HEADER IMMUNE SYSTEM 11-MAR-24 9B0A TITLE GA10 NANOBODY BOUND TO 2C7 PEPTIDE MIMITOPE OF NEISSERIA GONORRHOEAE TITLE 2 LIPOOLIGOSACCHARIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: GA10 NANOBODY; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CYCLIZED PEPTIDE; COMPND 7 CHAIN: C, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1211845; SOURCE 6 EXPRESSION_SYSTEM_ATCC_NUMBER: 53338; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PSB_INIT; SOURCE 9 MOL_ID: 2; SOURCE 10 SYNTHETIC: YES; SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 12 ORGANISM_TAXID: 32630 KEYWDS NANOBODY, SYNBODY, 2C7 PEPTIDE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.WILLIAMSON,E.WALKER,W.KELTON,J.HICKS REVDAT 1 26-MAR-25 9B0A 0 JRNL AUTH E.WALKER,A.WARRENDER,K.BEIJERLING,J.KELSON,J.PAN, JRNL AUTH 2 A.WILLIAMSON,J.HICKS,W.KELTON JRNL TITL STRUCTURAL CHARACTERIZATION OF A NANOBODY AGAINST A JRNL TITL 2 CONSERVED LIPOOLIGOSACCHARIDE MOTIF OF N. GONORRHOEAE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.87 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) : 1.87 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.84 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.950 REMARK 3 COMPLETENESS FOR RANGE (%) : 69.1 REMARK 3 NUMBER OF REFLECTIONS : 13139 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.198 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 673 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 34.8400 - 3.1900 0.98 3549 187 0.1676 0.1895 REMARK 3 2 3.1900 - 2.5400 0.95 3458 167 0.2207 0.2565 REMARK 3 3 2.5400 - 2.2200 0.75 2672 168 0.2290 0.2727 REMARK 3 4 2.2100 - 2.0100 0.50 1822 100 0.2358 0.2986 REMARK 3 5 2.0100 - 1.8700 0.27 965 51 0.2461 0.2746 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) : 0.186 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.690 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.55 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 : 0.010 2070 REMARK 3 ANGLE : 1.039 2813 REMARK 3 CHIRALITY : 0.054 302 REMARK 3 PLANARITY : 0.013 369 REMARK 3 DIHEDRAL : 7.932 300 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID -2 THROUGH 117) REMARK 3 ORIGIN FOR THE GROUP (A): 7.5906 2.3610 11.6745 REMARK 3 T TENSOR REMARK 3 T11: 0.1170 T22: 0.2917 REMARK 3 T33: 0.2227 T12: 0.0057 REMARK 3 T13: 0.0155 T23: 0.0958 REMARK 3 L TENSOR REMARK 3 L11: 2.6690 L22: 1.8505 REMARK 3 L33: 3.0382 L12: -0.0223 REMARK 3 L13: 0.7317 L23: -0.0800 REMARK 3 S TENSOR REMARK 3 S11: -0.0962 S12: 0.6483 S13: 0.4024 REMARK 3 S21: -0.1850 S22: -0.0959 S23: 0.1850 REMARK 3 S31: -0.0370 S32: 0.0295 S33: 0.1647 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID -3 THROUGH 116) REMARK 3 ORIGIN FOR THE GROUP (A): 7.7056 -13.0728 46.3006 REMARK 3 T TENSOR REMARK 3 T11: 0.1192 T22: 0.3043 REMARK 3 T33: 0.1702 T12: -0.0605 REMARK 3 T13: -0.0381 T23: 0.0892 REMARK 3 L TENSOR REMARK 3 L11: 2.8910 L22: 1.9756 REMARK 3 L33: 2.2514 L12: 0.0013 REMARK 3 L13: -0.2364 L23: -0.2029 REMARK 3 S TENSOR REMARK 3 S11: 0.0298 S12: -0.6742 S13: -0.1571 REMARK 3 S21: 0.2129 S22: 0.0001 S23: -0.0526 REMARK 3 S31: 0.0646 S32: -0.0266 S33: -0.0050 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 18) REMARK 3 ORIGIN FOR THE GROUP (A): 16.3634 -14.6287 24.9439 REMARK 3 T TENSOR REMARK 3 T11: 0.2765 T22: 0.1684 REMARK 3 T33: 0.2158 T12: -0.0156 REMARK 3 T13: -0.0479 T23: -0.0338 REMARK 3 L TENSOR REMARK 3 L11: 8.4775 L22: 6.6169 REMARK 3 L33: 7.1927 L12: -1.1682 REMARK 3 L13: -1.7305 L23: -1.6957 REMARK 3 S TENSOR REMARK 3 S11: 0.4809 S12: 0.5347 S13: -1.0169 REMARK 3 S21: -0.9561 S22: 0.3101 S23: -0.0916 REMARK 3 S31: 0.2821 S32: 0.3818 S33: -0.7201 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 18) REMARK 3 ORIGIN FOR THE GROUP (A): 16.7488 3.5339 33.2522 REMARK 3 T TENSOR REMARK 3 T11: 0.2079 T22: 0.1950 REMARK 3 T33: 0.1993 T12: 0.0045 REMARK 3 T13: 0.0396 T23: -0.0706 REMARK 3 L TENSOR REMARK 3 L11: 6.3943 L22: 8.1459 REMARK 3 L33: 4.6355 L12: 3.1301 REMARK 3 L13: 2.1035 L23: -2.3160 REMARK 3 S TENSOR REMARK 3 S11: 0.2916 S12: -0.2819 S13: 0.4564 REMARK 3 S21: 0.7692 S22: 0.2260 S23: -0.0164 REMARK 3 S31: -0.0329 S32: 0.6913 S33: -0.4136 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" and (resid -2 through 42 or REMARK 3 (resid 43 through 44 and (name N or name REMARK 3 CA or name C or name O or name CB )) or REMARK 3 resid 45 through 115)) 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 -2 through 0 or REMARK 3 (resid 1 and (name N or name CA or name C REMARK 3 or name O or name CB )) or resid 2 REMARK 3 through 43 or (resid 44 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 45 through 101 or (resid 102 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 103 through 115)) 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" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 1 through 7 or REMARK 3 (resid 8 and (name N or name CA or name C REMARK 3 or name O or name CB )) or resid 9 REMARK 3 through 18)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9B0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000282218. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JUL-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.953728 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 : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13142 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.868 REMARK 200 RESOLUTION RANGE LOW (A) : 34.840 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0 REMARK 200 DATA REDUNDANCY : 2.100 REMARK 200 R MERGE (I) : 0.05200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.10 REMARK 200 R MERGE FOR SHELL (I) : 0.31600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 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: SMALL PLATES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 18.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 7.0, 22 % PEG 4,000, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D 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 -26 REMARK 465 SER A -25 REMARK 465 LYS A -24 REMARK 465 TYR A -23 REMARK 465 LEU A -22 REMARK 465 LEU A -21 REMARK 465 PRO A -20 REMARK 465 THR A -19 REMARK 465 ALA A -18 REMARK 465 ALA A -17 REMARK 465 ALA A -16 REMARK 465 GLY A -15 REMARK 465 LEU A -14 REMARK 465 LEU A -13 REMARK 465 LEU A -12 REMARK 465 LEU A -11 REMARK 465 ALA A -10 REMARK 465 ALA A -9 REMARK 465 GLN A -8 REMARK 465 PRO A -7 REMARK 465 ALA A -6 REMARK 465 MET A -5 REMARK 465 ALA A -4 REMARK 465 GLY A -3 REMARK 465 ALA A 118 REMARK 465 GLY A 119 REMARK 465 GLU A 120 REMARK 465 GLN A 121 REMARK 465 LYS A 122 REMARK 465 LEU A 123 REMARK 465 ILE A 124 REMARK 465 SER A 125 REMARK 465 GLU A 126 REMARK 465 GLU A 127 REMARK 465 ASP A 128 REMARK 465 LEU A 129 REMARK 465 ASN A 130 REMARK 465 SER A 131 REMARK 465 ALA A 132 REMARK 465 VAL A 133 REMARK 465 ASP 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 MET B -26 REMARK 465 SER B -25 REMARK 465 LYS B -24 REMARK 465 TYR B -23 REMARK 465 LEU B -22 REMARK 465 LEU B -21 REMARK 465 PRO B -20 REMARK 465 THR B -19 REMARK 465 ALA B -18 REMARK 465 ALA B -17 REMARK 465 ALA B -16 REMARK 465 GLY B -15 REMARK 465 LEU B -14 REMARK 465 LEU B -13 REMARK 465 LEU B -12 REMARK 465 LEU B -11 REMARK 465 ALA B -10 REMARK 465 ALA B -9 REMARK 465 GLN B -8 REMARK 465 PRO B -7 REMARK 465 ALA B -6 REMARK 465 MET B -5 REMARK 465 ALA B -4 REMARK 465 ARG B 117 REMARK 465 ALA B 118 REMARK 465 GLY B 119 REMARK 465 GLU B 120 REMARK 465 GLN B 121 REMARK 465 LYS B 122 REMARK 465 LEU B 123 REMARK 465 ILE B 124 REMARK 465 SER B 125 REMARK 465 GLU B 126 REMARK 465 GLU B 127 REMARK 465 ASP B 128 REMARK 465 LEU B 129 REMARK 465 ASN B 130 REMARK 465 SER B 131 REMARK 465 ALA B 132 REMARK 465 VAL B 133 REMARK 465 ASP 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 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 GLN A 1 CG CD OE1 NE2 REMARK 470 GLU A 44 CG CD OE1 OE2 REMARK 470 VAL A 102 CG1 CG2 REMARK 470 ARG A 117 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 ASP C 8 CG OD1 OD2 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 PRO B 88 H THR B 91 1.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 HD21 ASN B 74 OE2 GLU C 9 1455 1.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 VAL B 12 CB VAL B 12 CG1 -0.128 REMARK 500 GLU B 89 CB GLU B 89 CG 0.143 REMARK 500 GLU B 89 CD GLU B 89 OE1 0.126 REMARK 500 GLU B 89 CD GLU B 89 OE2 0.091 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO B 88 N - CD - CG ANGL. DEV. = -11.4 DEGREES 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 GLN A 54 -135.60 61.94 REMARK 500 ALA A 92 170.87 177.78 REMARK 500 SER B -2 -67.72 -141.93 REMARK 500 GLN B 13 97.60 21.71 REMARK 500 GLN B 54 -135.62 60.84 REMARK 500 GLU B 89 -66.91 35.86 REMARK 500 ALA B 92 171.38 176.74 REMARK 500 ALA B 115 81.22 63.93 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 VAL B 12 GLN B 13 115.56 REMARK 500 PRO B 88 GLU B 89 108.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 67 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9B0A A -26 140 PDB 9B0A 9B0A -26 140 DBREF 9B0A B -26 140 PDB 9B0A 9B0A -26 140 DBREF 9B0A C 1 18 PDB 9B0A 9B0A 1 18 DBREF 9B0A D 1 18 PDB 9B0A 9B0A 1 18 SEQRES 1 A 167 MET SER LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU SEQRES 2 A 167 LEU LEU LEU ALA ALA GLN PRO ALA MET ALA GLY SER SER SEQRES 3 A 167 SER GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 4 A 167 GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 5 A 167 GLY PHE PRO VAL TYR TRP ASN SER MET TYR TRP TYR ARG SEQRES 6 A 167 GLN ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ALA ILE SEQRES 7 A 167 THR SER GLN GLY GLY GLY THR GLU TYR ALA ASP SER VAL SEQRES 8 A 167 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 9 A 167 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 10 A 167 THR ALA VAL TYR TYR CYS THR VAL GLY VAL GLY VAL SER SEQRES 11 A 167 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER ALA GLY SEQRES 12 A 167 ARG ALA GLY GLU GLN LYS LEU ILE SER GLU GLU ASP LEU SEQRES 13 A 167 ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS SEQRES 1 B 167 MET SER LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU SEQRES 2 B 167 LEU LEU LEU ALA ALA GLN PRO ALA MET ALA GLY SER SER SEQRES 3 B 167 SER GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 4 B 167 GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER SEQRES 5 B 167 GLY PHE PRO VAL TYR TRP ASN SER MET TYR TRP TYR ARG SEQRES 6 B 167 GLN ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ALA ILE SEQRES 7 B 167 THR SER GLN GLY GLY GLY THR GLU TYR ALA ASP SER VAL SEQRES 8 B 167 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 9 B 167 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 10 B 167 THR ALA VAL TYR TYR CYS THR VAL GLY VAL GLY VAL SER SEQRES 11 B 167 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER ALA GLY SEQRES 12 B 167 ARG ALA GLY GLU GLN LYS LEU ILE SER GLU GLU ASP LEU SEQRES 13 B 167 ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS SEQRES 1 C 18 CYS GLY PRO ILE PRO VAL LEU ASP GLU ASN GLY LEU PHE SEQRES 2 C 18 ALA PRO GLY PRO CYS SEQRES 1 D 18 CYS GLY PRO ILE PRO VAL LEU ASP GLU ASN GLY LEU PHE SEQRES 2 D 18 ALA PRO GLY PRO CYS FORMUL 5 HOH *142(H2 O) HELIX 1 AA1 SER A -2 VAL A 2 5 5 HELIX 2 AA2 PRO A 28 ASN A 32 5 5 HELIX 3 AA3 ASP A 62 LYS A 65 5 4 HELIX 4 AA4 LYS A 87 THR A 91 5 5 HELIX 5 AA5 SER B -2 VAL B 2 5 5 HELIX 6 AA6 PRO B 28 ASN B 32 5 5 HELIX 7 AA7 LYS B 87 THR B 91 5 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 6 LEU A 11 GLN A 13 0 SHEET 2 AA2 6 THR A 109 SER A 114 1 O SER A 114 N VAL A 12 SHEET 3 AA2 6 ALA A 92 VAL A 98 -1 N TYR A 94 O THR A 109 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N TYR A 37 O TYR A 95 SHEET 5 AA2 6 GLU A 46 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O GLU A 59 N ALA A 50 SHEET 1 AA3 4 LEU A 11 GLN A 13 0 SHEET 2 AA3 4 THR A 109 SER A 114 1 O SER A 114 N VAL A 12 SHEET 3 AA3 4 ALA A 92 VAL A 98 -1 N TYR A 94 O THR A 109 SHEET 4 AA3 4 TYR A 104 ARG A 105 -1 O TYR A 104 N VAL A 98 SHEET 1 AA4 4 GLN B 3 SER B 7 0 SHEET 2 AA4 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA4 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA4 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA5 6 LEU B 11 GLN B 13 0 SHEET 2 AA5 6 THR B 109 SER B 114 1 O THR B 112 N VAL B 12 SHEET 3 AA5 6 ALA B 92 VAL B 98 -1 N TYR B 94 O THR B 109 SHEET 4 AA5 6 MET B 34 GLN B 39 -1 N TYR B 37 O TYR B 95 SHEET 5 AA5 6 GLU B 46 ILE B 51 -1 O ILE B 51 N MET B 34 SHEET 6 AA5 6 THR B 58 TYR B 60 -1 O GLU B 59 N ALA B 50 SHEET 1 AA6 4 LEU B 11 GLN B 13 0 SHEET 2 AA6 4 THR B 109 SER B 114 1 O THR B 112 N VAL B 12 SHEET 3 AA6 4 ALA B 92 VAL B 98 -1 N TYR B 94 O THR B 109 SHEET 4 AA6 4 TYR B 104 ARG B 105 -1 O TYR B 104 N VAL B 98 SHEET 1 AA7 2 ILE C 4 LEU C 7 0 SHEET 2 AA7 2 PHE C 13 GLY C 16 -1 O ALA C 14 N VAL C 6 SHEET 1 AA8 2 ILE D 4 LEU D 7 0 SHEET 2 AA8 2 PHE D 13 GLY D 16 -1 O ALA D 14 N VAL D 6 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 3 CYS C 1 CYS C 18 1555 1555 2.03 SSBOND 4 CYS D 1 CYS D 18 1555 1555 2.04 CRYST1 26.878 31.631 69.783 88.86 87.08 89.24 P 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.037205 -0.000494 -0.001889 0.00000 SCALE2 0.000000 0.031617 -0.000609 0.00000 SCALE3 0.000000 0.000000 0.014351 0.00000 MTRIX1 1 0.999968 -0.007766 0.001669 -0.21827 1 MTRIX2 1 -0.007751 -0.999928 -0.009153 -10.54296 1 MTRIX3 1 0.001740 0.009140 -0.999957 58.25402 1 MTRIX1 2 0.999944 -0.002115 0.010349 -0.00671 1 MTRIX2 2 -0.002061 -0.999984 -0.005246 -10.86585 1 MTRIX3 2 0.010360 0.005225 -0.999933 58.22120 1