HEADER IMMUNE SYSTEM 27-JUN-24 9CF6 TITLE GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN EODGT8 IN TITLE 2 COMPLEX WITH FAB EOD-CL02.1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB EOD-CL02.1 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB EOD-CL02.1 LAMBDA LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN COMPND 11 EODGT8; COMPND 12 CHAIN: G; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 9 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 18 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 21 ORGANISM_TAXID: 11676; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 26 EXPRESSION_SYSTEM_ORGAN: KIDNEY KEYWDS HIV, FAB, VACCINE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.SARKAR,R.L.STANFIELD,I.A.WILSON REVDAT 1 25-JUN-25 9CF6 0 JRNL AUTH T.SCHIFFNER,A.PALSER JRNL TITL DIVERSE COMPETITOR B CELL RESPONSES TO A GERMLINE-TARGETING JRNL TITL 2 PRIMING IMMUNOGEN IN HUMAN IG LOCI TRANSGENIC MICE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.88 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 18169 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.276 REMARK 3 FREE R VALUE : 0.306 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.788 REMARK 3 FREE R VALUE TEST SET COUNT : 870 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1246 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.34 REMARK 3 BIN R VALUE (WORKING SET) : 0.4370 REMARK 3 BIN FREE R VALUE SET COUNT : 54 REMARK 3 BIN FREE R VALUE : 0.4900 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4430 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 52.94 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.51400 REMARK 3 B22 (A**2) : -2.39100 REMARK 3 B33 (A**2) : 2.88500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -4.09200 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.430 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.491 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.352 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.886 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.860 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4570 ; 0.004 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6231 ; 1.131 ; 1.794 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 586 ; 5.678 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 18 ; 3.833 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 696 ;11.710 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 709 ; 0.068 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3493 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1842 ; 0.227 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3095 ; 0.307 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 104 ; 0.160 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2359 ; 1.789 ; 5.284 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2940 ; 3.187 ; 9.490 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2211 ; 1.609 ; 5.343 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3291 ; 2.818 ; 9.812 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.10 REMARK 3 ION PROBE RADIUS : 1.00 REMARK 3 SHRINKAGE RADIUS : 1.00 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE NOT BEEN USED REMARK 4 REMARK 4 9CF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000285327. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-APR-19 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 : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18286 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 39.883 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : 0.15800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : 1.04000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.600 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 (%): 54.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM NITRATE, 20% PEG3350, REMARK 280 15% ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 52.51950 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.30050 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 52.51950 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.30050 REMARK 290 SMTRY3 4 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, 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 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 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 LYS H 216 REMARK 465 SER H 217 REMARK 465 CYS H 218 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 SER L 213 REMARK 465 GLU G -2 REMARK 465 THR G -1 REMARK 465 GLY G 0 REMARK 465 GLY G 29 REMARK 465 TYR G 30 REMARK 465 SER G 31 REMARK 465 ASN G 32 REMARK 465 ALA G 170 REMARK 465 SER G 171 REMARK 465 THR G 172 REMARK 465 GLY G 173 REMARK 465 THR G 174 REMARK 465 HIS G 175 REMARK 465 HIS G 176 REMARK 465 HIS G 177 REMARK 465 HIS G 178 REMARK 465 HIS G 179 REMARK 465 HIS G 180 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 SER H 14 99.25 -49.92 REMARK 500 THR H 28 92.08 -59.42 REMARK 500 PRO H 41 109.76 -55.17 REMARK 500 ALA H 97 -108.20 64.40 REMARK 500 LEU H 100 -78.87 67.85 REMARK 500 ALA H 114 -39.17 -151.03 REMARK 500 SER H 115 -108.49 75.21 REMARK 500 ASP H 144 69.40 64.38 REMARK 500 PRO H 167 174.93 -58.94 REMARK 500 SER H 173 6.40 -164.38 REMARK 500 THR H 191 -68.06 -136.85 REMARK 500 SER L 27 83.80 -46.25 REMARK 500 SER L 27A -56.44 -173.10 REMARK 500 ASP L 27B -84.40 -110.90 REMARK 500 ASP L 29 -48.98 -131.54 REMARK 500 VAL L 51 -56.21 67.75 REMARK 500 LEU L 107 101.61 -57.82 REMARK 500 PRO L 142 154.69 -40.69 REMARK 500 ASP L 152 -65.59 68.40 REMARK 500 SER L 153 -40.34 -151.95 REMARK 500 LYS L 157 -72.61 -75.33 REMARK 500 GLN G 61 -43.57 76.96 REMARK 500 ASP G 79 104.19 -170.72 REMARK 500 GLU G 125 3.46 -69.58 REMARK 500 LYS G 130 -168.92 -114.90 REMARK 500 PHE G 164 74.11 -105.98 REMARK 500 ALA G 165 83.81 -173.51 REMARK 500 REMARK 500 REMARK: NULL DBREF 9CF6 H 1 218 PDB 9CF6 9CF6 1 218 DBREF 9CF6 L 1 213 PDB 9CF6 9CF6 1 213 DBREF 9CF6 G -2 180 PDB 9CF6 9CF6 -2 180 SEQRES 1 H 221 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 221 SER GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 221 PHE THR PHE SER SER TYR ASN MET ASN TRP VAL ARG GLN SEQRES 4 H 221 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE SER SEQRES 5 H 221 TYR SER SER ASN THR ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 221 GLY ARG PHE THR VAL SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 221 LEU TYR LEU GLN MET ASN SER LEU ARG ASP GLU ASP THR SEQRES 8 H 221 ALA VAL TYR TYR CYS ALA ARG ASP GLY ALA ALA ALA LEU SEQRES 9 H 221 PHE ASP TYR TRP GLY GLN GLY ILE LEU VAL THR VAL SER SEQRES 10 H 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 216 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 216 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SEQRES 3 L 216 SER ASP VAL GLY ASP TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 L 216 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE PHE GLU SEQRES 5 L 216 VAL SER ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 216 GLY LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 L 216 SER TYR THR SER SER SER SER LEU VAL PHE GLY GLY GLY SEQRES 9 L 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 G 183 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 G 183 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 G 183 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 G 183 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 G 183 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 G 183 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 G 183 ARG SER GLU ASP TRP ARG ASP ASN ALA LYS SER ILE CYS SEQRES 8 G 183 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 G 183 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 G 183 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 G 183 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 G 183 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 G 183 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 G 183 THR TRP PHE ALA SER THR GLY THR HIS HIS HIS HIS HIS SEQRES 15 G 183 HIS HET NAG G 201 14 HET NAG G 202 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 2(C8 H15 N O6) HELIX 1 AA1 ARG H 83 THR H 87 5 5 HELIX 2 AA2 ALA H 97 ALA H 99 5 3 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 THR H 191 5 5 HELIX 5 AA5 PRO H 202 ASN H 204 5 3 HELIX 6 AA6 GLN L 79 GLU L 83 5 5 HELIX 7 AA7 SER L 122 ALA L 128 1 7 HELIX 8 AA8 THR L 182 HIS L 189 1 8 HELIX 9 AA9 PRO G 12 SER G 16 5 5 HELIX 10 AB1 ASP G 44 GLN G 52 1 9 HELIX 11 AB2 ARG G 109 GLY G 128 1 20 HELIX 12 AB3 ASP G 141 ASN G 146 1 6 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 SER H 17 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 SER H 77 ASN H 82A-1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 ILE H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA2 6 ALA H 88 ASP H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AA2 6 ILE H 57 TYR H 59 -1 O TYR H 58 N TYR H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 ILE H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA3 4 ALA H 88 ASP H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 AA3 4 PHE H 100A TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 VAL H 150 TRP H 154 0 SHEET 2 AA6 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AA6 3 THR H 205 VAL H 213 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 5 SER L 9 GLY L 13 0 SHEET 2 AA7 5 THR L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AA7 5 ALA L 84 TYR L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA7 5 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA7 5 LYS L 45 ILE L 48 -1 O MET L 47 N TRP L 35 SHEET 1 AA8 4 SER L 9 GLY L 13 0 SHEET 2 AA8 4 THR L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AA8 4 ALA L 84 TYR L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 4 LEU L 96 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AA9 3 ILE L 19 THR L 24 0 SHEET 2 AA9 3 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AA9 3 PHE L 62 LYS L 66 -1 N SER L 65 O SER L 72 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 ALA L 131 PHE L 140 -1 O SER L 138 N SER L 115 SHEET 3 AB1 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 AB1 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 AB2 4 SER L 115 PHE L 119 0 SHEET 2 AB2 4 ALA L 131 PHE L 140 -1 O SER L 138 N SER L 115 SHEET 3 AB2 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 AB2 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 AB3 4 SER L 154 PRO L 155 0 SHEET 2 AB3 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 AB3 4 TYR L 192 HIS L 198 -1 O THR L 197 N THR L 146 SHEET 4 AB3 4 SER L 201 VAL L 207 -1 O VAL L 203 N VAL L 196 SHEET 1 AB4 7 LEU G 62 LEU G 64 0 SHEET 2 AB4 7 SER G 17 ARG G 26 -1 N THR G 20 O PHE G 63 SHEET 3 AB4 7 ILE G 87 CYS G 99 -1 O VAL G 89 N LEU G 22 SHEET 4 AB4 7 HIS G 104 SER G 108 -1 O ALA G 106 N ALA G 98 SHEET 5 AB4 7 THR G 2 ARG G 8 -1 N ILE G 3 O ILE G 107 SHEET 6 AB4 7 GLU G 154 CYS G 158 -1 O TYR G 157 N ARG G 8 SHEET 7 AB4 7 HIS G 147 CYS G 151 -1 N CYS G 151 O GLU G 154 SHEET 1 AB5 6 VAL G 74 SER G 77 0 SHEET 2 AB5 6 ILE G 87 CYS G 99 -1 O GLN G 90 N VAL G 74 SHEET 3 AB5 6 SER G 17 ARG G 26 -1 N LEU G 22 O VAL G 89 SHEET 4 AB5 6 THR G 35 PRO G 40 -1 O ARG G 39 N THR G 25 SHEET 5 AB5 6 THR G 131 PHE G 134 1 O ILE G 133 N PHE G 38 SHEET 6 AB5 6 SER G 166 TRP G 168 -1 O SER G 166 N PHE G 134 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.06 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 4 CYS L 135 CYS L 194 1555 1555 2.05 SSBOND 5 CYS G 7 CYS G 158 1555 1555 2.06 SSBOND 6 CYS G 15 CYS G 151 1555 1555 2.04 SSBOND 7 CYS G 51 CYS G 88 1555 1555 2.05 SSBOND 8 CYS G 99 CYS G 105 1555 1555 2.05 LINK ND2 ASN G 18 C1 NAG G 202 1555 1555 1.44 LINK ND2 ASN G 65 C1 NAG G 201 1555 1555 1.47 CISPEP 1 PHE H 146 PRO H 147 0 -6.90 CISPEP 2 GLU H 148 PRO H 149 0 -12.12 CISPEP 3 TYR L 141 PRO L 142 0 -29.29 CISPEP 4 ARG G 8 PRO G 9 0 -2.79 CRYST1 105.039 72.601 93.817 90.00 107.52 90.00 C 1 2 1 4 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 0.009520 0.000000 0.003005 0.00000 SCALE2 0.000000 0.013774 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011178 0.00000