HEADER VIRAL PROTEIN 28-SEP-22 8EN5 TITLE STRUCTURE OF NANOBODY 56 IN COMPLEX WITH DOMINANT NOROVIRUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: GII.4 P DOMAIN; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY 56; COMPND 7 CHAIN: E, F, G, H; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NOROVIRUS; SOURCE 3 ORGANISM_TAXID: 142786; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 8 ORGANISM_TAXID: 30538; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NOROVIRUS, NANOBODY, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.KHER,C.SABIN,M.PANCERA,A.KOROMYSLOVA,G.HANSMAN JRNL AUTH G.KHER,C.SABIN,M.PANCERA,A.KOROMYSLOVA,G.HANSMAN JRNL TITL STRUCTURE OF NANOBODY 56 IN COMPLEX WITH DOMINANT NOROVIRUS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 3 NUMBER OF REFLECTIONS : 480738 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.188 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.219 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 23818 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 68.3800 - 4.9700 0.96 15307 794 0.1539 0.1776 REMARK 3 2 4.9700 - 3.9500 0.97 15470 791 0.1385 0.1705 REMARK 3 3 3.9500 - 3.4500 0.96 15319 836 0.1707 0.1888 REMARK 3 4 3.4500 - 3.1300 0.98 15713 796 0.1809 0.1970 REMARK 3 5 3.1300 - 2.9100 0.98 15657 780 0.1842 0.2481 REMARK 3 6 2.9100 - 2.7400 0.96 15313 772 0.1920 0.2335 REMARK 3 7 2.7400 - 2.6000 0.95 15129 769 0.1877 0.2256 REMARK 3 8 2.6000 - 2.4900 0.98 15685 833 0.1957 0.2324 REMARK 3 9 2.4900 - 2.3900 0.97 15348 847 0.1954 0.2352 REMARK 3 10 2.3900 - 2.3100 0.96 15424 759 0.1920 0.2292 REMARK 3 11 2.3100 - 2.2400 0.97 15463 801 0.1897 0.2147 REMARK 3 12 2.2400 - 2.1700 0.97 15345 837 0.1883 0.2380 REMARK 3 13 2.1700 - 2.1100 0.92 14710 823 0.2020 0.2457 REMARK 3 14 2.1100 - 2.0600 0.94 15009 814 0.1987 0.2272 REMARK 3 15 2.0600 - 2.0200 0.96 15202 786 0.1977 0.2556 REMARK 3 16 2.0200 - 1.9700 0.96 15294 798 0.2029 0.2312 REMARK 3 17 1.9700 - 1.9300 0.96 15313 770 0.2059 0.2413 REMARK 3 18 1.9300 - 1.9000 0.96 15410 742 0.2098 0.2467 REMARK 3 19 1.9000 - 1.8600 0.96 15268 809 0.2181 0.2524 REMARK 3 20 1.8600 - 1.8300 0.96 15330 754 0.2275 0.2598 REMARK 3 21 1.8300 - 1.8000 0.95 15143 745 0.2240 0.2517 REMARK 3 22 1.8000 - 1.7700 0.92 14857 789 0.2274 0.2656 REMARK 3 23 1.7700 - 1.7500 0.92 14639 769 0.2267 0.2548 REMARK 3 24 1.7500 - 1.7200 0.95 15143 820 0.2346 0.2718 REMARK 3 25 1.7200 - 1.7000 0.95 15034 876 0.2388 0.2578 REMARK 3 26 1.7000 - 1.6800 0.95 15153 735 0.2407 0.2909 REMARK 3 27 1.6800 - 1.6600 0.95 15003 795 0.2482 0.2739 REMARK 3 28 1.6600 - 1.6400 0.94 15158 780 0.2568 0.2964 REMARK 3 29 1.6400 - 1.6200 0.94 15007 816 0.2695 0.3113 REMARK 3 30 1.6200 - 1.6000 0.94 15074 782 0.2775 0.3090 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) : 0.180 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.310 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.49 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.88 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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 8EN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000267281. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-OCT-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 : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P14 (MX2) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97658 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 : MOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 480738 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 68.380 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.04900 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) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 0.41200 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: 4OOS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: (10% [W/V] PEG8000 AND 0.1 M MES [PH REMARK 280 6.0]), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K 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 117.69200 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 14110 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 54.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10370 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 33200 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H 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 ASN A 532 REMARK 465 GLY A 533 REMARK 465 THR A 534 REMARK 465 GLY A 535 REMARK 465 ARG A 536 REMARK 465 ARG A 537 REMARK 465 ARG A 538 REMARK 465 ALA A 539 REMARK 465 VAL A 540 REMARK 465 ASN B 531 REMARK 465 GLY B 532 REMARK 465 THR B 533 REMARK 465 GLY B 534 REMARK 465 ARG B 535 REMARK 465 ARG B 536 REMARK 465 ARG B 537 REMARK 465 ALA B 538 REMARK 465 VAL B 539 REMARK 465 HIS E 127 REMARK 465 HIS E 128 REMARK 465 HIS E 129 REMARK 465 HIS E 130 REMARK 465 HIS E 131 REMARK 465 HIS F 126 REMARK 465 HIS F 127 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 ASN C 532 REMARK 465 GLY C 533 REMARK 465 THR C 534 REMARK 465 GLY C 535 REMARK 465 ARG C 536 REMARK 465 ARG C 537 REMARK 465 ARG C 538 REMARK 465 ALA C 539 REMARK 465 VAL C 540 REMARK 465 THR D 224 REMARK 465 GLY D 531 REMARK 465 ASN D 532 REMARK 465 GLY D 533 REMARK 465 THR D 534 REMARK 465 GLY D 535 REMARK 465 ARG D 536 REMARK 465 ARG D 537 REMARK 465 ARG D 538 REMARK 465 ALA D 539 REMARK 465 VAL D 540 REMARK 465 SER H 125 REMARK 465 HIS H 126 REMARK 465 HIS H 127 REMARK 465 HIS H 128 REMARK 465 HIS H 129 REMARK 465 HIS H 130 REMARK 465 HIS H 131 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 SER G 125 NE2 HIS G 129 2.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS H 50 CB CYS H 50 SG -0.110 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 A 260 49.16 -142.98 REMARK 500 ARG A 373 -13.33 -152.92 REMARK 500 SER A 442 148.84 -175.68 REMARK 500 GLN B 260 53.96 -143.67 REMARK 500 ARG B 373 -14.93 -154.41 REMARK 500 ASP B 374 42.02 -102.72 REMARK 500 ARG B 410 4.90 -69.66 REMARK 500 SER B 441 143.92 -179.00 REMARK 500 LEU E 29 -103.58 75.82 REMARK 500 VAL E 48 -64.10 -106.02 REMARK 500 ASN E 77 52.07 31.40 REMARK 500 THR E 100 35.41 -84.00 REMARK 500 LEU F 29 -100.27 75.77 REMARK 500 VAL F 48 -60.90 -109.65 REMARK 500 THR F 100 39.79 -85.06 REMARK 500 GLN C 260 52.42 -144.99 REMARK 500 ARG C 373 -13.61 -147.58 REMARK 500 SER C 442 142.52 -177.92 REMARK 500 SER D 442 164.92 168.83 REMARK 500 LEU G 29 -101.45 77.57 REMARK 500 VAL G 48 -61.69 -108.14 REMARK 500 ALA G 92 167.65 174.98 REMARK 500 THR G 100 35.31 -87.43 REMARK 500 LEU H 29 -114.40 71.35 REMARK 500 SER H 85 61.80 37.69 REMARK 500 THR H 100 30.65 -86.85 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 ARG B 410 ASN B 411 -149.67 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 A1022 DISTANCE = 5.84 ANGSTROMS REMARK 525 HOH B 977 DISTANCE = 5.81 ANGSTROMS REMARK 525 HOH B 978 DISTANCE = 6.47 ANGSTROMS DBREF 8EN5 A 224 540 UNP K4LM89 K4LM89_9CALI 224 540 DBREF 8EN5 B 224 539 UNP K4LM89 K4LM89_9CALI 224 540 DBREF 8EN5 E 1 131 PDB 8EN5 8EN5 1 131 DBREF 8EN5 F 1 131 PDB 8EN5 8EN5 1 131 DBREF 8EN5 C 224 540 UNP K4LM89 K4LM89_9CALI 224 540 DBREF 8EN5 D 224 540 UNP K4LM89 K4LM89_9CALI 224 540 DBREF 8EN5 G 1 131 PDB 8EN5 8EN5 1 131 DBREF 8EN5 H 1 131 PDB 8EN5 8EN5 1 131 SEQRES 1 A 317 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 A 317 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 A 317 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 A 317 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 A 317 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 A 317 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 A 317 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 A 317 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 A 317 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 A 317 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 A 317 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 A 317 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 A 317 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 A 317 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 A 317 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 A 317 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 A 317 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 A 317 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 A 317 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 A 317 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 A 317 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 A 317 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 A 317 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 A 317 GLN PHE TYR THR LEU ALA PRO MET GLY ASN GLY THR GLY SEQRES 25 A 317 ARG ARG ARG ALA VAL SEQRES 1 B 317 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 B 317 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 B 317 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 B 317 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 B 317 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 B 317 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 B 317 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 B 317 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 B 317 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 B 317 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 B 317 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 B 317 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 B 317 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 B 317 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 B 317 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 B 317 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 B 317 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 B 317 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 B 317 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 B 317 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 B 317 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 B 317 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 B 317 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 B 317 GLN PHE TYR THR LEU ALA PRO MET GLY ASN GLY THR GLY SEQRES 25 B 317 ARG ARG ARG ALA VAL SEQRES 1 E 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 131 PRO GLY ASP SER LEU ARG LEU SER CYS ALA THR SER GLY SEQRES 3 E 131 PHE ILE LEU GLY ARG PRO VAL ILE THR TRP PHE ARG GLN SEQRES 4 E 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL LEU CYS ILE SER SEQRES 5 E 131 GLY SER ASP GLU ILE THR TYR PHE ILE ASP SER VAL LYS SEQRES 6 E 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 E 131 VAL TYR LEU GLN ILE ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 E 131 ALA ASN TYR TYR CYS ALA ALA ARG THR PHE THR ALA GLY SEQRES 9 E 131 CYS TYR SER ARG SER ILE ALA TYR PRO TYR TRP GLY GLN SEQRES 10 E 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 E 131 HIS SEQRES 1 F 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 131 PRO GLY ASP SER LEU ARG LEU SER CYS ALA THR SER GLY SEQRES 3 F 131 PHE ILE LEU GLY ARG PRO VAL ILE THR TRP PHE ARG GLN SEQRES 4 F 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL LEU CYS ILE SER SEQRES 5 F 131 GLY SER ASP GLU ILE THR TYR PHE ILE ASP SER VAL LYS SEQRES 6 F 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 F 131 VAL TYR LEU GLN ILE ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 F 131 ALA ASN TYR TYR CYS ALA ALA ARG THR PHE THR ALA GLY SEQRES 9 F 131 CYS TYR SER ARG SER ILE ALA TYR PRO TYR TRP GLY GLN SEQRES 10 F 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 F 131 HIS SEQRES 1 C 317 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 C 317 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 C 317 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 C 317 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 C 317 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 C 317 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 C 317 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 C 317 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 C 317 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 C 317 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 C 317 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 C 317 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 C 317 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 C 317 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 C 317 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 C 317 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 C 317 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 C 317 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 C 317 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 C 317 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 C 317 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 C 317 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 C 317 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 C 317 GLN PHE TYR THR LEU ALA PRO MET GLY ASN GLY THR GLY SEQRES 25 C 317 ARG ARG ARG ALA VAL SEQRES 1 D 317 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 D 317 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 D 317 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 D 317 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 D 317 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 D 317 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 D 317 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 D 317 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 D 317 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 D 317 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 D 317 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 D 317 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 D 317 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 D 317 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 D 317 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 D 317 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 D 317 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 D 317 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 D 317 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 D 317 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 D 317 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 D 317 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 D 317 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 D 317 GLN PHE TYR THR LEU ALA PRO MET GLY ASN GLY THR GLY SEQRES 25 D 317 ARG ARG ARG ALA VAL SEQRES 1 G 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 131 PRO GLY ASP SER LEU ARG LEU SER CYS ALA THR SER GLY SEQRES 3 G 131 PHE ILE LEU GLY ARG PRO VAL ILE THR TRP PHE ARG GLN SEQRES 4 G 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL LEU CYS ILE SER SEQRES 5 G 131 GLY SER ASP GLU ILE THR TYR PHE ILE ASP SER VAL LYS SEQRES 6 G 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 G 131 VAL TYR LEU GLN ILE ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 G 131 ALA ASN TYR TYR CYS ALA ALA ARG THR PHE THR ALA GLY SEQRES 9 G 131 CYS TYR SER ARG SER ILE ALA TYR PRO TYR TRP GLY GLN SEQRES 10 G 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 G 131 HIS SEQRES 1 H 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 131 PRO GLY ASP SER LEU ARG LEU SER CYS ALA THR SER GLY SEQRES 3 H 131 PHE ILE LEU GLY ARG PRO VAL ILE THR TRP PHE ARG GLN SEQRES 4 H 131 ALA PRO GLY LYS GLU ARG GLU GLY VAL LEU CYS ILE SER SEQRES 5 H 131 GLY SER ASP GLU ILE THR TYR PHE ILE ASP SER VAL LYS SEQRES 6 H 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 H 131 VAL TYR LEU GLN ILE ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 H 131 ALA ASN TYR TYR CYS ALA ALA ARG THR PHE THR ALA GLY SEQRES 9 H 131 CYS TYR SER ARG SER ILE ALA TYR PRO TYR TRP GLY GLN SEQRES 10 H 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 H 131 HIS HET EDO A 601 4 HET EDO A 602 4 HET EDO A 603 4 HET EDO A 604 4 HET EDO A 605 4 HET EDO A 606 4 HET EDO A 607 4 HET MES A 608 12 HET EDO A 609 10 HET EDO B 601 4 HET EDO B 602 4 HET EDO B 603 4 HET EDO B 604 4 HET EDO B 605 4 HET EDO B 606 4 HET EDO B 607 4 HET EDO B 608 4 HET EDO B 609 4 HET EDO B 610 4 HET EDO B 611 10 HET EDO B 612 10 HET EDO B 613 10 HET EDO E 201 10 HET EDO F 201 4 HET EDO F 202 4 HET EDO F 203 4 HET EDO C 601 4 HET EDO C 602 4 HET EDO C 603 4 HET EDO C 604 4 HET EDO C 605 10 HET EDO D 601 4 HET EDO D 602 4 HET EDO D 603 4 HET EDO D 604 4 HET EDO G 201 4 HET EDO H 201 4 HETNAM EDO 1,2-ETHANEDIOL HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID HETSYN EDO ETHYLENE GLYCOL FORMUL 9 EDO 36(C2 H6 O2) FORMUL 16 MES C6 H13 N O4 S FORMUL 46 HOH *1317(H2 O) HELIX 1 AA1 THR A 233 MET A 237 5 5 HELIX 2 AA2 SER A 279 ILE A 283 5 5 HELIX 3 AA3 PRO A 360 LEU A 362 5 3 HELIX 4 AA4 PRO A 454 ALA A 465 1 12 HELIX 5 AA5 THR B 233 MET B 237 5 5 HELIX 6 AA6 SER B 279 ILE B 283 5 5 HELIX 7 AA7 ALA B 359 LEU B 362 5 4 HELIX 8 AA8 PRO B 453 ALA B 464 1 12 HELIX 9 AA9 ILE E 61 LYS E 65 5 5 HELIX 10 AB1 ASN E 74 LYS E 76 5 3 HELIX 11 AB2 LYS E 87 THR E 91 5 5 HELIX 12 AB3 ARG E 108 TYR E 112 5 5 HELIX 13 AB4 ILE F 61 LYS F 65 5 5 HELIX 14 AB5 ASN F 74 LYS F 76 5 3 HELIX 15 AB6 LYS F 87 THR F 91 5 5 HELIX 16 AB7 ARG F 108 TYR F 112 5 5 HELIX 17 AB8 SER C 279 ILE C 283 5 5 HELIX 18 AB9 ALA C 359 LEU C 362 5 4 HELIX 19 AC1 PRO C 454 ALA C 465 1 12 HELIX 20 AC2 THR D 233 MET D 237 5 5 HELIX 21 AC3 SER D 279 ILE D 283 5 5 HELIX 22 AC4 ALA D 359 LEU D 362 5 4 HELIX 23 AC5 PRO D 454 ALA D 465 1 12 HELIX 24 AC6 ILE G 61 LYS G 65 5 5 HELIX 25 AC7 ASN G 74 LYS G 76 5 3 HELIX 26 AC8 LYS G 87 THR G 91 5 5 HELIX 27 AC9 ARG G 108 TYR G 112 5 5 HELIX 28 AD1 ASN H 74 LYS H 76 5 3 HELIX 29 AD2 LYS H 87 THR H 91 5 5 HELIX 30 AD3 ARG H 108 TYR H 112 5 5 SHEET 1 AA1 9 LYS A 248 THR A 251 0 SHEET 2 AA1 9 GLU A 429 THR A 437 -1 O PHE A 433 N PHE A 250 SHEET 3 AA1 9 ASP A 448 CYS A 451 -1 O CYS A 451 N PHE A 434 SHEET 4 AA1 9 VAL A 472 VAL A 478 0 SHEET 5 AA1 9 VAL A 485 HIS A 492 -1 O LEU A 491 N ALA A 473 SHEET 6 AA1 9 TYR A 496 ALA A 500 -1 O TYR A 496 N HIS A 492 SHEET 7 AA1 9 HIS A 505 VAL A 508 -1 O LEU A 507 N LEU A 249 SHEET 8 AA1 9 TYR A 514 VAL A 521 -1 O SER A 519 N LEU A 474 SHEET 9 AA1 9 PHE E 27 LEU E 29 1 O ILE E 28 N VAL A 508 SHEET 1 AA215 PHE A 286 HIS A 292 0 SHEET 2 AA215 ASN A 298 LEU A 303 -1 O THR A 300 N THR A 291 SHEET 3 AA215 LYS A 329 THR A 337 0 SHEET 4 AA215 THR A 344 TYR A 352 -1 O ALA A 349 N GLY A 332 SHEET 5 AA215 PHE A 358 ALA A 359 0 SHEET 6 AA215 ARG A 364 THR A 369 -1 O ARG A 364 N ALA A 359 SHEET 7 AA215 THR A 381 ILE A 389 -1 O LYS A 382 N THR A 335 SHEET 8 AA215 GLY A 440 GLY A 443 1 O CYS A 441 N VAL A 388 SHEET 9 AA215 PHE B 286 THR B 291 0 SHEET 10 AA215 ASN B 298 LEU B 303 -1 O THR B 300 N THR B 291 SHEET 11 AA215 LYS B 329 THR B 337 0 SHEET 12 AA215 THR B 344 TYR B 352 -1 O HIS B 347 N LEU B 334 SHEET 13 AA215 ARG B 364 THR B 369 -1 O GLU B 368 N THR B 350 SHEET 14 AA215 THR B 381 ILE B 389 -1 O LYS B 382 N THR B 335 SHEET 15 AA215 GLY B 439 GLY B 442 1 O CYS B 440 N VAL B 388 SHEET 1 AA3 9 LYS B 248 GLY B 252 0 SHEET 2 AA3 9 GLU B 428 THR B 436 -1 O PHE B 432 N PHE B 250 SHEET 3 AA3 9 ASP B 447 CYS B 450 -1 O CYS B 450 N PHE B 433 SHEET 4 AA3 9 VAL B 471 VAL B 477 0 SHEET 5 AA3 9 VAL B 484 HIS B 491 -1 O LEU B 490 N ALA B 472 SHEET 6 AA3 9 TYR B 495 ALA B 499 -1 O TYR B 495 N HIS B 491 SHEET 7 AA3 9 HIS B 504 VAL B 507 -1 O LEU B 506 N LEU B 249 SHEET 8 AA3 9 TYR B 513 VAL B 520 -1 O SER B 518 N LEU B 473 SHEET 9 AA3 9 PHE F 27 LEU F 29 1 O ILE F 28 N VAL B 507 SHEET 1 AA4 4 GLN E 3 SER E 7 0 SHEET 2 AA4 4 LEU E 18 SER E 25 -1 O ALA E 23 N GLN E 5 SHEET 3 AA4 4 THR E 78 ILE E 83 -1 O LEU E 81 N LEU E 20 SHEET 4 AA4 4 PHE E 68 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AA5 7 GLY E 10 VAL E 12 0 SHEET 2 AA5 7 ILE E 34 GLN E 39 0 SHEET 3 AA5 7 GLU E 46 ILE E 51 -1 O VAL E 48 N TRP E 36 SHEET 4 AA5 7 ILE E 57 TYR E 59 -1 O THR E 58 N CYS E 50 SHEET 5 AA5 7 ALA E 92 ALA E 98 -1 O TYR E 95 N PHE E 37 SHEET 6 AA5 7 TYR E 114 TRP E 115 -1 O TYR E 114 N ALA E 98 SHEET 7 AA5 7 THR E 119 VAL E 123 -1 O VAL E 121 N ALA E 92 SHEET 1 AA6 4 GLN F 3 SER F 7 0 SHEET 2 AA6 4 LEU F 18 SER F 25 -1 O ALA F 23 N GLN F 5 SHEET 3 AA6 4 THR F 78 ILE F 83 -1 O ILE F 83 N LEU F 18 SHEET 4 AA6 4 PHE F 68 ASP F 73 -1 N ASP F 73 O THR F 78 SHEET 1 AA7 7 GLY F 10 VAL F 12 0 SHEET 2 AA7 7 ILE F 34 GLN F 39 0 SHEET 3 AA7 7 GLU F 46 ILE F 51 -1 O GLU F 46 N ARG F 38 SHEET 4 AA7 7 ILE F 57 TYR F 59 -1 O THR F 58 N CYS F 50 SHEET 5 AA7 7 ALA F 92 ALA F 98 -1 O TYR F 95 N PHE F 37 SHEET 6 AA7 7 TYR F 114 TRP F 115 -1 O TYR F 114 N ALA F 98 SHEET 7 AA7 7 THR F 119 VAL F 123 -1 O VAL F 121 N ALA F 92 SHEET 1 AA8 9 LYS C 248 THR C 251 0 SHEET 2 AA8 9 GLU C 429 THR C 437 -1 O PHE C 433 N PHE C 250 SHEET 3 AA8 9 ASP C 448 CYS C 451 -1 O CYS C 451 N PHE C 434 SHEET 4 AA8 9 VAL C 472 VAL C 478 0 SHEET 5 AA8 9 VAL C 485 HIS C 492 -1 O LEU C 491 N ALA C 473 SHEET 6 AA8 9 TYR C 496 ALA C 500 -1 O TYR C 496 N HIS C 492 SHEET 7 AA8 9 HIS C 505 VAL C 508 -1 O LEU C 507 N LEU C 249 SHEET 8 AA8 9 TYR C 514 VAL C 521 -1 O SER C 519 N LEU C 474 SHEET 9 AA8 9 PHE G 27 LEU G 29 1 O ILE G 28 N VAL C 508 SHEET 1 AA914 PHE C 286 HIS C 292 0 SHEET 2 AA914 ASN C 298 LEU C 303 -1 O THR C 300 N THR C 291 SHEET 3 AA914 LYS C 329 THR C 337 0 SHEET 4 AA914 THR C 344 TYR C 352 -1 O HIS C 347 N LEU C 334 SHEET 5 AA914 ARG C 364 THR C 369 -1 O GLU C 368 N THR C 350 SHEET 6 AA914 THR C 381 ILE C 389 -1 O LYS C 382 N THR C 335 SHEET 7 AA914 GLY C 440 GLY C 443 1 O CYS C 441 N VAL C 388 SHEET 8 AA914 PHE D 286 ILE D 293 0 SHEET 9 AA914 ASN D 298 ALA D 304 -1 O ALA D 304 N ARG D 287 SHEET 10 AA914 LYS D 329 THR D 337 0 SHEET 11 AA914 THR D 344 TYR D 352 -1 O HIS D 347 N LEU D 334 SHEET 12 AA914 ARG D 364 THR D 369 -1 O GLU D 368 N THR D 350 SHEET 13 AA914 THR D 381 ILE D 389 -1 O LYS D 382 N THR D 335 SHEET 14 AA914 GLY D 440 GLY D 443 1 O CYS D 441 N VAL D 388 SHEET 1 AB1 9 LYS D 248 GLY D 252 0 SHEET 2 AB1 9 GLU D 429 THR D 437 -1 O PHE D 433 N PHE D 250 SHEET 3 AB1 9 ASP D 448 CYS D 451 -1 O LEU D 449 N SER D 436 SHEET 4 AB1 9 VAL D 472 VAL D 478 0 SHEET 5 AB1 9 VAL D 485 HIS D 492 -1 O LEU D 491 N ALA D 473 SHEET 6 AB1 9 TYR D 496 ALA D 500 -1 O THR D 498 N LYS D 490 SHEET 7 AB1 9 HIS D 505 VAL D 508 -1 O LEU D 507 N LEU D 249 SHEET 8 AB1 9 TYR D 514 VAL D 521 -1 O SER D 519 N LEU D 474 SHEET 9 AB1 9 PHE H 27 LEU H 29 1 O ILE H 28 N VAL D 508 SHEET 1 AB2 4 GLN G 3 SER G 7 0 SHEET 2 AB2 4 LEU G 18 SER G 25 -1 O SER G 21 N SER G 7 SHEET 3 AB2 4 THR G 78 ILE G 83 -1 O ILE G 83 N LEU G 18 SHEET 4 AB2 4 PHE G 68 ASP G 73 -1 N THR G 69 O GLN G 82 SHEET 1 AB3 7 GLY G 10 VAL G 12 0 SHEET 2 AB3 7 ILE G 34 GLN G 39 0 SHEET 3 AB3 7 GLU G 46 ILE G 51 -1 O VAL G 48 N TRP G 36 SHEET 4 AB3 7 ILE G 57 TYR G 59 -1 O THR G 58 N CYS G 50 SHEET 5 AB3 7 ALA G 92 ALA G 98 -1 O TYR G 95 N PHE G 37 SHEET 6 AB3 7 TYR G 114 TRP G 115 -1 O TYR G 114 N ALA G 98 SHEET 7 AB3 7 THR G 119 VAL G 123 -1 O THR G 119 N TYR G 94 SHEET 1 AB4 4 GLN H 3 SER H 7 0 SHEET 2 AB4 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AB4 4 THR H 78 ILE H 83 -1 O ILE H 83 N LEU H 18 SHEET 4 AB4 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB5 7 GLY H 10 VAL H 12 0 SHEET 2 AB5 7 ILE H 34 GLN H 39 0 SHEET 3 AB5 7 GLU H 46 ILE H 51 -1 O LEU H 49 N TRP H 36 SHEET 4 AB5 7 ILE H 57 TYR H 59 -1 O THR H 58 N CYS H 50 SHEET 5 AB5 7 ALA H 92 ALA H 98 -1 O TYR H 95 N PHE H 37 SHEET 6 AB5 7 TYR H 114 TRP H 115 -1 O TYR H 114 N ALA H 98 SHEET 7 AB5 7 THR H 119 VAL H 123 -1 O THR H 119 N TYR H 94 SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.06 SSBOND 2 CYS E 50 CYS E 105 1555 1555 2.02 SSBOND 3 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 4 CYS F 50 CYS F 105 1555 1555 2.01 SSBOND 5 CYS G 22 CYS G 96 1555 1555 2.07 SSBOND 6 CYS G 50 CYS G 105 1555 1555 2.05 SSBOND 7 CYS H 22 CYS H 96 1555 1555 2.01 SSBOND 8 CYS H 50 CYS H 105 1555 1555 2.05 CISPEP 1 GLU A 399 PRO A 400 0 -3.96 CISPEP 2 GLU B 398A PRO B 399 0 -10.07 CISPEP 3 GLU C 399 PRO C 400 0 -3.56 CISPEP 4 GLU D 399 PRO D 400 0 -2.98 CRYST1 61.244 235.384 70.566 90.00 104.30 90.00 P 1 21 1 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 0.016328 0.000000 0.004161 0.00000 SCALE2 0.000000 0.004248 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014624 0.00000