HEADER IMMUNE SYSTEM 03-APR-18 6CXG TITLE ANTI-HIV-1 FAB 2G12 IN COMPLEX WITH GLYCOPEPTIDE 10V1S COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-HIV-1 FAB 2G12 LIGHT CHAIN; COMPND 3 CHAIN: L, K; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-HIV-1 FAB 2G12 HEAVY CHAIN; COMPND 7 CHAIN: H, M; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 10V1S GLYCOPEPTIDE; COMPND 11 CHAIN: A, C; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: 293FREESTYLE; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: 293FREESTYLE; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 16 ORGANISM_TAXID: 32630 KEYWDS ANTIBODY, GLYCOPEPTIDE, HIV-1, GLYCOBIOLOGY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.L.STANFIELD,I.A.WILSON REVDAT 1 20-FEB-19 6CXG 0 JRNL AUTH D.N.NGUYEN,B.XU,R.L.STANFIELD,K.B.JENNIFER,S.HORIYA, JRNL AUTH 2 J.S.TEMME,R.L.DEBORAH,C.C.LABRANCHE,D.C.MONTEFIORI, JRNL AUTH 3 C.E.COSTELLO,I.A.WILSON,I.J.KRAUSS JRNL TITL OLIGOMANNOSE GLYCOPEPTIDE CONJUGATES ELICIT ANTIBODIES JRNL TITL 2 TARGETING 2 THE GLYCAN CORE RATHER THAN ITS EXTREMITIES JRNL REF ACS CENT.SCI. 2019 JRNL REFN ESSN 2374-7951 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.12_2829: ???) 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.39 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 45732 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) : 0.197 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880 REMARK 3 FREE R VALUE TEST SET COUNT : 2230 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 42.3924 - 5.7852 0.99 2924 155 0.1754 0.2022 REMARK 3 2 5.7852 - 4.5937 0.99 2790 144 0.1487 0.1734 REMARK 3 3 4.5937 - 4.0135 1.00 2784 139 0.1416 0.1410 REMARK 3 4 4.0135 - 3.6468 1.00 2749 143 0.1705 0.2045 REMARK 3 5 3.6468 - 3.3855 1.00 2726 140 0.1769 0.2181 REMARK 3 6 3.3855 - 3.1860 1.00 2743 123 0.2024 0.2532 REMARK 3 7 3.1860 - 3.0265 0.99 2673 145 0.2167 0.2967 REMARK 3 8 3.0265 - 2.8947 1.00 2745 131 0.2147 0.2544 REMARK 3 9 2.8947 - 2.7833 1.00 2685 147 0.2213 0.3055 REMARK 3 10 2.7833 - 2.6873 1.00 2699 144 0.2233 0.2729 REMARK 3 11 2.6873 - 2.6033 1.00 2744 123 0.2431 0.2896 REMARK 3 12 2.6033 - 2.5289 1.00 2645 144 0.2574 0.3008 REMARK 3 13 2.5289 - 2.4623 0.99 2685 133 0.2667 0.3215 REMARK 3 14 2.4623 - 2.4022 1.00 2682 139 0.2626 0.3187 REMARK 3 15 2.4022 - 2.3476 1.00 2679 156 0.2800 0.3340 REMARK 3 16 2.3476 - 2.2977 0.95 2549 124 0.2841 0.3127 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.270 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.700 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.30 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 : 0.009 7270 REMARK 3 ANGLE : 1.349 9915 REMARK 3 CHIRALITY : 0.064 1166 REMARK 3 PLANARITY : 0.006 1215 REMARK 3 DIHEDRAL : 17.336 2712 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 6CXG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-18. REMARK 100 THE DEPOSITION ID IS D_1000233651. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-AUG-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 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) : 0.97950 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 : 45804 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.298 REMARK 200 RESOLUTION RANGE LOW (A) : 42.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.17400 REMARK 200 R SYM (I) : 0.17400 REMARK 200 FOR THE DATA SET : 8.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : 5.10 REMARK 200 R MERGE FOR SHELL (I) : 1.00000 REMARK 200 R SYM FOR SHELL (I) : 1.00000 REMARK 200 FOR SHELL : 1.900 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: 4RBP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1M CITRATE, 10MM SODIUM BORATE, PH REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 22.61050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.77050 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.58950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.77050 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.61050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.58950 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 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, A 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: K, M, 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 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 130 REMARK 465 LYS H 131 REMARK 465 SER H 132 REMARK 465 THR H 133 REMARK 465 SER H 134 REMARK 465 FOD A 1 REMARK 465 ALA A 2 REMARK 465 THR A 3 REMARK 465 LYS A 4 REMARK 465 THR A 5 REMARK 465 ASN A 6 REMARK 465 SER A 7 REMARK 465 LYS A 8 REMARK 465 ARG A 9 REMARK 465 GLU A 10 REMARK 465 LYS A 11 REMARK 465 THR A 12 REMARK 465 FOD A 13 REMARK 465 ASP A 14 REMARK 465 ASN A 15 REMARK 465 HIS A 16 REMARK 465 VAL A 17 REMARK 465 GLY A 34 REMARK 465 SER A 35 REMARK 465 GLY A 36 REMARK 465 SER A 37 REMARK 465 GLY A 38 REMARK 465 BUC A 39 REMARK 465 ALA A 40 REMARK 465 FOD C 1 REMARK 465 ALA C 2 REMARK 465 THR C 3 REMARK 465 LYS C 4 REMARK 465 THR C 5 REMARK 465 ASN C 6 REMARK 465 SER C 7 REMARK 465 LYS C 8 REMARK 465 ARG C 9 REMARK 465 GLU C 10 REMARK 465 LYS C 11 REMARK 465 THR C 12 REMARK 465 FOD C 13 REMARK 465 ASP C 14 REMARK 465 ASN C 15 REMARK 465 HIS C 16 REMARK 465 VAL C 17 REMARK 465 THR C 18 REMARK 465 ASN C 33 REMARK 465 GLY C 34 REMARK 465 SER C 35 REMARK 465 GLY C 36 REMARK 465 SER C 37 REMARK 465 GLY C 38 REMARK 465 BUC C 39 REMARK 465 ALA C 40 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 O2 FOD A 20 O5 BMA A 101 1.63 REMARK 500 O3 MAN A 102 O5 MAN A 105 2.15 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 GLU L 30 -118.37 48.03 REMARK 500 ALA L 51 -42.31 75.24 REMARK 500 ALA L 84 -177.20 -176.35 REMARK 500 ASN L 152 -0.89 72.65 REMARK 500 PHE H 148 135.55 -171.73 REMARK 500 THR H 200 -63.11 -152.51 REMARK 500 GLU K 30 -120.30 50.80 REMARK 500 ALA K 51 -36.71 71.37 REMARK 500 ALA K 84 -179.45 -178.46 REMARK 500 ASP M 76 60.61 63.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 484 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH H 407 DISTANCE = 5.91 ANGSTROMS REMARK 525 HOH M 393 DISTANCE = 5.90 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL K 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues ILE A REMARK 800 19 through MAN A 109 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues ILE C REMARK 800 19 through MAN C 107 DBREF 6CXG L 1 213 PDB 6CXG 6CXG 1 213 DBREF 6CXG H 1 228 PDB 6CXG 6CXG 1 228 DBREF 6CXG K 1 213 PDB 6CXG 6CXG 1 213 DBREF 6CXG M 1 228 PDB 6CXG 6CXG 1 228 DBREF 6CXG A 1 40 PDB 6CXG 6CXG 1 40 DBREF 6CXG C 1 40 PDB 6CXG 6CXG 1 40 SEQRES 1 L 213 ALA VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 L 213 SER VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER SEQRES 3 L 213 GLN SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 L 213 THR LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU SEQRES 7 L 213 GLN PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR SEQRES 8 L 213 ALA GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL SEQRES 9 L 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 213 PHE ASN ARG GLY GLU SEQRES 1 H 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 224 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN SEQRES 3 H 224 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG SEQRES 4 H 224 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 H 224 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS SEQRES 6 H 224 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE SEQRES 7 H 224 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR SEQRES 8 H 224 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU SEQRES 9 H 224 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR SEQRES 10 H 224 VAL VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER SEQRES 11 H 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 224 GLU PRO LYS SEQRES 1 K 213 ALA VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 K 213 SER VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER SEQRES 3 K 213 GLN SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 K 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 K 213 THR LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 K 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU SEQRES 7 K 213 GLN PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR SEQRES 8 K 213 ALA GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL SEQRES 9 K 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 K 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 K 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 K 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 K 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 K 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 K 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 K 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 K 213 PHE ASN ARG GLY GLU SEQRES 1 M 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 M 224 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN SEQRES 3 M 224 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG SEQRES 4 M 224 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 M 224 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS SEQRES 6 M 224 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE SEQRES 7 M 224 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR SEQRES 8 M 224 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU SEQRES 9 M 224 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR SEQRES 10 M 224 VAL VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER SEQRES 11 M 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 M 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 M 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 M 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 M 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 M 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 M 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 M 224 GLU PRO LYS SEQRES 1 A 40 FOD ALA THR LYS THR ASN SER LYS ARG GLU LYS THR FOD SEQRES 2 A 40 ASP ASN HIS VAL THR ILE FOD ARG SER ILE PRO TRP TYR SEQRES 3 A 40 THR TYR ARG TRP LEU PRO ASN GLY SER GLY SER GLY BUC SEQRES 4 A 40 ALA SEQRES 1 C 40 FOD ALA THR LYS THR ASN SER LYS ARG GLU LYS THR FOD SEQRES 2 C 40 ASP ASN HIS VAL THR ILE FOD ARG SER ILE PRO TRP TYR SEQRES 3 C 40 THR TYR ARG TRP LEU PRO ASN GLY SER GLY SER GLY BUC SEQRES 4 C 40 ALA HET FOD A 20 18 HET FOD C 20 18 HET GOL L 301 6 HET GOL L 302 6 HET GOL K 301 6 HET BMA A 101 11 HET MAN A 102 11 HET MAN A 103 11 HET MAN A 104 11 HET MAN A 105 11 HET MAN A 106 11 HET MAN A 107 11 HET MAN A 108 11 HET MAN A 109 11 HET BMA C 101 11 HET MAN C 102 11 HET MAN C 103 11 HET MAN C 104 11 HET MAN C 105 11 HET MAN C 106 11 HET MAN C 107 11 HETNAM FOD (2S)-2-AMINO-4-[1-(TRANS-4-HYDROXYCYCLOHEXYL)-1H-1,2,3- HETNAM 2 FOD TRIAZOL-4-YL]BUTANOIC ACID HETNAM GOL GLYCEROL HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 FOD 2(C12 H20 N4 O3) FORMUL 7 GOL 3(C3 H8 O3) FORMUL 10 BMA 2(C6 H12 O6) FORMUL 10 MAN 14(C6 H12 O6) FORMUL 12 HOH *423(H2 O) HELIX 1 AA1 GLN L 79 PHE L 83 5 5 HELIX 2 AA2 SER L 121 SER L 127 1 7 HELIX 3 AA3 LYS L 183 GLU L 187 1 5 HELIX 4 AA4 THR H 52A THR H 55 5 4 HELIX 5 AA5 ARG H 83 THR H 87 5 5 HELIX 6 AA6 SER H 163 ALA H 165 5 3 HELIX 7 AA7 LYS H 213 ASN H 216 5 4 HELIX 8 AA8 GLN K 79 PHE K 83 5 5 HELIX 9 AA9 SER K 121 SER K 127 1 7 HELIX 10 AB1 LYS K 183 LYS K 188 1 6 HELIX 11 AB2 ARG M 28 HIS M 32 5 5 HELIX 12 AB3 THR M 52A THR M 55 5 4 HELIX 13 AB4 ARG M 83 THR M 87 5 5 HELIX 14 AB5 SER M 127 LYS M 129 5 3 HELIX 15 AB6 SER M 163 ALA M 165 5 3 HELIX 16 AB7 SER M 196 LEU M 198 5 3 HELIX 17 AB8 LYS M 213 ASN M 216 5 4 SHEET 1 AA1 4 MET L 4 SER L 7 0 SHEET 2 AA1 4 THR L 18 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA1 4 GLU L 70 SER L 76 -1 O PHE L 71 N CYS L 23 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA2 6 THR L 10 ALA L 13 0 SHEET 2 AA2 6 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11 SHEET 3 AA2 6 THR L 85 ALA L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N TYR L 36 O HIS L 87 SHEET 5 AA2 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA3 4 THR L 10 ALA L 13 0 SHEET 2 AA3 4 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11 SHEET 3 AA3 4 THR L 85 ALA L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA3 4 SER L 95 PHE L 98 -1 O SER L 95 N ALA L 92 SHEET 1 AA4 4 SER L 114 PHE L 118 0 SHEET 2 AA4 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AA4 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AA4 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AA5 4 ALA L 153 LEU L 154 0 SHEET 2 AA5 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AA5 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AA5 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AA6 4 GLN H 3 SER H 7 0 SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O GLY H 23 N VAL H 5 SHEET 3 AA6 4 PHE H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA6 4 PHE H 67 ASP H 72 -1 N ASP H 72 O PHE H 77 SHEET 1 AA7 6 LEU H 11 LYS H 13 0 SHEET 2 AA7 6 THR H 107 SER H 112 1 O THR H 110 N VAL H 12 SHEET 3 AA7 6 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA7 6 MET H 34 ARG H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA7 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA7 6 ARG H 57 TYR H 59 -1 O ASP H 58 N SER H 50 SHEET 1 AA8 4 LEU H 11 LYS H 13 0 SHEET 2 AA8 4 THR H 107 SER H 112 1 O THR H 110 N VAL H 12 SHEET 3 AA8 4 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA8 4 PHE H 100F TRP H 103 -1 O ALA H 102 N ARG H 94 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 THR H 137 TYR H 147 -1 O GLY H 141 N LEU H 124 SHEET 3 AA9 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 138 SHEET 4 AA9 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 190 SHEET 1 AB1 4 SER H 120 LEU H 124 0 SHEET 2 AB1 4 THR H 137 TYR H 147 -1 O GLY H 141 N LEU H 124 SHEET 3 AB1 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 138 SHEET 4 AB1 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 186 SHEET 1 AB2 3 THR H 153 TRP H 157 0 SHEET 2 AB2 3 ILE H 207 HIS H 212 -1 O ASN H 209 N SER H 156 SHEET 3 AB2 3 THR H 217 LYS H 222 -1 O THR H 217 N HIS H 212 SHEET 1 AB3 4 MET K 4 SER K 7 0 SHEET 2 AB3 4 THR K 18 ALA K 25 -1 O ARG K 24 N THR K 5 SHEET 3 AB3 4 GLU K 70 SER K 76 -1 O PHE K 71 N CYS K 23 SHEET 4 AB3 4 PHE K 62 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 AB4 6 THR K 10 ALA K 13 0 SHEET 2 AB4 6 THR K 102 ILE K 106 1 O ARG K 103 N LEU K 11 SHEET 3 AB4 6 THR K 85 ALA K 92 -1 N TYR K 86 O THR K 102 SHEET 4 AB4 6 LEU K 33 GLN K 38 -1 N TYR K 36 O HIS K 87 SHEET 5 AB4 6 LYS K 45 TYR K 49 -1 O LYS K 45 N GLN K 37 SHEET 6 AB4 6 THR K 53 LEU K 54 -1 O THR K 53 N TYR K 49 SHEET 1 AB5 4 THR K 10 ALA K 13 0 SHEET 2 AB5 4 THR K 102 ILE K 106 1 O ARG K 103 N LEU K 11 SHEET 3 AB5 4 THR K 85 ALA K 92 -1 N TYR K 86 O THR K 102 SHEET 4 AB5 4 SER K 95 PHE K 98 -1 O SER K 95 N ALA K 92 SHEET 1 AB6 4 SER K 114 PHE K 118 0 SHEET 2 AB6 4 THR K 129 PHE K 139 -1 O ASN K 137 N SER K 114 SHEET 3 AB6 4 TYR K 173 SER K 182 -1 O LEU K 179 N VAL K 132 SHEET 4 AB6 4 SER K 159 VAL K 163 -1 N GLN K 160 O THR K 178 SHEET 1 AB7 4 ALA K 153 LEU K 154 0 SHEET 2 AB7 4 LYS K 145 VAL K 150 -1 N VAL K 150 O ALA K 153 SHEET 3 AB7 4 VAL K 191 THR K 197 -1 O GLU K 195 N GLN K 147 SHEET 4 AB7 4 VAL K 205 ASN K 210 -1 O VAL K 205 N VAL K 196 SHEET 1 AB8 4 GLN M 3 SER M 7 0 SHEET 2 AB8 4 LEU M 18 SER M 25 -1 O GLY M 23 N VAL M 5 SHEET 3 AB8 4 PHE M 77 MET M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 AB8 4 PHE M 67 ASP M 72 -1 N THR M 68 O GLN M 81 SHEET 1 AB9 6 GLY M 10 LYS M 13 0 SHEET 2 AB9 6 THR M 107 SER M 112 1 O THR M 110 N VAL M 12 SHEET 3 AB9 6 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107 SHEET 4 AB9 6 MET M 34 ARG M 39 -1 N VAL M 37 O TYR M 91 SHEET 5 AB9 6 LEU M 45 ILE M 51 -1 O ALA M 49 N TRP M 36 SHEET 6 AB9 6 ARG M 57 TYR M 59 -1 O ASP M 58 N SER M 50 SHEET 1 AC1 4 GLY M 10 LYS M 13 0 SHEET 2 AC1 4 THR M 107 SER M 112 1 O THR M 110 N VAL M 12 SHEET 3 AC1 4 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107 SHEET 4 AC1 4 PHE M 100F TRP M 103 -1 O ALA M 102 N ARG M 94 SHEET 1 AC2 4 SER M 120 LEU M 124 0 SHEET 2 AC2 4 THR M 137 TYR M 147 -1 O LEU M 143 N PHE M 122 SHEET 3 AC2 4 TYR M 185 PRO M 194 -1 O VAL M 193 N ALA M 138 SHEET 4 AC2 4 VAL M 171 THR M 173 -1 N HIS M 172 O VAL M 190 SHEET 1 AC3 4 THR M 133 SER M 134 0 SHEET 2 AC3 4 THR M 137 TYR M 147 -1 O THR M 137 N SER M 134 SHEET 3 AC3 4 TYR M 185 PRO M 194 -1 O VAL M 193 N ALA M 138 SHEET 4 AC3 4 VAL M 177 LEU M 178 -1 N VAL M 177 O SER M 186 SHEET 1 AC4 3 THR M 153 TRP M 157 0 SHEET 2 AC4 3 ILE M 207 HIS M 212 -1 O ASN M 209 N SER M 156 SHEET 3 AC4 3 THR M 217 LYS M 222 -1 O VAL M 219 N VAL M 210 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 4 CYS H 142 CYS H 208 1555 1555 2.03 SSBOND 5 CYS K 23 CYS K 88 1555 1555 2.05 SSBOND 6 CYS K 134 CYS K 194 1555 1555 2.04 SSBOND 7 CYS M 22 CYS M 92 1555 1555 2.05 SSBOND 8 CYS M 142 CYS M 208 1555 1555 2.03 LINK C ILE A 19 N FOD A 20 1555 1555 1.33 LINK O2 FOD A 20 C1 BMA A 101 1555 1555 1.37 LINK C FOD A 20 N ARG A 21 1555 1555 1.33 LINK C ILE C 19 N FOD C 20 1555 1555 1.33 LINK O2 FOD C 20 C1 BMA C 101 1555 1555 1.40 LINK C FOD C 20 N ARG C 21 1555 1555 1.33 LINK O3 BMA A 101 C1 MAN A 107 1555 1555 1.43 LINK O6 BMA A 101 C1 MAN A 102 1555 1555 1.41 LINK O3 MAN A 102 C1 MAN A 105 1555 1555 1.26 LINK O6 MAN A 102 C1 MAN A 103 1555 1555 1.39 LINK O2 MAN A 103 C1 MAN A 104 1555 1555 1.45 LINK O2 MAN A 105 C1 MAN A 106 1555 1555 1.45 LINK O2 MAN A 107 C1 MAN A 108 1555 1555 1.44 LINK O2 MAN A 108 C1 MAN A 109 1555 1555 1.45 LINK O3 BMA C 101 C1 MAN C 106 1555 1555 1.45 LINK O6 BMA C 101 C1 MAN C 102 1555 1555 1.45 LINK O3 MAN C 102 C1 MAN C 105 1555 1555 1.45 LINK O6 MAN C 102 C1 MAN C 103 1555 1555 1.44 LINK O2 MAN C 103 C1 MAN C 104 1555 1555 1.44 LINK O2 MAN C 106 C1 MAN C 107 1555 1555 1.45 CISPEP 1 SER L 7 PRO L 8 0 -2.26 CISPEP 2 TYR L 140 PRO L 141 0 -2.88 CISPEP 3 PHE H 148 PRO H 149 0 -4.16 CISPEP 4 GLU H 150 PRO H 151 0 2.61 CISPEP 5 SER K 7 PRO K 8 0 -0.27 CISPEP 6 TYR K 140 PRO K 141 0 4.54 CISPEP 7 PHE M 148 PRO M 149 0 -2.28 CISPEP 8 GLU M 150 PRO M 151 0 1.69 CISPEP 9 ILE A 23 PRO A 24 0 -1.68 CISPEP 10 ILE C 23 PRO C 24 0 -1.35 SITE 1 AC1 10 GLN L 160 SER L 176 SER L 177 THR L 178 SITE 2 AC1 10 PHE M 174 PRO M 175 VAL M 177 SER M 186 SITE 3 AC1 10 LEU M 187 SER M 188 SITE 1 AC2 7 SER L 60 SER L 76 THR L 197 HIS L 198 SITE 2 AC2 7 LEU L 201 SER L 203 PRO L 204 SITE 1 AC3 11 PHE H 174 PRO H 175 VAL H 177 SER H 186 SITE 2 AC3 11 LEU H 187 SER H 188 SER K 162 SER K 176 SITE 3 AC3 11 SER K 177 THR K 178 HOH K 403 SITE 1 AC4 37 THR A 18 SER A 22 TRP A 25 TYR A 26 SITE 2 AC4 37 THR A 27 TYR A 28 ARG A 29 TRP A 30 SITE 3 AC4 37 ASN A 33 HOH A 201 HOH A 202 HOH A 208 SITE 4 AC4 37 HOH A 209 HOH A 210 ALA H 31 HIS H 32 SITE 5 AC4 37 THR H 33 THR H 52A SER H 53 THR H 55 SITE 6 AC4 37 LYS H 95 GLY H 96 LEU H 100 SER H 100A SITE 7 AC4 37 ASP H 100B ASN H 100C ASP H 100D LYS K 145 SITE 8 AC4 37 GLN K 147 SER K 168 GLY L 93 TYR L 94 SITE 9 AC4 37 ARG M 28 GLU M 75 ASP M 76 HOH M 313 SITE 10 AC4 37 HOH M 354 SITE 1 AC5 67 THR A 18 SER A 22 TRP A 25 TYR A 26 SITE 2 AC5 67 THR A 27 TYR A 28 ARG A 29 TRP A 30 SITE 3 AC5 67 ASN A 33 HOH A 201 HOH A 202 HOH A 208 SITE 4 AC5 67 HOH A 209 HOH A 210 SER C 22 TRP C 25 SITE 5 AC5 67 TYR C 26 THR C 27 TYR C 28 ARG C 29 SITE 6 AC5 67 TRP C 30 HOH C 204 HOH C 205 ARG H 28 SITE 7 AC5 67 ALA H 31 HIS H 32 THR H 33 THR H 52A SITE 8 AC5 67 SER H 53 THR H 55 LEU H 74 GLU H 75 SITE 9 AC5 67 ASP H 76 LYS H 95 GLY H 96 LEU H 100 SITE 10 AC5 67 SER H 100A ASP H 100B ASN H 100C ASP H 100D SITE 11 AC5 67 HOH H 316 HOH H 368 GLY K 93 TYR K 94 SITE 12 AC5 67 LYS K 145 GLN K 147 SER K 168 GLY L 93 SITE 13 AC5 67 TYR L 94 ARG M 28 ALA M 31 HIS M 32 SITE 14 AC5 67 THR M 33 THR M 52A SER M 53 THR M 55 SITE 15 AC5 67 GLU M 75 ASP M 76 LYS M 95 GLY M 96 SITE 16 AC5 67 LEU M 100 SER M 100A ASP M 100B ASN M 100C SITE 17 AC5 67 ASP M 100D HOH M 313 HOH M 354 CRYST1 45.221 131.179 169.541 90.00 90.00 90.00 P 21 21 21 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 0.022114 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007623 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005898 0.00000