HEADER IMMUNE SYSTEM 27-JUN-24 9CFA TITLE GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN EODGT8 IN TITLE 2 COMPLEX WITH FAB EOD-CL04.1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB EOD-CL04.1 LAMBDA LIGHT CHAIN; COMPND 3 CHAIN: L, A, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB EOD-CL04.1 HEAVY CHAIN; COMPND 7 CHAIN: H, B, F; 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: C, D, 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_ORGAN: 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 9CFA 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. 3.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 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) : 3.06 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.22 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1 REMARK 3 NUMBER OF REFLECTIONS : 42011 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 2108 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 48.2200 - 7.5500 0.93 2729 136 0.1796 0.2070 REMARK 3 2 7.5500 - 5.9900 0.98 2820 152 0.2148 0.2504 REMARK 3 3 5.9900 - 5.2400 0.92 2641 132 0.1945 0.2051 REMARK 3 4 5.2400 - 4.7600 0.95 2720 137 0.1776 0.1949 REMARK 3 5 4.7600 - 4.4200 0.98 2815 136 0.1845 0.2295 REMARK 3 6 4.4200 - 4.1600 0.98 2805 137 0.1993 0.2467 REMARK 3 7 4.1600 - 3.9500 0.99 2853 136 0.2175 0.2722 REMARK 3 8 3.9500 - 3.7800 0.99 2816 148 0.2451 0.2751 REMARK 3 9 3.7800 - 3.6300 0.92 2580 156 0.2482 0.3073 REMARK 3 10 3.6300 - 3.5100 0.91 2617 140 0.2755 0.2888 REMARK 3 11 3.5100 - 3.4000 0.97 2733 164 0.2793 0.2961 REMARK 3 12 3.4000 - 3.3000 0.97 2771 164 0.3022 0.3587 REMARK 3 13 3.3000 - 3.2100 0.97 2752 130 0.3198 0.3615 REMARK 3 14 3.2100 - 3.1400 0.95 2685 145 0.3622 0.3886 REMARK 3 15 3.1400 - 3.0600 0.55 1566 95 0.3715 0.4089 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) : 0.489 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.013 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 72.12 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.84 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 : 0.003 13950 REMARK 3 ANGLE : 0.593 19017 REMARK 3 CHIRALITY : 0.045 2179 REMARK 3 PLANARITY : 0.005 2414 REMARK 3 DIHEDRAL : 11.634 4847 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 : 3 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 "E" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "L" 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 "B" and (resid 1 through 128 or REMARK 3 resid 135 through 216 or resid 217)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "F" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 1 through 128 or REMARK 3 resid 135 through 216 or resid 217)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 4 through 35 or REMARK 3 resid 41 through 194 or resid 195)) 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 4 through 189 or REMARK 3 resid 289 through 290)) 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 4 through 189 or REMARK 3 resid 239 through 240)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9CFA 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_1000285323. 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42163 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.060 REMARK 200 RESOLUTION RANGE LOW (A) : 48.220 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.23800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.06 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 2.00000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.900 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 (%): 61.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM DIHYDROGEN PHOSPHATE, 20% REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 79.90900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.66650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.90900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 79.66650 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, C, I 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, J 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 GLN L 1 REMARK 465 SER H 217 REMARK 465 CYS H 218 REMARK 465 GLU C 1 REMARK 465 THR C 2 REMARK 465 GLY C 3 REMARK 465 SER C 190 REMARK 465 THR C 191 REMARK 465 GLY C 192 REMARK 465 THR C 193 REMARK 465 HIS C 194 REMARK 465 HIS C 195 REMARK 465 HIS C 196 REMARK 465 HIS C 197 REMARK 465 HIS C 198 REMARK 465 HIS C 199 REMARK 465 GLN A 1 REMARK 465 SER B 217 REMARK 465 CYS B 218 REMARK 465 GLU D 1 REMARK 465 THR D 2 REMARK 465 GLY D 3 REMARK 465 GLY D 36 REMARK 465 GLY D 37 REMARK 465 TYR D 38 REMARK 465 SER D 39 REMARK 465 ASN D 40 REMARK 465 THR D 191 REMARK 465 GLY D 192 REMARK 465 THR D 193 REMARK 465 HIS D 194 REMARK 465 HIS D 195 REMARK 465 HIS D 196 REMARK 465 HIS D 197 REMARK 465 HIS D 198 REMARK 465 HIS D 199 REMARK 465 GLN E 1 REMARK 465 LYS F 129 REMARK 465 SER F 130 REMARK 465 THR F 131 REMARK 465 SER F 132 REMARK 465 GLY F 133 REMARK 465 GLY F 134 REMARK 465 SER F 217 REMARK 465 CYS F 218 REMARK 465 GLU G 1 REMARK 465 THR G 2 REMARK 465 GLY G 3 REMARK 465 GLY G 36 REMARK 465 GLY G 37 REMARK 465 TYR G 38 REMARK 465 SER G 39 REMARK 465 ASN G 40 REMARK 465 THR G 191 REMARK 465 GLY G 192 REMARK 465 THR G 193 REMARK 465 HIS G 194 REMARK 465 HIS G 195 REMARK 465 HIS G 196 REMARK 465 HIS G 197 REMARK 465 HIS G 198 REMARK 465 HIS G 199 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 TYR L 32 63.25 33.87 REMARK 500 SER L 50 70.75 46.26 REMARK 500 THR L 51 -60.77 62.66 REMARK 500 ALA L 84 -172.83 -170.06 REMARK 500 ASP L 151 -90.35 57.36 REMARK 500 ASN L 170 -17.96 68.75 REMARK 500 ASN H 28 90.47 -68.54 REMARK 500 ALA H 114 -179.25 -62.49 REMARK 500 SER H 127 -164.29 -121.99 REMARK 500 SER H 130 51.97 -105.31 REMARK 500 ASP H 144 81.75 55.58 REMARK 500 THR H 160 -67.96 50.13 REMARK 500 TYR C 38 -89.48 51.67 REMARK 500 ALA C 41 -81.14 63.18 REMARK 500 ASN C 42 -0.15 -150.29 REMARK 500 ILE C 61 -1.65 -140.54 REMARK 500 GLN C 69 -57.10 64.57 REMARK 500 ALA C 137 -149.30 -113.63 REMARK 500 LYS C 138 -53.21 -140.54 REMARK 500 SER C 146 41.70 -84.34 REMARK 500 PHE C 183 76.90 -115.58 REMARK 500 ALA C 184 71.73 -164.42 REMARK 500 TYR A 32 62.55 33.80 REMARK 500 SER A 50 70.96 45.74 REMARK 500 THR A 51 -59.36 63.09 REMARK 500 LEU A 106A -155.32 -74.83 REMARK 500 ASP A 151 -92.70 60.07 REMARK 500 ASN A 170 -20.16 68.51 REMARK 500 ASN B 28 91.24 -68.63 REMARK 500 ALA B 114 -179.68 -63.61 REMARK 500 SER B 127 -165.00 -121.02 REMARK 500 SER B 130 39.98 -95.29 REMARK 500 ASP B 144 81.46 56.00 REMARK 500 ASN B 155 -63.18 52.47 REMARK 500 SER B 156 25.21 -175.85 REMARK 500 THR B 160 -66.81 53.79 REMARK 500 GLN D 69 -54.91 67.31 REMARK 500 ASN D 73 15.67 52.41 REMARK 500 LYS D 138 -73.48 64.88 REMARK 500 PRO D 144 -179.83 -66.98 REMARK 500 SER D 146 37.41 -85.97 REMARK 500 PHE D 183 77.35 -116.64 REMARK 500 ALA D 184 71.52 -160.80 REMARK 500 TYR E 32 63.43 33.61 REMARK 500 SER E 50 71.70 46.41 REMARK 500 THR E 51 -60.61 63.24 REMARK 500 LEU E 106A -161.74 -74.30 REMARK 500 ASP E 151 -90.15 56.68 REMARK 500 ASN E 170 -18.20 68.75 REMARK 500 ASN F 28 91.28 -68.72 REMARK 500 REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 9CFA L 1 212 PDB 9CFA 9CFA 1 212 DBREF 9CFA H 1 218 PDB 9CFA 9CFA 1 218 DBREF 9CFA C 1 199 PDB 9CFA 9CFA 1 199 DBREF 9CFA A 1 212 PDB 9CFA 9CFA 1 212 DBREF 9CFA B 1 218 PDB 9CFA 9CFA 1 218 DBREF 9CFA D 1 199 PDB 9CFA 9CFA 1 199 DBREF 9CFA E 1 212 PDB 9CFA 9CFA 1 212 DBREF 9CFA F 1 218 PDB 9CFA 9CFA 1 218 DBREF 9CFA G 1 199 PDB 9CFA 9CFA 1 199 SEQRES 1 L 215 GLN THR VAL VAL THR GLN GLU PRO SER LEU THR VAL SER SEQRES 2 L 215 PRO GLY GLY THR VAL THR LEU THR CYS ALA SER SER THR SEQRES 3 L 215 GLY ALA VAL THR SER GLY PHE TYR PRO SER TRP PHE GLN SEQRES 4 L 215 GLN LYS PRO GLY GLN THR PRO ARG THR LEU ILE TYR SER SEQRES 5 L 215 THR ASN ASN LYS HIS SER TRP THR PRO ALA ARG PHE SER SEQRES 6 L 215 GLY SER LEU LEU GLY GLY LYS ALA ALA LEU THR LEU SER SEQRES 7 L 215 GLY VAL GLN PRO GLU ASP GLU ALA ASP TYR TYR CYS LEU SEQRES 8 L 215 LEU TYR TYR GLY GLY VAL TRP VAL PHE GLY GLY GLY THR SEQRES 9 L 215 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER SEQRES 10 L 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA SEQRES 11 L 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR SEQRES 12 L 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER SEQRES 13 L 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS SEQRES 14 L 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER SEQRES 15 L 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER SEQRES 16 L 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR SEQRES 17 L 215 VAL ALA PRO THR GLU CYS SER SEQRES 1 H 219 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLU SEQRES 2 H 219 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 219 PHE ASN PHE SER ASN TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 H 219 ALA PRO GLY LYS GLY LEU GLU CYS ILE SER TYR ILE SER SEQRES 5 H 219 GLY SER SER SER THR LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 219 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 219 LEU TYR LEU GLN MET ASN SER LEU ARG ASP GLU ASP THR SEQRES 8 H 219 ALA VAL TYR TYR CYS ALA ARG ASP HIS TRP GLY LEU ASP SEQRES 9 H 219 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 H 219 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 219 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 219 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 219 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 219 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 219 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 219 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 219 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 C 183 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 C 183 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 C 183 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 C 183 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 C 183 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 C 183 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 C 183 ARG SER GLU ASP TRP ARG ASP ASN ALA LYS SER ILE CYS SEQRES 8 C 183 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 C 183 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 C 183 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 C 183 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 C 183 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 C 183 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 C 183 THR TRP PHE ALA SER THR GLY THR HIS HIS HIS HIS HIS SEQRES 15 C 183 HIS SEQRES 1 A 215 GLN THR VAL VAL THR GLN GLU PRO SER LEU THR VAL SER SEQRES 2 A 215 PRO GLY GLY THR VAL THR LEU THR CYS ALA SER SER THR SEQRES 3 A 215 GLY ALA VAL THR SER GLY PHE TYR PRO SER TRP PHE GLN SEQRES 4 A 215 GLN LYS PRO GLY GLN THR PRO ARG THR LEU ILE TYR SER SEQRES 5 A 215 THR ASN ASN LYS HIS SER TRP THR PRO ALA ARG PHE SER SEQRES 6 A 215 GLY SER LEU LEU GLY GLY LYS ALA ALA LEU THR LEU SER SEQRES 7 A 215 GLY VAL GLN PRO GLU ASP GLU ALA ASP TYR TYR CYS LEU SEQRES 8 A 215 LEU TYR TYR GLY GLY VAL TRP VAL PHE GLY GLY GLY THR SEQRES 9 A 215 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER SEQRES 10 A 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA SEQRES 11 A 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR SEQRES 12 A 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER SEQRES 13 A 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS SEQRES 14 A 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER SEQRES 15 A 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER SEQRES 16 A 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR SEQRES 17 A 215 VAL ALA PRO THR GLU CYS SER SEQRES 1 B 219 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLU SEQRES 2 B 219 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 219 PHE ASN PHE SER ASN TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 B 219 ALA PRO GLY LYS GLY LEU GLU CYS ILE SER TYR ILE SER SEQRES 5 B 219 GLY SER SER SER THR LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 B 219 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 B 219 LEU TYR LEU GLN MET ASN SER LEU ARG ASP GLU ASP THR SEQRES 8 B 219 ALA VAL TYR TYR CYS ALA ARG ASP HIS TRP GLY LEU ASP SEQRES 9 B 219 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 B 219 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 B 219 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 B 219 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 B 219 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 B 219 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 B 219 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 B 219 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 B 219 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 D 183 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 D 183 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 D 183 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 D 183 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 D 183 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 D 183 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 D 183 ARG SER GLU ASP TRP ARG ASP ASN ALA LYS SER ILE CYS SEQRES 8 D 183 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 D 183 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 D 183 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 D 183 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 D 183 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 D 183 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 D 183 THR TRP PHE ALA SER THR GLY THR HIS HIS HIS HIS HIS SEQRES 15 D 183 HIS SEQRES 1 E 215 GLN THR VAL VAL THR GLN GLU PRO SER LEU THR VAL SER SEQRES 2 E 215 PRO GLY GLY THR VAL THR LEU THR CYS ALA SER SER THR SEQRES 3 E 215 GLY ALA VAL THR SER GLY PHE TYR PRO SER TRP PHE GLN SEQRES 4 E 215 GLN LYS PRO GLY GLN THR PRO ARG THR LEU ILE TYR SER SEQRES 5 E 215 THR ASN ASN LYS HIS SER TRP THR PRO ALA ARG PHE SER SEQRES 6 E 215 GLY SER LEU LEU GLY GLY LYS ALA ALA LEU THR LEU SER SEQRES 7 E 215 GLY VAL GLN PRO GLU ASP GLU ALA ASP TYR TYR CYS LEU SEQRES 8 E 215 LEU TYR TYR GLY GLY VAL TRP VAL PHE GLY GLY GLY THR SEQRES 9 E 215 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER SEQRES 10 E 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA SEQRES 11 E 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR SEQRES 12 E 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER SEQRES 13 E 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS SEQRES 14 E 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER SEQRES 15 E 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER SEQRES 16 E 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR SEQRES 17 E 215 VAL ALA PRO THR GLU CYS SER SEQRES 1 F 219 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLU SEQRES 2 F 219 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 219 PHE ASN PHE SER ASN TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 F 219 ALA PRO GLY LYS GLY LEU GLU CYS ILE SER TYR ILE SER SEQRES 5 F 219 GLY SER SER SER THR LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 F 219 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 F 219 LEU TYR LEU GLN MET ASN SER LEU ARG ASP GLU ASP THR SEQRES 8 F 219 ALA VAL TYR TYR CYS ALA ARG ASP HIS TRP GLY LEU ASP SEQRES 9 F 219 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 F 219 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 F 219 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 F 219 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 F 219 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 F 219 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 F 219 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 F 219 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 F 219 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS 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 I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET SO4 L 301 5 HET SO4 L 302 5 HET NAG C 201 14 HET NAG C 202 14 HET SO4 C 203 5 HET NAG D 201 14 HET NAG D 202 14 HET NAG F 301 14 HET NAG G 201 14 HET NAG G 202 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM SO4 SULFATE ION 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 10 NAG 11(C8 H15 N O6) FORMUL 12 SO4 3(O4 S 2-) HELIX 1 AA1 THR L 28 TYR L 32 5 5 HELIX 2 AA2 GLN L 79 GLU L 83 5 5 HELIX 3 AA3 SER L 121 ALA L 127 1 7 HELIX 4 AA4 THR L 181 SER L 187 1 7 HELIX 5 AA5 ASN H 28 TYR H 32 5 5 HELIX 6 AA6 ASP H 61 LYS H 64 5 4 HELIX 7 AA7 ARG H 83 THR H 87 5 5 HELIX 8 AA8 SER H 187 LEU H 189 5 3 HELIX 9 AA9 LYS H 201 ASN H 204 5 4 HELIX 10 AB1 PRO C 15 SER C 19 5 5 HELIX 11 AB2 ASP C 52 GLN C 60 1 9 HELIX 12 AB3 ARG C 117 GLY C 136 1 20 HELIX 13 AB4 ASP C 149 ASN C 154 1 6 HELIX 14 AB5 THR A 28 TYR A 32 5 5 HELIX 15 AB6 GLN A 79 GLU A 83 5 5 HELIX 16 AB7 SER A 121 ALA A 127 1 7 HELIX 17 AB8 THR A 181 SER A 187 1 7 HELIX 18 AB9 ASN B 28 TYR B 32 5 5 HELIX 19 AC1 ASP B 61 LYS B 64 5 4 HELIX 20 AC2 ARG B 83 THR B 87 5 5 HELIX 21 AC3 SER B 187 LEU B 189 5 3 HELIX 22 AC4 LYS B 201 ASN B 204 5 4 HELIX 23 AC5 PRO D 15 SER D 19 5 5 HELIX 24 AC6 ASP D 52 GLN D 60 1 9 HELIX 25 AC7 ARG D 117 GLY D 136 1 20 HELIX 26 AC8 ASP D 149 ASN D 154 1 6 HELIX 27 AC9 THR E 28 TYR E 32 5 5 HELIX 28 AD1 GLN E 79 GLU E 83 5 5 HELIX 29 AD2 SER E 121 ALA E 127 1 7 HELIX 30 AD3 THR E 181 SER E 187 1 7 HELIX 31 AD4 ASN F 28 TYR F 32 5 5 HELIX 32 AD5 ASP F 61 LYS F 64 5 4 HELIX 33 AD6 ARG F 83 THR F 87 5 5 HELIX 34 AD7 PRO F 185 LEU F 189 5 5 HELIX 35 AD8 LYS F 201 ASN F 204 5 4 HELIX 36 AD9 PRO G 15 SER G 19 5 5 HELIX 37 AE1 ASP G 52 GLN G 60 1 9 HELIX 38 AE2 ARG G 117 GLY G 136 1 20 HELIX 39 AE3 ASP G 149 ASN G 154 1 6 SHEET 1 AA1 4 VAL L 4 GLN L 6 0 SHEET 2 AA1 4 THR L 18 SER L 25 -1 O ALA L 24 N THR L 5 SHEET 3 AA1 4 LYS L 70 SER L 76 -1 O LEU L 73 N LEU L 21 SHEET 4 AA1 4 PHE L 62 LEU L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA2 6 SER L 9 VAL L 13 0 SHEET 2 AA2 6 THR L 102 VAL L 106 1 O ARG L 103 N LEU L 11 SHEET 3 AA2 6 ALA L 84 TYR L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AA2 6 SER L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AA2 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA2 6 ASN L 53 LYS L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA3 4 SER L 9 VAL L 13 0 SHEET 2 AA3 4 THR L 102 VAL L 106 1 O ARG L 103 N LEU L 11 SHEET 3 AA3 4 ALA L 84 TYR L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AA3 4 VAL L 95 PHE L 98 -1 O VAL L 97 N LEU L 90 SHEET 1 AA4 4 SER L 114 PHE L 118 0 SHEET 2 AA4 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AA4 4 TYR L 172 LEU L 180 -1 O LEU L 180 N ALA L 130 SHEET 4 AA4 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AA5 4 SER L 114 PHE L 118 0 SHEET 2 AA5 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AA5 4 TYR L 172 LEU L 180 -1 O LEU L 180 N ALA L 130 SHEET 4 AA5 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AA6 4 SER L 153 VAL L 155 0 SHEET 2 AA6 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AA6 4 TYR L 191 HIS L 197 -1 O GLN L 194 N ALA L 147 SHEET 4 AA6 4 SER L 200 VAL L 206 -1 O SER L 200 N HIS L 197 SHEET 1 AA7 4 GLN H 3 SER H 7 0 SHEET 2 AA7 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA7 4 SER H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA7 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA8 6 GLY H 10 VAL H 12 0 SHEET 2 AA8 6 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA8 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA8 6 GLY H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA8 6 LYS H 57 TYR H 59 -1 O TYR H 58 N TYR H 50 SHEET 1 AA9 4 GLY H 10 VAL H 12 0 SHEET 2 AA9 4 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA9 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 4 LEU H 99 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AB1 4 SER H 120 LEU H 124 0 SHEET 2 AB1 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB1 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AB1 4 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB2 4 SER H 120 LEU H 124 0 SHEET 2 AB2 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB2 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AB2 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB3 3 THR H 151 TRP H 154 0 SHEET 2 AB3 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AB3 3 THR H 205 VAL H 213 -1 O VAL H 207 N VAL H 198 SHEET 1 AB4 7 LEU C 70 LEU C 72 0 SHEET 2 AB4 7 SER C 20 ARG C 34 -1 N GLY C 24 O PHE C 71 SHEET 3 AB4 7 ILE C 95 CYS C 107 -1 O VAL C 103 N ILE C 22 SHEET 4 AB4 7 HIS C 112 SER C 116 -1 O ALA C 114 N ALA C 106 SHEET 5 AB4 7 THR C 5 ARG C 11 -1 N ILE C 6 O ILE C 115 SHEET 6 AB4 7 GLU C 162 CYS C 166 -1 O TYR C 165 N ARG C 11 SHEET 7 AB4 7 HIS C 155 CYS C 159 -1 N PHE C 157 O PHE C 164 SHEET 1 AB5 6 VAL C 82 ARG C 84 0 SHEET 2 AB5 6 ILE C 95 CYS C 107 -1 O GLN C 98 N VAL C 82 SHEET 3 AB5 6 SER C 20 ARG C 34 -1 N ILE C 22 O VAL C 103 SHEET 4 AB5 6 THR C 43 PRO C 48 -1 O ARG C 47 N THR C 33 SHEET 5 AB5 6 THR C 139 PHE C 142 1 O THR C 139 N VAL C 44 SHEET 6 AB5 6 SER C 185 TRP C 187 -1 O SER C 185 N PHE C 142 SHEET 1 AB6 4 VAL A 4 GLN A 6 0 SHEET 2 AB6 4 THR A 18 SER A 25 -1 O ALA A 24 N THR A 5 SHEET 3 AB6 4 LYS A 70 SER A 76 -1 O LEU A 75 N VAL A 19 SHEET 4 AB6 4 PHE A 62 LEU A 67 -1 N SER A 63 O THR A 74 SHEET 1 AB7 6 SER A 9 VAL A 13 0 SHEET 2 AB7 6 THR A 102 VAL A 106 1 O ARG A 103 N LEU A 11 SHEET 3 AB7 6 ALA A 84 TYR A 92 -1 N ALA A 84 O LEU A 104 SHEET 4 AB7 6 SER A 34 GLN A 38 -1 N GLN A 38 O ASP A 85 SHEET 5 AB7 6 ARG A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AB7 6 ASN A 53 LYS A 54 -1 O ASN A 53 N TYR A 49 SHEET 1 AB8 4 SER A 9 VAL A 13 0 SHEET 2 AB8 4 THR A 102 VAL A 106 1 O ARG A 103 N LEU A 11 SHEET 3 AB8 4 ALA A 84 TYR A 92 -1 N ALA A 84 O LEU A 104 SHEET 4 AB8 4 VAL A 95 PHE A 98 -1 O VAL A 97 N LEU A 90 SHEET 1 AB9 4 SER A 114 PHE A 118 0 SHEET 2 AB9 4 ALA A 130 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 AB9 4 TYR A 172 LEU A 180 -1 O ALA A 174 N ILE A 136 SHEET 4 AB9 4 VAL A 159 THR A 161 -1 N GLU A 160 O TYR A 177 SHEET 1 AC1 4 SER A 114 PHE A 118 0 SHEET 2 AC1 4 ALA A 130 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 AC1 4 TYR A 172 LEU A 180 -1 O ALA A 174 N ILE A 136 SHEET 4 AC1 4 SER A 165 LYS A 166 -1 N SER A 165 O ALA A 173 SHEET 1 AC2 4 SER A 153 VAL A 155 0 SHEET 2 AC2 4 VAL A 144 ALA A 150 -1 N ALA A 150 O SER A 153 SHEET 3 AC2 4 TYR A 191 HIS A 197 -1 O THR A 196 N THR A 145 SHEET 4 AC2 4 SER A 200 VAL A 206 -1 O SER A 200 N HIS A 197 SHEET 1 AC3 4 GLN B 3 SER B 7 0 SHEET 2 AC3 4 LEU B 18 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AC3 4 SER B 77 MET B 82 -1 O LEU B 80 N LEU B 20 SHEET 4 AC3 4 PHE B 67 ASP B 72 -1 N THR B 68 O GLN B 81 SHEET 1 AC4 6 GLY B 10 VAL B 12 0 SHEET 2 AC4 6 THR B 107 VAL B 111 1 O LEU B 108 N GLY B 10 SHEET 3 AC4 6 ALA B 88 ASP B 95 -1 N TYR B 90 O THR B 107 SHEET 4 AC4 6 GLY B 33 GLN B 39 -1 N VAL B 37 O TYR B 91 SHEET 5 AC4 6 LEU B 45 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AC4 6 LYS B 57 TYR B 59 -1 O TYR B 58 N TYR B 50 SHEET 1 AC5 4 GLY B 10 VAL B 12 0 SHEET 2 AC5 4 THR B 107 VAL B 111 1 O LEU B 108 N GLY B 10 SHEET 3 AC5 4 ALA B 88 ASP B 95 -1 N TYR B 90 O THR B 107 SHEET 4 AC5 4 LEU B 99 TRP B 103 -1 O TYR B 102 N ARG B 94 SHEET 1 AC6 4 SER B 120 LEU B 124 0 SHEET 2 AC6 4 THR B 135 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AC6 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145 SHEET 4 AC6 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AC7 4 SER B 120 LEU B 124 0 SHEET 2 AC7 4 THR B 135 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AC7 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145 SHEET 4 AC7 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AC8 3 THR B 151 TRP B 154 0 SHEET 2 AC8 3 TYR B 194 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AC8 3 THR B 205 VAL B 213 -1 O VAL B 207 N VAL B 198 SHEET 1 AC9 7 LEU D 70 LEU D 72 0 SHEET 2 AC9 7 SER D 20 ARG D 29 -1 N THR D 23 O PHE D 71 SHEET 3 AC9 7 ILE D 95 CYS D 107 -1 O VAL D 97 N LEU D 25 SHEET 4 AC9 7 HIS D 112 SER D 116 -1 O ALA D 114 N ALA D 106 SHEET 5 AC9 7 THR D 5 ARG D 11 -1 N ILE D 6 O ILE D 115 SHEET 6 AC9 7 GLU D 162 CYS D 166 -1 O TYR D 165 N ARG D 11 SHEET 7 AC9 7 HIS D 155 CYS D 159 -1 N PHE D 157 O PHE D 164 SHEET 1 AD1 6 VAL D 82 SER D 85 0 SHEET 2 AD1 6 ILE D 95 CYS D 107 -1 O GLN D 98 N VAL D 82 SHEET 3 AD1 6 SER D 20 ARG D 29 -1 N LEU D 25 O VAL D 97 SHEET 4 AD1 6 THR D 43 PRO D 48 -1 O ARG D 47 N THR D 28 SHEET 5 AD1 6 THR D 139 PHE D 142 1 O ILE D 141 N VAL D 44 SHEET 6 AD1 6 SER D 185 TRP D 187 -1 O TRP D 187 N ILE D 140 SHEET 1 AD2 4 VAL E 4 GLN E 6 0 SHEET 2 AD2 4 THR E 18 SER E 25 -1 O ALA E 24 N THR E 5 SHEET 3 AD2 4 LYS E 70 SER E 76 -1 O LEU E 73 N LEU E 21 SHEET 4 AD2 4 PHE E 62 LEU E 67 -1 N SER E 63 O THR E 74 SHEET 1 AD3 6 SER E 9 VAL E 13 0 SHEET 2 AD3 6 THR E 102 VAL E 106 1 O ARG E 103 N LEU E 11 SHEET 3 AD3 6 ASP E 85 TYR E 92 -1 N TYR E 86 O THR E 102 SHEET 4 AD3 6 SER E 34 GLN E 38 -1 N GLN E 38 O ASP E 85 SHEET 5 AD3 6 ARG E 45 TYR E 49 -1 O LEU E 47 N TRP E 35 SHEET 6 AD3 6 ASN E 53 LYS E 54 -1 O ASN E 53 N TYR E 49 SHEET 1 AD4 4 SER E 9 VAL E 13 0 SHEET 2 AD4 4 THR E 102 VAL E 106 1 O ARG E 103 N LEU E 11 SHEET 3 AD4 4 ASP E 85 TYR E 92 -1 N TYR E 86 O THR E 102 SHEET 4 AD4 4 VAL E 95 PHE E 98 -1 O VAL E 97 N LEU E 90 SHEET 1 AD5 4 SER E 114 PHE E 118 0 SHEET 2 AD5 4 ALA E 130 PHE E 139 -1 O VAL E 133 N PHE E 118 SHEET 3 AD5 4 TYR E 172 LEU E 180 -1 O ALA E 174 N ILE E 136 SHEET 4 AD5 4 VAL E 159 THR E 161 -1 N GLU E 160 O TYR E 177 SHEET 1 AD6 4 SER E 114 PHE E 118 0 SHEET 2 AD6 4 ALA E 130 PHE E 139 -1 O VAL E 133 N PHE E 118 SHEET 3 AD6 4 TYR E 172 LEU E 180 -1 O ALA E 174 N ILE E 136 SHEET 4 AD6 4 SER E 165 LYS E 166 -1 N SER E 165 O ALA E 173 SHEET 1 AD7 4 SER E 153 VAL E 155 0 SHEET 2 AD7 4 THR E 145 ALA E 150 -1 N ALA E 150 O SER E 153 SHEET 3 AD7 4 TYR E 191 HIS E 197 -1 O GLN E 194 N ALA E 147 SHEET 4 AD7 4 SER E 200 VAL E 206 -1 O SER E 200 N HIS E 197 SHEET 1 AD8 4 GLN F 3 SER F 7 0 SHEET 2 AD8 4 LEU F 18 SER F 25 -1 O SER F 25 N GLN F 3 SHEET 3 AD8 4 SER F 77 MET F 82 -1 O LEU F 80 N LEU F 20 SHEET 4 AD8 4 PHE F 67 ASP F 72 -1 N THR F 68 O GLN F 81 SHEET 1 AD9 6 GLY F 10 VAL F 12 0 SHEET 2 AD9 6 THR F 107 VAL F 111 1 O LEU F 108 N GLY F 10 SHEET 3 AD9 6 ALA F 88 ASP F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AD9 6 GLY F 33 GLN F 39 -1 N VAL F 37 O TYR F 91 SHEET 5 AD9 6 LEU F 45 ILE F 51 -1 O GLU F 46 N ARG F 38 SHEET 6 AD9 6 LYS F 57 TYR F 59 -1 O TYR F 58 N TYR F 50 SHEET 1 AE1 4 GLY F 10 VAL F 12 0 SHEET 2 AE1 4 THR F 107 VAL F 111 1 O LEU F 108 N GLY F 10 SHEET 3 AE1 4 ALA F 88 ASP F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AE1 4 LEU F 99 TRP F 103 -1 O TYR F 102 N ARG F 94 SHEET 1 AE2 4 SER F 120 LEU F 124 0 SHEET 2 AE2 4 ALA F 136 TYR F 145 -1 O LEU F 141 N PHE F 122 SHEET 3 AE2 4 TYR F 176 VAL F 184 -1 O TYR F 176 N TYR F 145 SHEET 4 AE2 4 VAL F 163 THR F 165 -1 N HIS F 164 O VAL F 181 SHEET 1 AE3 4 SER F 120 LEU F 124 0 SHEET 2 AE3 4 ALA F 136 TYR F 145 -1 O LEU F 141 N PHE F 122 SHEET 3 AE3 4 TYR F 176 VAL F 184 -1 O TYR F 176 N TYR F 145 SHEET 4 AE3 4 VAL F 169 LEU F 170 -1 N VAL F 169 O SER F 177 SHEET 1 AE4 3 THR F 151 TRP F 154 0 SHEET 2 AE4 3 TYR F 194 HIS F 200 -1 O ASN F 199 N THR F 151 SHEET 3 AE4 3 THR F 205 VAL F 213 -1 O VAL F 207 N VAL F 198 SHEET 1 AE5 7 LEU G 70 LEU G 72 0 SHEET 2 AE5 7 SER G 20 ARG G 29 -1 N THR G 23 O PHE G 71 SHEET 3 AE5 7 ILE G 95 CYS G 107 -1 O VAL G 103 N ILE G 22 SHEET 4 AE5 7 HIS G 112 SER G 116 -1 O ALA G 114 N ALA G 106 SHEET 5 AE5 7 THR G 5 ARG G 11 -1 N ILE G 6 O ILE G 115 SHEET 6 AE5 7 GLU G 162 CYS G 166 -1 O TYR G 165 N ARG G 11 SHEET 7 AE5 7 HIS G 155 CYS G 159 -1 N PHE G 157 O PHE G 164 SHEET 1 AE6 6 VAL G 82 ARG G 84 0 SHEET 2 AE6 6 ILE G 95 CYS G 107 -1 O GLN G 98 N VAL G 82 SHEET 3 AE6 6 SER G 20 ARG G 29 -1 N ILE G 22 O VAL G 103 SHEET 4 AE6 6 THR G 43 PRO G 48 -1 O ARG G 47 N THR G 28 SHEET 5 AE6 6 THR G 139 PHE G 142 1 O ILE G 141 N PHE G 46 SHEET 6 AE6 6 SER G 185 TRP G 187 -1 O SER G 185 N PHE G 142 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 2 CYS L 134 CYS L 193 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 5 CYS C 10 CYS C 166 1555 1555 2.03 SSBOND 6 CYS C 18 CYS C 159 1555 1555 2.04 SSBOND 7 CYS C 59 CYS C 96 1555 1555 2.03 SSBOND 8 CYS C 107 CYS C 113 1555 1555 2.04 SSBOND 9 CYS A 23 CYS A 88 1555 1555 2.03 SSBOND 10 CYS A 134 CYS A 193 1555 1555 2.03 SSBOND 11 CYS B 22 CYS B 92 1555 1555 2.03 SSBOND 12 CYS B 140 CYS B 196 1555 1555 2.03 SSBOND 13 CYS D 10 CYS D 166 1555 1555 2.03 SSBOND 14 CYS D 18 CYS D 159 1555 1555 2.04 SSBOND 15 CYS D 59 CYS D 96 1555 1555 2.04 SSBOND 16 CYS D 107 CYS D 113 1555 1555 2.04 SSBOND 17 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 18 CYS E 134 CYS E 193 1555 1555 2.03 SSBOND 19 CYS F 22 CYS F 92 1555 1555 2.03 SSBOND 20 CYS F 140 CYS F 196 1555 1555 2.04 SSBOND 21 CYS G 10 CYS G 166 1555 1555 2.03 SSBOND 22 CYS G 18 CYS G 159 1555 1555 2.04 SSBOND 23 CYS G 59 CYS G 96 1555 1555 2.03 SSBOND 24 CYS G 107 CYS G 113 1555 1555 2.04 LINK ND2 ASN H 28 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN C 21 C1 NAG C 202 1555 1555 1.44 LINK ND2 ASN C 73 C1 NAG C 201 1555 1555 1.43 LINK ND2 ASN B 28 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN D 21 C1 NAG D 202 1555 1555 1.44 LINK ND2 ASN D 73 C1 NAG D 201 1555 1555 1.44 LINK ND2 ASN F 28 C1 NAG F 301 1555 1555 1.44 LINK ND2 ASN G 21 C1 NAG G 202 1555 1555 1.44 LINK ND2 ASN G 73 C1 NAG G 201 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 CISPEP 1 TYR L 140 PRO L 141 0 -2.28 CISPEP 2 PHE H 146 PRO H 147 0 -2.58 CISPEP 3 GLU H 148 PRO H 149 0 -5.01 CISPEP 4 ARG C 11 PRO C 12 0 -1.26 CISPEP 5 TYR A 140 PRO A 141 0 -2.83 CISPEP 6 PHE B 146 PRO B 147 0 -2.41 CISPEP 7 GLU B 148 PRO B 149 0 -4.50 CISPEP 8 ARG D 11 PRO D 12 0 -1.27 CISPEP 9 TYR E 140 PRO E 141 0 -1.33 CISPEP 10 PHE F 146 PRO F 147 0 -2.02 CISPEP 11 GLU F 148 PRO F 149 0 -4.45 CISPEP 12 ARG G 11 PRO G 12 0 -2.02 CRYST1 159.818 159.333 101.057 90.00 108.23 90.00 C 1 2 1 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 0.006257 0.000000 0.002061 0.00000 SCALE2 0.000000 0.006276 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010419 0.00000 MTRIX1 1 0.401380 0.520514 0.753631 20.84473 1 MTRIX2 1 -0.544790 -0.525762 0.653282 27.54860 1 MTRIX3 1 0.736273 -0.672785 0.072541 31.03786 1 MTRIX1 2 -0.444538 0.534277 -0.718981 40.37607 1 MTRIX2 2 0.555238 -0.465503 -0.689215 21.08084 1 MTRIX3 2 -0.702920 -0.705588 -0.089717 49.84926 1 MTRIX1 3 0.393871 0.504038 0.768643 21.12762 1 MTRIX2 3 -0.538245 -0.551392 0.637385 27.65837 1 MTRIX3 3 0.745089 -0.664766 0.054119 30.47128 1 MTRIX1 4 -0.436978 0.529136 -0.727369 40.05255 1 MTRIX2 4 0.570120 -0.462536 -0.678988 20.55483 1 MTRIX3 4 -0.695711 -0.711390 -0.099553 50.08263 1 MTRIX1 5 -0.439586 0.535064 -0.721436 42.58792 1 MTRIX2 5 0.527826 -0.495999 -0.689481 24.86605 1 MTRIX3 5 -0.726749 -0.683879 -0.064387 47.57629 1 MTRIX1 6 -0.432169 -0.530523 -0.729229 85.33519 1 MTRIX2 6 -0.542885 -0.492638 0.680135 24.76005 1 MTRIX3 6 -0.720073 0.689821 -0.075110 48.13030 1