HEADER IMMUNE SYSTEM 17-APR-24 8Z4C TITLE THE FAB FRAGMENT OF ANTI-FIBRIN MONOCLONAL ANTIBODY 59D8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 59D8 HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 59D8 LIGHT CHAIN; COMPND 7 CHAIN: L, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTI-FIBRIN, ANTIBODY, 59D8, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.ZHANG,C.SUN REVDAT 1 23-APR-25 8Z4C 0 JRNL AUTH J.ZHANG,C.SUN JRNL TITL CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF MONOCLONAL ANTIBODY JRNL TITL 2 TARGETING THE KNOB B MOTIF OF FIBRIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.15.2_3472: ???) 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) : 2.06 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 56461 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) : 0.198 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 2773 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 9.9710 - 5.5897 0.99 2771 138 0.1853 0.2076 REMARK 3 2 5.5897 - 4.4374 1.00 2726 128 0.1564 0.1842 REMARK 3 3 4.4374 - 3.8767 1.00 2714 140 0.1551 0.1905 REMARK 3 4 3.8767 - 3.5223 1.00 2710 130 0.1805 0.2350 REMARK 3 5 3.5223 - 3.2699 1.00 2688 138 0.1845 0.2063 REMARK 3 6 3.2699 - 3.0771 1.00 2665 158 0.2029 0.2368 REMARK 3 7 3.0771 - 2.9230 1.00 2665 147 0.2021 0.2509 REMARK 3 8 2.9230 - 2.7958 1.00 2681 147 0.1982 0.2137 REMARK 3 9 2.7958 - 2.6882 1.00 2689 132 0.2112 0.2341 REMARK 3 10 2.6882 - 2.5954 1.00 2680 137 0.2198 0.2801 REMARK 3 11 2.5954 - 2.5142 1.00 2665 143 0.2289 0.2616 REMARK 3 12 2.5142 - 2.4424 1.00 2693 126 0.2378 0.2888 REMARK 3 13 2.4424 - 2.3781 1.00 2694 128 0.2450 0.2709 REMARK 3 14 2.3781 - 2.3201 1.00 2651 147 0.2522 0.2933 REMARK 3 15 2.3201 - 2.2673 1.00 2668 158 0.2495 0.3216 REMARK 3 16 2.2673 - 2.2191 1.00 2641 136 0.2652 0.3420 REMARK 3 17 2.2191 - 2.1747 1.00 2645 138 0.2694 0.2960 REMARK 3 18 2.1747 - 2.1336 1.00 2713 116 0.2753 0.3183 REMARK 3 19 2.1336 - 2.0955 1.00 2636 148 0.2900 0.3101 REMARK 3 20 2.0955 - 2.0600 1.00 2693 138 0.3027 0.3364 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) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.020 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 : 0.004 6837 REMARK 3 ANGLE : 0.806 9283 REMARK 3 CHIRALITY : 0.049 1041 REMARK 3 PLANARITY : 0.005 1186 REMARK 3 DIHEDRAL : 14.028 4101 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 10.3081 4.6937 25.6581 REMARK 3 T TENSOR REMARK 3 T11: 0.2491 T22: 0.1373 REMARK 3 T33: 0.2477 T12: -0.0262 REMARK 3 T13: -0.0077 T23: 0.0020 REMARK 3 L TENSOR REMARK 3 L11: 0.2646 L22: 0.1152 REMARK 3 L33: 0.9223 L12: -0.0050 REMARK 3 L13: 0.1108 L23: -0.0227 REMARK 3 S TENSOR REMARK 3 S11: -0.0031 S12: -0.0431 S13: -0.0156 REMARK 3 S21: 0.0094 S22: -0.0058 S23: 0.0297 REMARK 3 S31: 0.0150 S32: 0.0368 S33: 0.0095 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 8Z4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 18-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046586. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JAN-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 : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56469 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060 REMARK 200 RESOLUTION RANGE LOW (A) : 43.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.35200 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM CITRIC ACID (PH 5.0), 1 M REMARK 280 LITHIUM CHLORIDE, 10% W/V POLYETHYLENE GLYCOL 6000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 32.64500 REMARK 290 SMTRY3 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3620 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3640 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D 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 ARG H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS A 219 REMARK 465 HIS A 220 REMARK 465 HIS A 221 REMARK 465 HIS A 222 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 GLY A 101 O HOH A 301 2.06 REMARK 500 O HIS H 216 O HOH H 301 2.06 REMARK 500 O HOH L 327 O HOH L 357 2.08 REMARK 500 O HOH D 319 O HOH D 346 2.09 REMARK 500 O HOH H 318 O HOH H 389 2.10 REMARK 500 O HOH H 389 O HOH L 314 2.14 REMARK 500 OG1 THR A 40 OD1 ASP A 42 2.14 REMARK 500 NH2 ARG L 148 O HOH L 301 2.15 REMARK 500 O HOH A 326 O HOH A 333 2.17 REMARK 500 O SER L 72 O HOH L 302 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH H 387 O HOH L 345 2545 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 GLN H 99 153.31 80.54 REMARK 500 ASP H 102 68.72 -101.12 REMARK 500 TYR H 103 82.86 -44.91 REMARK 500 ASP H 147 66.61 65.71 REMARK 500 TYR L 31 -139.50 -83.78 REMARK 500 SER L 32 -159.18 -107.98 REMARK 500 ASP L 33 -5.76 63.67 REMARK 500 THR L 36 -73.05 -76.21 REMARK 500 ASN L 144 74.62 56.67 REMARK 500 ASP A 10 -65.89 -123.74 REMARK 500 GLN A 99 150.20 82.68 REMARK 500 TYR A 103 78.18 45.01 REMARK 500 SER A 133 156.41 178.47 REMARK 500 SER A 135 28.65 94.11 REMARK 500 GLU A 136 135.98 -171.79 REMARK 500 SER A 137 -120.02 66.13 REMARK 500 ASP A 147 66.57 65.11 REMARK 500 VAL D 56 -57.94 75.43 REMARK 500 ASN D 144 74.63 55.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 132 0.28 SIDE CHAIN 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 D 363 DISTANCE = 7.93 ANGSTROMS DBREF 8Z4C H 1 222 PDB 8Z4C 8Z4C 1 222 DBREF 8Z4C L 1 220 PDB 8Z4C 8Z4C 1 220 DBREF 8Z4C A 1 222 PDB 8Z4C 8Z4C 1 222 DBREF 8Z4C D 1 220 PDB 8Z4C 8Z4C 1 220 SEQRES 1 H 222 GLN VAL GLN LEU GLN GLN SER GLY GLY ASP LEU VAL LYS SEQRES 2 H 222 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 222 PHE SER PHE SER SER TYR GLY MET SER TRP VAL ARG GLN SEQRES 4 H 222 THR PRO ASP LYS ARG LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 H 222 SER GLY GLY ARG HIS THR TYR TYR PRO ASP SER VAL LYS SEQRES 6 H 222 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 H 222 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 H 222 ALA MET TYR PHE CYS ALA ARG GLN GLU GLY ASP TYR ASP SEQRES 9 H 222 ASP TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SEQRES 10 H 222 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO CYS SEQRES 11 H 222 SER ARG SER THR SER GLU SER THR ALA ALA LEU GLY CYS SEQRES 12 H 222 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 222 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 222 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 222 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR LYS SEQRES 16 H 222 THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER ASN THR SEQRES 17 H 222 LYS VAL ASP LYS ARG VAL HIS HIS HIS HIS HIS HIS HIS SEQRES 18 H 222 HIS SEQRES 1 L 220 ASP ILE GLU LEU THR GLN SER PRO LEU THR LEU SER VAL SEQRES 2 L 220 ILE ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 L 220 GLN SER LEU LEU TYR SER ASP GLY THR THR TYR LEU ASN SEQRES 4 L 220 TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 L 220 ILE TYR LEU VAL SER LYS VAL ASP SER GLY VAL PRO ASP SEQRES 6 L 220 ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 220 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 220 TYR CYS TRP GLN GLY THR HIS PHE PRO PHE THR PHE GLY SEQRES 9 L 220 SER GLY THR LYS LEU GLU LEU LYS ARG 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 A 222 GLN VAL GLN LEU GLN GLN SER GLY GLY ASP LEU VAL LYS SEQRES 2 A 222 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 A 222 PHE SER PHE SER SER TYR GLY MET SER TRP VAL ARG GLN SEQRES 4 A 222 THR PRO ASP LYS ARG LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 A 222 SER GLY GLY ARG HIS THR TYR TYR PRO ASP SER VAL LYS SEQRES 6 A 222 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 A 222 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 A 222 ALA MET TYR PHE CYS ALA ARG GLN GLU GLY ASP TYR ASP SEQRES 9 A 222 ASP TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SEQRES 10 A 222 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO CYS SEQRES 11 A 222 SER ARG SER THR SER GLU SER THR ALA ALA LEU GLY CYS SEQRES 12 A 222 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 A 222 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 A 222 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 A 222 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR LYS SEQRES 16 A 222 THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER ASN THR SEQRES 17 A 222 LYS VAL ASP LYS ARG VAL HIS HIS HIS HIS HIS HIS HIS SEQRES 18 A 222 HIS SEQRES 1 D 220 ASP ILE GLU LEU THR GLN SER PRO LEU THR LEU SER VAL SEQRES 2 D 220 ILE ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 D 220 GLN SER LEU LEU TYR SER ASP GLY THR THR TYR LEU ASN SEQRES 4 D 220 TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 D 220 ILE TYR LEU VAL SER LYS VAL ASP SER GLY VAL PRO ASP SEQRES 6 D 220 ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 D 220 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 D 220 TYR CYS TRP GLN GLY THR HIS PHE PRO PHE THR PHE GLY SEQRES 9 D 220 SER GLY THR LYS LEU GLU LEU LYS ARG ARG THR VAL ALA SEQRES 10 D 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 D 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 D 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 D 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 D 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 D 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 D 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 D 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS FORMUL 5 HOH *270(H2 O) HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 LYS H 87 THR H 91 5 5 HELIX 3 AA3 SER H 159 ALA H 161 5 3 HELIX 4 AA4 SER H 189 LYS H 195 1 7 HELIX 5 AA5 LYS H 204 ASN H 207 5 4 HELIX 6 AA6 GLU L 84 LEU L 88 5 5 HELIX 7 AA7 SER L 127 SER L 133 1 7 HELIX 8 AA8 LYS L 189 LYS L 194 1 6 HELIX 9 AA9 SER A 28 TYR A 32 5 5 HELIX 10 AB1 LYS A 87 THR A 91 5 5 HELIX 11 AB2 SER A 159 ALA A 161 5 3 HELIX 12 AB3 SER A 190 THR A 194 5 5 HELIX 13 AB4 LYS A 204 ASN A 207 5 4 HELIX 14 AB5 GLU D 84 LEU D 88 5 5 HELIX 15 AB6 SER D 127 LYS D 132 1 6 HELIX 16 AB7 LYS D 189 LYS D 194 1 6 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 THR H 69 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA2 6 ASP H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12 SHEET 3 AA2 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 110 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O PHE H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 58 TYR H 59 -1 O TYR H 59 N SER H 50 SHEET 1 AA3 4 SER H 123 LEU H 127 0 SHEET 2 AA3 4 THR H 138 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AA3 4 TYR H 179 PRO H 188 -1 O VAL H 187 N ALA H 139 SHEET 4 AA3 4 VAL H 166 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AA4 4 SER H 123 LEU H 127 0 SHEET 2 AA4 4 THR H 138 TYR H 148 -1 O LEU H 144 N PHE H 125 SHEET 3 AA4 4 TYR H 179 PRO H 188 -1 O VAL H 187 N ALA H 139 SHEET 4 AA4 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180 SHEET 1 AA5 3 THR H 154 TRP H 157 0 SHEET 2 AA5 3 TYR H 197 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AA5 3 THR H 208 VAL H 214 -1 O VAL H 210 N VAL H 201 SHEET 1 AA6 4 LEU L 4 SER L 7 0 SHEET 2 AA6 4 ALA L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA6 4 ASP L 75 ILE L 80 -1 O LEU L 78 N ILE L 21 SHEET 4 AA6 4 PHE L 67 SER L 72 -1 N THR L 68 O LYS L 79 SHEET 1 AA7 5 THR L 10 ILE L 14 0 SHEET 2 AA7 5 THR L 107 LYS L 112 1 O LYS L 108 N LEU L 11 SHEET 3 AA7 5 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA7 5 LEU L 38 GLN L 43 -1 N ASN L 39 O TRP L 94 SHEET 5 AA7 5 LYS L 50 ILE L 53 -1 O ILE L 53 N TRP L 40 SHEET 1 AA8 4 THR L 10 ILE L 14 0 SHEET 2 AA8 4 THR L 107 LYS L 112 1 O LYS L 108 N LEU L 11 SHEET 3 AA8 4 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA8 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AA9 4 SER L 120 PHE L 124 0 SHEET 2 AA9 4 THR L 135 PHE L 145 -1 O VAL L 139 N PHE L 124 SHEET 3 AA9 4 TYR L 179 SER L 188 -1 O LEU L 185 N VAL L 138 SHEET 4 AA9 4 SER L 165 VAL L 169 -1 N SER L 168 O SER L 182 SHEET 1 AB1 4 ALA L 159 LEU L 160 0 SHEET 2 AB1 4 LYS L 151 VAL L 156 -1 N VAL L 156 O ALA L 159 SHEET 3 AB1 4 VAL L 197 THR L 203 -1 O GLU L 201 N GLN L 153 SHEET 4 AB1 4 VAL L 211 ASN L 216 -1 O LYS L 213 N CYS L 200 SHEET 1 AB2 4 GLN A 3 SER A 7 0 SHEET 2 AB2 4 LEU A 18 SER A 25 -1 O ALA A 23 N GLN A 5 SHEET 3 AB2 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AB2 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AB3 6 LEU A 11 VAL A 12 0 SHEET 2 AB3 6 THR A 110 VAL A 114 1 O THR A 113 N VAL A 12 SHEET 3 AB3 6 ALA A 92 ARG A 98 -1 N TYR A 94 O THR A 110 SHEET 4 AB3 6 MET A 34 GLN A 39 -1 N VAL A 37 O PHE A 95 SHEET 5 AB3 6 LEU A 45 ILE A 51 -1 O ILE A 51 N MET A 34 SHEET 6 AB3 6 THR A 58 TYR A 59 -1 O TYR A 59 N SER A 50 SHEET 1 AB4 4 SER A 123 LEU A 127 0 SHEET 2 AB4 4 THR A 138 TYR A 148 -1 O LEU A 144 N PHE A 125 SHEET 3 AB4 4 TYR A 179 PRO A 188 -1 O VAL A 187 N ALA A 139 SHEET 4 AB4 4 VAL A 166 THR A 168 -1 N HIS A 167 O VAL A 184 SHEET 1 AB5 4 SER A 123 LEU A 127 0 SHEET 2 AB5 4 THR A 138 TYR A 148 -1 O LEU A 144 N PHE A 125 SHEET 3 AB5 4 TYR A 179 PRO A 188 -1 O VAL A 187 N ALA A 139 SHEET 4 AB5 4 VAL A 172 LEU A 173 -1 N VAL A 172 O SER A 180 SHEET 1 AB6 3 THR A 154 TRP A 157 0 SHEET 2 AB6 3 THR A 198 HIS A 203 -1 O ASN A 200 N SER A 156 SHEET 3 AB6 3 THR A 208 ARG A 213 -1 O VAL A 210 N VAL A 201 SHEET 1 AB7 4 LEU D 4 SER D 7 0 SHEET 2 AB7 4 ALA D 19 SER D 25 -1 O SER D 22 N SER D 7 SHEET 3 AB7 4 ASP D 75 ILE D 80 -1 O LEU D 78 N ILE D 21 SHEET 4 AB7 4 PHE D 67 SER D 72 -1 N THR D 68 O LYS D 79 SHEET 1 AB8 6 THR D 10 VAL D 13 0 SHEET 2 AB8 6 THR D 107 LEU D 111 1 O GLU D 110 N LEU D 11 SHEET 3 AB8 6 GLY D 89 GLN D 95 -1 N GLY D 89 O LEU D 109 SHEET 4 AB8 6 LEU D 38 GLN D 43 -1 N LEU D 41 O TYR D 92 SHEET 5 AB8 6 LYS D 50 TYR D 54 -1 O ILE D 53 N TRP D 40 SHEET 6 AB8 6 LYS D 58 VAL D 59 -1 O LYS D 58 N TYR D 54 SHEET 1 AB9 4 THR D 10 VAL D 13 0 SHEET 2 AB9 4 THR D 107 LEU D 111 1 O GLU D 110 N LEU D 11 SHEET 3 AB9 4 GLY D 89 GLN D 95 -1 N GLY D 89 O LEU D 109 SHEET 4 AB9 4 THR D 102 PHE D 103 -1 O THR D 102 N GLN D 95 SHEET 1 AC1 4 SER D 120 PHE D 124 0 SHEET 2 AC1 4 THR D 135 PHE D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AC1 4 TYR D 179 SER D 188 -1 O LEU D 185 N VAL D 138 SHEET 4 AC1 4 SER D 165 VAL D 169 -1 N SER D 168 O SER D 182 SHEET 1 AC2 4 ALA D 159 LEU D 160 0 SHEET 2 AC2 4 LYS D 151 VAL D 156 -1 N VAL D 156 O ALA D 159 SHEET 3 AC2 4 VAL D 197 THR D 203 -1 O GLU D 201 N GLN D 153 SHEET 4 AC2 4 VAL D 211 ASN D 216 -1 O VAL D 211 N VAL D 202 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 2 CYS H 130 CYS L 220 1555 1555 2.03 SSBOND 3 CYS H 143 CYS H 199 1555 1555 2.04 SSBOND 4 CYS L 23 CYS L 93 1555 1555 2.05 SSBOND 5 CYS L 140 CYS L 200 1555 1555 2.03 SSBOND 6 CYS A 22 CYS A 96 1555 1555 2.05 SSBOND 7 CYS A 130 CYS D 220 1555 1555 2.02 SSBOND 8 CYS A 143 CYS A 199 1555 1555 2.04 SSBOND 9 CYS D 23 CYS D 93 1555 1555 2.06 SSBOND 10 CYS D 140 CYS D 200 1555 1555 2.05 CISPEP 1 PHE H 149 PRO H 150 0 -5.66 CISPEP 2 GLU H 151 PRO H 152 0 1.73 CISPEP 3 SER L 7 PRO L 8 0 -3.05 CISPEP 4 PHE L 99 PRO L 100 0 -8.65 CISPEP 5 TYR L 146 PRO L 147 0 1.54 CISPEP 6 PHE A 149 PRO A 150 0 -6.28 CISPEP 7 GLU A 151 PRO A 152 0 1.70 CISPEP 8 SER D 7 PRO D 8 0 -2.51 CISPEP 9 PHE D 99 PRO D 100 0 -7.97 CISPEP 10 TYR D 146 PRO D 147 0 0.61 CRYST1 71.160 65.290 100.140 90.00 97.90 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014053 0.000000 0.001951 0.00000 SCALE2 0.000000 0.015316 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010082 0.00000