HEADER VIRAL PROTEIN/IMMUNE SYSTEM 18-JUL-24 9CPX TITLE CRYSTAL STRUCTURE OF SARS-COV-2 RECEPTOR BINDING DOMAIN IN COMPLEX TITLE 2 WITH ANTIBODIES C03-0138 AND CC12.3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: C03-0138 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: C03-0138 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CC12.3 FAB HEAVY CHAIN; COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: CC12.3 FAB LIGHT CHAIN; COMPND 15 CHAIN: D; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: SPIKE PROTEIN S1; COMPND 19 CHAIN: A; COMPND 20 FRAGMENT: RECEPTOR BINDING DOMAIN (UNP RESIDUES 333-530); COMPND 21 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 31 2; SOURCE 32 ORGANISM_TAXID: 2697049; SOURCE 33 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 34 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS COVID-19, SARS-COV-2, RECEPTOR BINDING DOMAIN, ANTIBODY, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR Z.FENG,I.A.WILSON REVDAT 1 25-JUN-25 9CPX 0 JRNL AUTH Z.FENG,I.A.WILSON JRNL TITL STRUCTURES OF CR3022-LIKE ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 3 NUMBER OF REFLECTIONS : 38939 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.232 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.271 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110 REMARK 3 FREE R VALUE TEST SET COUNT : 3557 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 49.5400 - 7.8900 1.00 2766 155 0.1882 0.2240 REMARK 3 2 7.8800 - 6.2600 1.00 2795 152 0.2218 0.2338 REMARK 3 3 6.2600 - 5.4700 1.00 2763 148 0.2111 0.2623 REMARK 3 4 5.4700 - 4.9700 1.00 2790 143 0.1953 0.2193 REMARK 3 5 4.9700 - 4.6200 1.00 2772 155 0.1807 0.2213 REMARK 3 6 4.6100 - 4.3400 1.00 2775 142 0.1802 0.2380 REMARK 3 7 4.3400 - 4.1300 1.00 2771 153 0.1910 0.2223 REMARK 3 8 4.1300 - 3.9500 1.00 2780 152 0.2019 0.2509 REMARK 3 9 3.9500 - 3.7900 1.00 2763 146 0.2175 0.2319 REMARK 3 10 3.7900 - 3.6600 1.00 2773 155 0.2222 0.2425 REMARK 3 11 3.6600 - 3.5500 1.00 2751 149 0.2259 0.2764 REMARK 3 12 3.5500 - 3.4500 1.00 2805 147 0.2311 0.2604 REMARK 3 13 3.4500 - 3.3600 1.00 2782 152 0.2401 0.2302 REMARK 3 14 3.3600 - 3.2700 1.00 2792 146 0.2523 0.3049 REMARK 3 15 3.2700 - 3.2000 1.00 2802 145 0.2654 0.3833 REMARK 3 16 3.2000 - 3.1300 1.00 2734 147 0.2967 0.3297 REMARK 3 17 3.1300 - 3.0700 1.00 2782 150 0.2964 0.3200 REMARK 3 18 3.0700 - 3.0100 1.00 2793 146 0.2999 0.3602 REMARK 3 19 3.0100 - 2.9600 1.00 2781 152 0.3003 0.4176 REMARK 3 20 2.9600 - 2.9100 0.99 2747 147 0.3018 0.3376 REMARK 3 21 2.9100 - 2.8600 0.97 2680 149 0.2998 0.3935 REMARK 3 22 2.8600 - 2.8200 0.89 2451 139 0.2867 0.3636 REMARK 3 23 2.8200 - 2.7800 0.74 2078 113 0.3025 0.3183 REMARK 3 24 2.7800 - 2.7400 0.64 1766 95 0.2994 0.3789 REMARK 3 25 2.7400 - 2.7000 0.55 1528 79 0.2965 0.3487 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) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.870 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.002 NULL REMARK 3 ANGLE : 0.500 NULL REMARK 3 CHIRALITY : 0.043 1263 REMARK 3 PLANARITY : 0.004 1438 REMARK 3 DIHEDRAL : 13.938 2955 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 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9CPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000286007. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-APR-24 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 : BL12-1 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 EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39168 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 26.30 REMARK 200 R MERGE (I) : 0.10100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 28.20 REMARK 200 R MERGE FOR SHELL (I) : 1.15500 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 (%): 57.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE / CITRIC ACID REMARK 280 BUFFER, PH 3.33, 25% V/V PEG200, 9% W/V PEG6000, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 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 113.29500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.08400 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.08400 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.64750 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.08400 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.08400 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 169.94250 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.08400 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.08400 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 56.64750 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.08400 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.08400 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 169.94250 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 113.29500 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, C, D, A, B 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 215 REMARK 465 CYS H 216 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 LYS C 129 REMARK 465 SER C 130 REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 LYS C 214 REMARK 465 SER C 215 REMARK 465 CYS C 216 REMARK 465 GLY D 212 REMARK 465 GLU D 213 REMARK 465 CYS D 214 REMARK 465 THR A 333 REMARK 465 GLY A 446 REMARK 465 GLY A 447 REMARK 465 ASN A 448 REMARK 465 LYS A 529 REMARK 465 SER A 530 REMARK 465 GLY A 531 REMARK 465 HIS A 532 REMARK 465 HIS A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 HIS A 536 REMARK 465 HIS A 537 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 ASN A 439 OG SER A 443 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 ASP H 144 66.36 61.75 REMARK 500 THR L 51 -14.08 70.45 REMARK 500 VAL C 48 -61.85 -102.84 REMARK 500 ASP C 144 62.99 62.87 REMARK 500 ALA D 51 -6.38 73.40 REMARK 500 LEU A 518 -162.42 54.83 REMARK 500 REMARK 500 REMARK: NULL DBREF 9CPX H 1 216 PDB 9CPX 9CPX 1 216 DBREF 9CPX L 1 214 PDB 9CPX 9CPX 1 214 DBREF 9CPX C 1 216 PDB 9CPX 9CPX 1 216 DBREF 9CPX D 1 214 PDB 9CPX 9CPX 1 214 DBREF 9CPX A 333 530 UNP P0DTC2 SPIKE_SARS2 333 530 SEQADV 9CPX GLY A 531 UNP P0DTC2 EXPRESSION TAG SEQADV 9CPX HIS A 532 UNP P0DTC2 EXPRESSION TAG SEQADV 9CPX HIS A 533 UNP P0DTC2 EXPRESSION TAG SEQADV 9CPX HIS A 534 UNP P0DTC2 EXPRESSION TAG SEQADV 9CPX HIS A 535 UNP P0DTC2 EXPRESSION TAG SEQADV 9CPX HIS A 536 UNP P0DTC2 EXPRESSION TAG SEQADV 9CPX HIS A 537 UNP P0DTC2 EXPRESSION TAG SEQRES 1 H 222 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 222 PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY SEQRES 3 H 222 TYR SER LEU ILE MET TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 H 222 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5 H 222 PRO GLY ASP SER ASP THR ARG TYR SER PRO SER PHE GLN SEQRES 6 H 222 GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 H 222 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 H 222 ALA MET TYR TYR CYS ALA GLY GLY SER GLY ILE PHE THR SEQRES 9 H 222 PRO MET ASP VAL TRP GLY GLN GLY THR ALA VAL ALA VAL SEQRES 10 H 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 H 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 H 222 CYS SEQRES 1 L 220 ASP ILE VAL MET THR GLN THR PRO ASP SER LEU ALA VAL SEQRES 2 L 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 L 220 GLN SER LEU LEU TYR SER SER ILE LYS LYS ASN TYR LEU SEQRES 4 L 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 220 LEU ILE TYR TRP THR SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 220 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 L 220 TYR TYR CYS GLN GLN TYR TYR SER THR PRO TYR THR PHE SEQRES 9 L 220 GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA SEQRES 10 L 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 L 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 L 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 L 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 L 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 L 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 L 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 220 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ILE GLN SEQRES 2 C 220 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 220 PHE THR VAL SER SER ASN TYR MET SER TRP VAL ARG GLN SEQRES 4 C 220 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 C 220 SER GLY GLY SER THR PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 C 220 ARG PHE THR ILE SER ARG ASP ASN SER LYS SER THR LEU SEQRES 7 C 220 TYR LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR ALA SEQRES 8 C 220 VAL TYR TYR CYS ALA ARG ASP PHE GLY ASP PHE TYR PHE SEQRES 9 C 220 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 C 220 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 C 220 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 C 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 C 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 C 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 C 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 C 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 C 220 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 D 214 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 D 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 D 214 GLN SER VAL SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 D 214 SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG LEU SEQRES 7 D 214 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 D 214 GLY SER SER PRO ARG THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 205 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 A 205 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 A 205 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 A 205 ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 A 205 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 A 205 ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE SEQRES 7 A 205 ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR SEQRES 8 A 205 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 A 205 ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 10 A 205 ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 11 A 205 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 A 205 GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS SEQRES 13 A 205 TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN SEQRES 14 A 205 GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 A 205 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 16 A 205 LYS LYS SER GLY HIS HIS HIS HIS HIS HIS HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 6 NAG 2(C8 H15 N O6) FORMUL 6 BMA C6 H12 O6 FORMUL 7 HOH *20(H2 O) HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 LYS H 83 THR H 87 5 5 HELIX 3 AA3 SER H 127 LYS H 129 5 3 HELIX 4 AA4 SER H 187 LEU H 189 5 3 HELIX 5 AA5 GLN L 79 VAL L 83 5 5 HELIX 6 AA6 SER L 121 SER L 127 1 7 HELIX 7 AA7 LYS L 183 LYS L 188 1 6 HELIX 8 AA8 THR C 28 ASN C 32 5 5 HELIX 9 AA9 ARG C 83 THR C 87 5 5 HELIX 10 AB1 SER C 156 ALA C 158 5 3 HELIX 11 AB2 LYS C 201 ASN C 204 5 4 HELIX 12 AB3 SER D 121 SER D 127 1 7 HELIX 13 AB4 LYS D 183 LYS D 188 1 6 HELIX 14 AB5 PHE A 338 ASN A 343 1 6 HELIX 15 AB6 SER A 349 TRP A 353 5 5 HELIX 16 AB7 TYR A 365 ASN A 370 1 6 HELIX 17 AB8 SER A 383 LEU A 390 5 8 HELIX 18 AB9 GLU A 406 ILE A 410 5 5 HELIX 19 AC1 GLY A 416 ASN A 422 1 7 HELIX 20 AC2 GLY A 502 TYR A 505 5 4 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 TRP H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 AA1 4 THR H 68 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O ALA H 110 N LYS H 12 SHEET 3 AA2 6 ALA H 88 GLY H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 TRP H 33 GLN H 39 -1 N TRP H 33 O GLY H 95 SHEET 5 AA2 6 GLU H 46 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 ASP H 56 TYR H 59 -1 O ARG H 58 N ILE H 50 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O ALA H 110 N LYS H 12 SHEET 3 AA3 4 ALA H 88 GLY H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 VAL H 102 TRP H 103 -1 O VAL H 102 N GLY 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 LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 THR L 7 0 SHEET 2 AA7 4 ALA L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 VAL L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA8 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 VAL L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SHEET 1 AB3 4 GLN C 3 SER C 7 0 SHEET 2 AB3 4 LEU C 18 SER C 25 -1 O SER C 21 N SER C 7 SHEET 3 AB3 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AB3 4 PHE C 67 ASP C 72 -1 N SER C 70 O TYR C 79 SHEET 1 AB4 6 LEU C 11 ILE C 12 0 SHEET 2 AB4 6 THR C 107 VAL C 111 1 O THR C 110 N ILE C 12 SHEET 3 AB4 6 ALA C 88 PHE C 96 -1 N TYR C 90 O THR C 107 SHEET 4 AB4 6 TYR C 33 GLN C 39 -1 N VAL C 37 O TYR C 91 SHEET 5 AB4 6 LEU C 45 ILE C 51 -1 O ILE C 51 N MET C 34 SHEET 6 AB4 6 THR C 57 TYR C 59 -1 O PHE C 58 N VAL C 50 SHEET 1 AB5 4 LEU C 11 ILE C 12 0 SHEET 2 AB5 4 THR C 107 VAL C 111 1 O THR C 110 N ILE C 12 SHEET 3 AB5 4 ALA C 88 PHE C 96 -1 N TYR C 90 O THR C 107 SHEET 4 AB5 4 TYR C 100 TRP C 103 -1 O TYR C 100 N PHE C 96 SHEET 1 AB6 4 SER C 120 LEU C 124 0 SHEET 2 AB6 4 THR C 135 TYR C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AB6 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142 SHEET 4 AB6 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AB7 4 SER C 120 LEU C 124 0 SHEET 2 AB7 4 THR C 135 TYR C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AB7 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142 SHEET 4 AB7 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AB8 3 THR C 151 TRP C 154 0 SHEET 2 AB8 3 TYR C 194 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AB8 3 THR C 205 VAL C 211 -1 O VAL C 207 N VAL C 198 SHEET 1 AB9 4 LEU D 4 SER D 7 0 SHEET 2 AB9 4 ALA D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB9 4 ASP D 70 ILE D 75 -1 O ILE D 75 N ALA D 19 SHEET 4 AB9 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AC1 2 THR D 10 LEU D 13 0 SHEET 2 AC1 2 LYS D 103 ILE D 106 1 O GLU D 105 N LEU D 13 SHEET 1 AC2 4 SER D 53 ARG D 54 0 SHEET 2 AC2 4 ARG D 45 TYR D 49 -1 N TYR D 49 O SER D 53 SHEET 3 AC2 4 LEU D 33 GLN D 38 -1 N GLN D 37 O ARG D 45 SHEET 4 AC2 4 VAL D 85 GLN D 90 -1 O VAL D 85 N GLN D 38 SHEET 1 AC3 4 SER D 114 PHE D 118 0 SHEET 2 AC3 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AC3 4 TYR D 173 SER D 182 -1 O LEU D 179 N VAL D 132 SHEET 4 AC3 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AC4 4 ALA D 153 GLN D 155 0 SHEET 2 AC4 4 LYS D 145 VAL D 150 -1 N TRP D 148 O GLN D 155 SHEET 3 AC4 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AC4 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SHEET 1 AC5 5 ASN A 354 ILE A 358 0 SHEET 2 AC5 5 ASN A 394 ARG A 403 -1 O ALA A 397 N LYS A 356 SHEET 3 AC5 5 PRO A 507 GLU A 516 -1 O SER A 514 N TYR A 396 SHEET 4 AC5 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AC5 5 THR A 376 TYR A 380 -1 N TYR A 380 O GLY A 431 SHEET 1 AC6 2 CYS A 361 VAL A 362 0 SHEET 2 AC6 2 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 1 AC7 2 LEU A 452 ARG A 454 0 SHEET 2 AC7 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AC8 2 TYR A 473 GLN A 474 0 SHEET 2 AC8 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 92 1555 1555 2.03 SSBOND 6 CYS C 140 CYS C 196 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.03 SSBOND 9 CYS A 336 CYS A 361 1555 1555 2.03 SSBOND 10 CYS A 379 CYS A 432 1555 1555 2.04 SSBOND 11 CYS A 391 CYS A 525 1555 1555 2.03 SSBOND 12 CYS A 480 CYS A 488 1555 1555 2.04 LINK ND2 ASN A 343 C1 NAG B 1 1555 1555 1.44 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45 CISPEP 1 PHE H 146 PRO H 147 0 -1.71 CISPEP 2 GLU H 148 PRO H 149 0 0.47 CISPEP 3 THR L 7 PRO L 8 0 -4.28 CISPEP 4 THR L 94 PRO L 95 0 0.22 CISPEP 5 TYR L 140 PRO L 141 0 1.77 CISPEP 6 PHE C 146 PRO C 147 0 -2.88 CISPEP 7 GLU C 148 PRO C 149 0 3.67 CISPEP 8 SER D 7 PRO D 8 0 1.49 CISPEP 9 SER D 94 PRO D 95 0 -6.33 CISPEP 10 TYR D 140 PRO D 141 0 1.91 CRYST1 110.168 110.168 226.590 90.00 90.00 90.00 P 41 21 2 8 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 0.009077 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009077 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004413 0.00000