA LYS LYS ALA VAL SEQRES 7 E 124 TYR LEU ARG MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 E 124 VAL TYR TYR CYS ASN ALA ASP PHE GLY THR LEU GLY ARG SEQRES 9 E 124 TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 E 124 SER HIS HIS HIS HIS HIS HIS SEQRES 1 G 124 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 124 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 124 SER ILE PHE ARG ILE ASN ASP MET GLY TRP TYR ARG GLN SEQRES 4 G 124 ALA THR GLY LYS GLN ARG GLU LEU VAL ALA VAL ILE THR SEQRES 5 G 124 SER GLY GLY SER ALA ASN TYR ALA ASP SER VAL LYS GLY SEQRES 6 G 124 ARG PHE SER ILE SER ARG ASP ASN ALA LYS LYS ALA VAL SEQRES 7 G 124 TYR LEU ARG MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 G 124 VAL TYR TYR CYS ASN ALA ASP PHE GLY THR LEU GLY ARG SEQRES 9 G 124 TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 G 124 SER HIS HIS HIS HIS HIS HIS MODRES 8RWF MSE A 304 MET MODIFIED RESIDUE MODRES 8RWF MSE B 304 MET MODIFIED RESIDUE MODRES 8RWF MSE D 304 MET MODIFIED RESIDUE HET MSE A 304 8 HET MSE B 304 8 HET MSE D 304 8 HETNAM MSE SELENOMETHIONINE FORMUL 1 MSE 3(C5 H11 N O2 SE) FORMUL 7 HOH *102(H2 O) HELIX 1 AA1 THR A 237 GLU A 239 5 3 HELIX 2 AA2 ALA A 341 ILE A 345 5 5 HELIX 3 AA3 ALA B 341 ILE B 345 5 5 HELIX 4 AA4 LYS C 86 THR C 90 5 5 HELIX 5 AA5 ALA D 341 ILE D 345 5 5 HELIX 6 AA6 LYS E 86 THR E 90 5 5 HELIX 7 AA7 LYS G 86 THR G 90 5 5 SHEET 1 AA1 4 ALA A 217 ALA A 219 0 SHEET 2 AA1 4 LYS A 224 LYS A 228 -1 O GLU A 226 N LYS A 218 SHEET 3 AA1 4 SER A 265 LEU A 270 -1 O VAL A 268 N VAL A 225 SHEET 4 AA1 4 VAL A 254 LEU A 259 -1 N LYS A 255 O GLU A 269 SHEET 1 AA2 4 LYS A 251 VAL A 252 0 SHEET 2 AA2 4 ILE A 241 ASN A 245 -1 N VAL A 243 O VAL A 252 SHEET 3 AA2 4 THR A 279 VAL A 284 -1 O ASP A 283 N LYS A 242 SHEET 4 AA2 4 GLY A 288 ALA A 293 -1 O VAL A 292 N TYR A 280 SHEET 1 AA3 3 THR A 301 GLU A 303 0 SHEET 2 AA3 3 THR A 320 LYS A 322 -1 O THR A 320 N GLU A 303 SHEET 3 AA3 3 GLU A 328 VAL A 329 -1 O VAL A 329 N VAL A 321 SHEET 1 AA4 4 GLN A 307 VAL A 310 0 SHEET 2 AA4 4 VAL A 378 GLU A 383 1 O SER A 381 N VAL A 309 SHEET 3 AA4 4 SER A 358 LYS A 367 -1 N VAL A 361 O VAL A 378 SHEET 4 AA4 4 ILE A 335 VAL A 338 -1 N VAL A 338 O LYS A 362 SHEET 1 AA5 4 GLN A 307 VAL A 310 0 SHEET 2 AA5 4 VAL A 378 GLU A 383 1 O SER A 381 N VAL A 309 SHEET 3 AA5 4 SER A 358 LYS A 367 -1 N VAL A 361 O VAL A 378 SHEET 4 AA5 4 LYS A 370 GLU A 374 -1 O LYS A 370 N LYS A 367 SHEET 1 AA6 2 THR A 315 ALA A 316 0 SHEET 2 AA6 2 GLU A 350 ILE A 351 -1 O ILE A 351 N THR A 315 SHEET 1 AA7 4 ALA B 217 ALA B 219 0 SHEET 2 AA7 4 LYS B 224 LYS B 228 -1 O GLU B 226 N LYS B 218 SHEET 3 AA7 4 SER B 265 LEU B 270 -1 O VAL B 268 N VAL B 225 SHEET 4 AA7 4 VAL B 254 LEU B 259 -1 N GLU B 256 O GLU B 269 SHEET 1 AA8 4 LYS B 251 VAL B 252 0 SHEET 2 AA8 4 ILE B 241 ASN B 245 -1 N VAL B 243 O VAL B 252 SHEET 3 AA8 4 THR B 279 VAL B 284 -1 O ASP B 283 N LYS B 242 SHEET 4 AA8 4 GLY B 288 ALA B 293 -1 O VAL B 292 N TYR B 280 SHEET 1 AA9 3 THR B 301 GLU B 303 0 SHEET 2 AA9 3 THR B 320 LYS B 322 -1 O THR B 320 N GLU B 303 SHEET 3 AA9 3 GLU B 328 VAL B 329 -1 O VAL B 329 N VAL B 321 SHEET 1 AB1 4 GLN B 307 VAL B 310 0 SHEET 2 AB1 4 VAL B 378 GLU B 383 1 O SER B 381 N GLN B 307 SHEET 3 AB1 4 SER B 358 LYS B 367 -1 N VAL B 361 O VAL B 378 SHEET 4 AB1 4 ILE B 335 VAL B 338 -1 N GLU B 336 O VAL B 364 SHEET 1 AB2 4 GLN B 307 VAL B 310 0 SHEET 2 AB2 4 VAL B 378 GLU B 383 1 O SER B 381 N GLN B 307 SHEET 3 AB2 4 SER B 358 LYS B 367 -1 N VAL B 361 O VAL B 378 SHEET 4 AB2 4 LYS B 370 GLU B 374 -1 O VAL B 372 N TYR B 365 SHEET 1 AB3 2 THR B 315 ALA B 316 0 SHEET 2 AB3 2 GLU B 350 ILE B 351 -1 O ILE B 351 N THR B 315 SHEET 1 AB4 4 GLN C 3 GLY C 8 0 SHEET 2 AB4 4 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AB4 4 ALA C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AB4 4 PHE C 67 ASP C 72 -1 N SER C 70 O TYR C 79 SHEET 1 AB5 6 GLY C 10 GLN C 13 0 SHEET 2 AB5 6 THR C 112 SER C 117 1 O THR C 115 N GLY C 10 SHEET 3 AB5 6 ALA C 91 ASP C 98 -1 N ALA C 91 O VAL C 114 SHEET 4 AB5 6 MET C 34 GLN C 39 -1 N GLY C 35 O ASN C 96 SHEET 5 AB5 6 ARG C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB5 6 ALA C 57 TYR C 59 -1 O ASN C 58 N VAL C 50 SHEET 1 AB6 4 GLY C 10 GLN C 13 0 SHEET 2 AB6 4 THR C 112 SER C 117 1 O THR C 115 N GLY C 10 SHEET 3 AB6 4 ALA C 91 ASP C 98 -1 N ALA C 91 O VAL C 114 SHEET 4 AB6 4 ASP C 106 TRP C 108 -1 O TYR C 107 N ALA C 97 SHEET 1 AB7 4 ALA D 217 ALA D 219 0 SHEET 2 AB7 4 LYS D 224 LYS D 228 -1 O GLU D 226 N LYS D 218 SHEET 3 AB7 4 SER D 265 LEU D 270 -1 O VAL D 268 N VAL D 225 SHEET 4 AB7 4 VAL D 254 LEU D 259 -1 N LYS D 255 O GLU D 269 SHEET 1 AB8 4 LYS D 251 VAL D 252 0 SHEET 2 AB8 4 ILE D 241 ASN D 245 -1 N VAL D 243 O VAL D 252 SHEET 3 AB8 4 THR D 279 VAL D 284 -1 O ASP D 283 N LYS D 242 SHEET 4 AB8 4 GLY D 288 ALA D 293 -1 O THR D 290 N VAL D 282 SHEET 1 AB9 3 THR D 301 MSE D 304 0 SHEET 2 AB9 3 PHE D 319 LYS D 322 -1 O THR D 320 N GLU D 303 SHEET 3 AB9 3 GLU D 328 VAL D 329 -1 O VAL D 329 N VAL D 321 SHEET 1 AC1 4 GLN D 307 VAL D 310 0 SHEET 2 AC1 4 VAL D 378 GLU D 383 1 O SER D 381 N VAL D 309 SHEET 3 AC1 4 SER D 358 LYS D 367 -1 N VAL D 361 O VAL D 378 SHEET 4 AC1 4 ILE D 335 VAL D 338 -1 N GLU D 336 O VAL D 364 SHEET 1 AC2 4 GLN D 307 VAL D 310 0 SHEET 2 AC2 4 VAL D 378 GLU D 383 1 O SER D 381 N VAL D 309 SHEET 3 AC2 4 SER D 358 LYS D 367 -1 N VAL D 361 O VAL D 378 SHEET 4 AC2 4 LYS D 370 GLU D 374 -1 O VAL D 372 N TYR D 365 SHEET 1 AC3 2 THR D 315 ALA D 316 0 SHEET 2 AC3 2 GLU D 350 ILE D 351 -1 O ILE D 351 N THR D 315 SHEET 1 AC4 4 GLN E 3 SER E 7 0 SHEET 2 AC4 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AC4 4 ALA E 77 MET E 82 -1 O VAL E 78 N CYS E 22 SHEET 4 AC4 4 PHE E 67 ASP E 72 -1 N SER E 70 O TYR E 79 SHEET 1 AC5 6 GLY E 10 GLN E 13 0 SHEET 2 AC5 6 THR E 112 SER E 117 1 O THR E 115 N VAL E 12 SHEET 3 AC5 6 ALA E 91 ASP E 98 -1 N ALA E 91 O VAL E 114 SHEET 4 AC5 6 MET E 34 GLN E 39 -1 N GLY E 35 O ASN E 96 SHEET 5 AC5 6 ARG E 45 ILE E 51 -1 O ALA E 49 N TRP E 36 SHEET 6 AC5 6 ALA E 57 TYR E 59 -1 O ASN E 58 N VAL E 50 SHEET 1 AC6 4 GLY E 10 GLN E 13 0 SHEET 2 AC6 4 THR E 112 SER E 117 1 O THR E 115 N VAL E 12 SHEET 3 AC6 4 ALA E 91 ASP E 98 -1 N ALA E 91 O VAL E 114 SHEET 4 AC6 4 ASP E 106 TRP E 108 -1 O TYR E 107 N ALA E 97 SHEET 1 AC7 4 GLN G 3 GLY G 8 0 SHEET 2 AC7 4 LEU G 18 SER G 25 -1 O SER G 25 N GLN G 3 SHEET 3 AC7 4 ALA G 77 MET G 82 -1 O MET G 82 N LEU G 18 SHEET 4 AC7 4 PHE G 67 ASP G 72 -1 N ASP G 72 O ALA G 77 SHEET 1 AC8 6 GLY G 10 GLN G 13 0 SHEET 2 AC8 6 THR G 112 SER G 117 1 O GLN G 113 N GLY G 10 SHEET 3 AC8 6 ALA G 91 ASP G 98 -1 N TYR G 93 O THR G 112 SHEET 4 AC8 6 MET G 34 GLN G 39 -1 N TYR G 37 O TYR G 94 SHEET 5 AC8 6 ARG G 45 ILE G 51 -1 O ALA G 49 N TRP G 36 SHEET 6 AC8 6 ALA G 57 TYR G 59 -1 O ASN G 58 N VAL G 50 SHEET 1 AC9 4 GLY G 10 GLN G 13 0 SHEET 2 AC9 4 THR G 112 SER G 117 1 O GLN G 113 N GLY G 10 SHEET 3 AC9 4 ALA G 91 ASP G 98 -1 N TYR G 93 O THR G 112 SHEET 4 AC9 4 ASP G 106 TRP G 108 -1 O TYR G 107 N ALA G 97 SSBOND 1 CYS C 22 CYS C 95 1555 1555 2.03 SSBOND 2 CYS E 22 CYS E 95 1555 1555 2.03 SSBOND 3 CYS G 22 CYS G 95 1555 1555 2.04 LINK C GLU A 303 N MSE A 304 1555 1555 1.33 LINK C MSE A 304 N ALA A 305 1555 1555 1.34 LINK C GLU B 303 N MSE B 304 1555 1555 1.32 LINK C MSE B 304 N ALA B 305 1555 1555 1.33 LINK C GLU D 303 N MSE D 304 1555 1555 1.33 LINK C MSE D 304 N ALA D 305 1555 1555 1.33 CRYST1 213.264 213.264 53.267 90.00 90.00 90.00 P 43 21 2 24 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 0.004689 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004689 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018773 0.00000 MTRIX1 1 0.539817 -0.841500 0.021798 -49.34417 1 MTRIX2 1 -0.841777 -0.539725 0.010386 -90.62716 1 MTRIX3 1 0.003025 -0.023955 -0.999708 -2.93585 1 MTRIX1 2 0.196390 -0.504671 0.840677 -28.59096 1 MTRIX2 2 -0.384857 0.748897 0.539480 12.13557 1 MTRIX3 2 -0.901840 -0.429489 -0.047150 -89.49748 1 MTRIX1 3 0.621875 0.122815 -0.773426 11.27289 1 MTRIX2 3 -0.771337 -0.074591 -0.632040 -32.27193 1 MTRIX3 3 -0.135315 0.989623 0.048345 -6.54215 1 MTRIX1 4 0.540388 -0.841414 -0.002031 -49.53367 1 MTRIX2 4 -0.841399 -0.540360 -0.007673 -90.65227 1 MTRIX3 4 0.005358 0.005855 -0.999969 -1.75888 1