HEADER ANTIVIRAL PROTEIN 24-FEB-22 7Z1D TITLE NANOBODY H11-H6 BOUND TO RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: EEE; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: H11-H6 NANOBODY; COMPND 7 CHAIN: FFF; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SPIKE, NANOBODY, HIGH AFFINITY, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.MIKOLAJEK,J.H.NAISMITH JRNL AUTH H.MIKOLAJEK,J.H.NAISMITH JRNL TITL STRUCTURE OF H11-H6 BOUND TO RBD JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.04 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 48825 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.186 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.832 REMARK 3 FREE R VALUE TEST SET COUNT : 2359 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3354 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.85 REMARK 3 BIN R VALUE (WORKING SET) : 0.2540 REMARK 3 BIN FREE R VALUE SET COUNT : 148 REMARK 3 BIN FREE R VALUE : 0.2750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2525 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 20 REMARK 3 SOLVENT ATOMS : 312 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.49 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.58700 REMARK 3 B22 (A**2) : 0.19300 REMARK 3 B33 (A**2) : 0.39500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.076 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.359 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2665 ; 0.006 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 2344 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3637 ; 1.315 ; 1.653 REMARK 3 BOND ANGLES OTHERS (DEGREES): 5442 ; 1.357 ; 1.580 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 346 ;13.735 ; 5.231 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 139 ;31.213 ;21.655 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 402 ;11.952 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;14.261 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 336 ; 0.066 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3266 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 628 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 386 ; 0.189 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 34 ; 0.243 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1257 ; 0.174 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 198 ; 0.137 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.028 ; 0.200 REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1306 ; 2.038 ; 2.019 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1305 ; 2.022 ; 2.016 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1634 ; 2.949 ; 3.025 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1635 ; 2.955 ; 3.028 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1359 ; 3.398 ; 2.347 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1360 ; 3.397 ; 2.349 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1993 ; 5.125 ; 3.391 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1994 ; 5.124 ; 3.393 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.90 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 7Z1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292120233. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-JUN-20 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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 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 : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48875 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 45.040 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 13.50 REMARK 200 R MERGE (I) : 0.08300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1 REMARK 200 DATA REDUNDANCY IN SHELL : 13.20 REMARK 200 R MERGE FOR SHELL (I) : 1.24300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.200 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: 6ZBP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5 AND 20% W/V PEG REMARK 280 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K 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 31.20500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.45000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.54000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.45000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.20500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.54000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: EEE, FFF 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 PRO E 330 REMARK 465 ASN E 331 REMARK 465 ILE E 332 REMARK 465 THR E 333 REMARK 465 LYS E 528 REMARK 465 LYS E 529 REMARK 465 SER E 530 REMARK 465 THR E 531 REMARK 465 ASN E 532 REMARK 465 LYS E 533 REMARK 465 HIS E 534 REMARK 465 HIS E 535 REMARK 465 HIS E 536 REMARK 465 HIS E 537 REMARK 465 HIS E 538 REMARK 465 HIS E 539 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 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 OE1 GLNFF 1 O HOHFF 201 1.88 REMARK 500 O HOHEE 829 O HOHEE 848 2.03 REMARK 500 O HOHFF 239 O HOHFF 321 2.05 REMARK 500 O HOHFF 264 O HOHFF 321 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 PHEEE 377 87.03 -150.65 REMARK 500 ASNEE 422 -54.48 -125.71 REMARK 500 SERFF 30 -117.85 38.10 REMARK 500 ALAFF 32 -147.61 -94.06 REMARK 500 ALAFF 92 168.37 179.74 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SEREE 494 TYREE 495 146.87 REMARK 500 REMARK 500 REMARK: NULL DBREF 7Z1DEE 330 532 UNP P0DTC2 SPIKE_SARS2 330 532 DBREF 7Z1DFF 1 134 PDB 7Z1D 7Z1D 1 134 SEQADV 7Z1D LYSEE 533 UNP P0DTC2 EXPRESSION TAG SEQADV 7Z1D HISEE 534 UNP P0DTC2 EXPRESSION TAG SEQADV 7Z1D HISEE 535 UNP P0DTC2 EXPRESSION TAG SEQADV 7Z1D HISEE 536 UNP P0DTC2 EXPRESSION TAG SEQADV 7Z1D HISEE 537 UNP P0DTC2 EXPRESSION TAG SEQADV 7Z1D HISEE 538 UNP P0DTC2 EXPRESSION TAG SEQADV 7Z1D HISEE 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1EE 210 PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE SEQRES 2EE 210 ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG SEQRES 3EE 210 LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU SEQRES 4EE 210 TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR GLY SEQRES 5EE 210 VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN SEQRES 6EE 210 VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL SEQRES 7EE 210 ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP SEQRES 8EE 210 TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL SEQRES 9EE 210 ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY SEQRES 10EE 210 GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER SEQRES 11EE 210 ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE SEQRES 12EE 210 TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY SEQRES 13EE 210 PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN SEQRES 14EE 210 PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL SEQRES 15EE 210 VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL SEQRES 16EE 210 CYS GLY PRO LYS LYS SER THR ASN LYS HIS HIS HIS HIS SEQRES 17EE 210 HIS HIS SEQRES 1FF 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU MET GLN SEQRES 2FF 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3FF 134 ARG THR PHE SER THR ALA ALA MET GLY TRP PHE ARG GLN SEQRES 4FF 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE ARG SEQRES 5FF 134 TRP SER GLY GLY SER ALA TYR TYR ALA ASP SER VAL LYS SEQRES 6FF 134 GLY ARG PHE THR ILE SER ARG ASP LYS ALA LYS ASN THR SEQRES 7FF 134 VAL TYR LEU GLN MET ASN SER LEU LYS TYR GLU ASP THR SEQRES 8FF 134 ALA VAL TYR TYR CYS ALA GLY SER LYS ILE THR ARG SER SEQRES 9FF 134 LEU LEU SER ASP TYR ALA THR TRP PRO TYR ASP TYR TRP SEQRES 10FF 134 GLY GLN GLY THR GLN VAL THR VAL SER SER LYS HIS HIS SEQRES 11FF 134 HIS HIS HIS HIS HET NAG EE 601 14 HET GOL EE 602 6 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 NAG C8 H15 N O6 FORMUL 4 GOL C3 H8 O3 FORMUL 5 HOH *312(H2 O) HELIX 1 AA1 PROEE 337 ASNEE 343 1 7 HELIX 2 AA2 SEREE 349 TRPEE 353 5 5 HELIX 3 AA3 TYREE 365 ASNEE 370 1 6 HELIX 4 AA4 SEREE 383 ASPEE 389 5 7 HELIX 5 AA5 ASPEE 405 ILEEE 410 5 6 HELIX 6 AA6 GLYEE 416 ASNEE 422 1 7 HELIX 7 AA7 SEREE 438 SEREE 443 1 6 HELIX 8 AA8 GLYEE 502 TYREE 505 5 4 HELIX 9 AA9 ASPFF 62 LYSFF 65 5 4 HELIX 10 AB1 LYSFF 87 THRFF 91 5 5 HELIX 11 AB2 LEUFF 105 THRFF 111 5 7 SHEET 1 AA1 5 ASNEE 354 ILEEE 358 0 SHEET 2 AA1 5 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AA1 5 PROEE 507 GLUEE 516 -1 O TYREE 508 N ILEEE 402 SHEET 4 AA1 5 GLYEE 431 ASNEE 437 -1 N CYSEE 432 O LEUEE 513 SHEET 5 AA1 5 THREE 376 TYREE 380 -1 N LYSEE 378 O VALEE 433 SHEET 1 AA2 3 CYSEE 361 VALEE 362 0 SHEET 2 AA2 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AA2 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AA3 2 LEUEE 452 ARGEE 454 0 SHEET 2 AA3 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AA4 2 TYREE 473 GLNEE 474 0 SHEET 2 AA4 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AA5 4 GLNFF 3 GLYFF 8 0 SHEET 2 AA5 4 LEUFF 18 SERFF 25 -1 O ALAFF 23 N VALFF 5 SHEET 3 AA5 4 THRFF 78 METFF 83 -1 O METFF 83 N LEUFF 18 SHEET 4 AA5 4 PHEFF 68 ASPFF 73 -1 N SERFF 71 O TYRFF 80 SHEET 1 AA6 6 GLYFF 10 GLNFF 13 0 SHEET 2 AA6 6 THRFF 121 SERFF 126 1 O THRFF 124 N GLYFF 10 SHEET 3 AA6 6 ALAFF 92 GLYFF 98 -1 N TYRFF 94 O THRFF 121 SHEET 4 AA6 6 ALAFF 33 GLNFF 39 -1 N PHEFF 37 O TYRFF 95 SHEET 5 AA6 6 GLUFF 46 ARGFF 52 -1 O GLUFF 46 N ARGFF 38 SHEET 6 AA6 6 ALAFF 58 TYRFF 60 -1 O TYRFF 59 N ALAFF 50 SHEET 1 AA7 4 GLYFF 10 GLNFF 13 0 SHEET 2 AA7 4 THRFF 121 SERFF 126 1 O THRFF 124 N GLYFF 10 SHEET 3 AA7 4 ALAFF 92 GLYFF 98 -1 N TYRFF 94 O THRFF 121 SHEET 4 AA7 4 TYRFF 116 TRPFF 117 -1 O TYRFF 116 N GLYFF 98 SSBOND 1 CYSEE 336 CYSEE 361 1555 1555 2.05 SSBOND 2 CYSEE 379 CYSEE 432 1555 1555 2.10 SSBOND 3 CYSEE 391 CYSEE 525 1555 1555 2.05 SSBOND 4 CYSEE 480 CYSEE 488 1555 1555 2.01 SSBOND 5 CYSFF 22 CYSFF 96 1555 1555 2.09 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.43 CRYST1 62.410 65.080 82.900 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.016023 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015366 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012063 0.00000