HEADER MEMBRANE PROTEIN 29-MAR-23 8IVW TITLE CRYSTAL STRUCTURE OF NRP2 IN COMPLEX WITH ANRP2-10 FAB FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROPILIN-2; COMPND 3 CHAIN: A, D, G, J; COMPND 4 SYNONYM: VASCULAR ENDOTHELIAL CELL GROWTH FACTOR 165 RECEPTOR 2; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHIAN OF ANTIBODY 10V8 FAB FRAGMENT; COMPND 8 CHAIN: B, E, H, K; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN OF ANTIBODY 10V8 FAB FRAGMENT; COMPND 12 CHAIN: C, F, I, L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: NRP2, VEGF165R2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS COMPLEX, ANTIBODY, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.GENG,L.ZHAI JRNL AUTH Z.XU,H.L.GOEL,C.BURKART,L.BURMAN,Y.E.CHONG,A.G.BARBER, JRNL AUTH 2 Y.GENG,L.ZHAI,M.WANG,A.KUMAR,A.MENEFEE,C.POLIZZI,L.EIDE, JRNL AUTH 3 K.RAUCH,J.RAHMAN,K.HAMEL,Z.FOGASSY,S.KLOPP-SAVINO,S.PAZ, JRNL AUTH 4 M.ZHANG,A.CUBITT,L.A.NANGLE,A.M.MERCURIO JRNL TITL INHIBITION OF VEGF BINDING TO NEUROPILIN-2 ENHANCES JRNL TITL 2 CHEMOSENSITIVITY AND INHIBITS METASTASIS IN TRIPLE-NEGATIVE JRNL TITL 3 BREAST CANCER. JRNL REF SCI TRANSL MED V. 15 F1128 2023 JRNL REFN ESSN 1946-6242 JRNL PMID 37134152 JRNL DOI 10.1126/SCITRANSLMED.ADF1128 REMARK 2 REMARK 2 RESOLUTION. 3.21 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0352 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) : 3.21 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.65 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6 REMARK 3 NUMBER OF REFLECTIONS : 62689 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.248 REMARK 3 FREE R VALUE : 0.294 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3309 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.21 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.29 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4285 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.24 REMARK 3 BIN R VALUE (WORKING SET) : 0.3450 REMARK 3 BIN FREE R VALUE SET COUNT : 216 REMARK 3 BIN FREE R VALUE : 0.3740 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 26621 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.44 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.01800 REMARK 3 B22 (A**2) : 1.91100 REMARK 3 B33 (A**2) : -0.84800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.97500 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.646 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.581 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.687 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.859 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.805 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 27322 ; 0.006 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 24170 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 37165 ; 1.313 ; 1.651 REMARK 3 BOND ANGLES OTHERS (DEGREES): 56578 ; 0.477 ; 1.561 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3387 ; 6.879 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ; 5.769 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4422 ;24.159 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4078 ; 0.062 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30913 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 5447 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4710 ; 0.207 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 141 ; 0.316 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 12565 ; 0.180 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 398 ; 0.233 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL 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): 13629 ; 6.311 ; 8.800 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 13629 ; 6.310 ; 8.800 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16989 ;10.370 ;13.160 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 16990 ;10.371 ;13.161 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13693 ; 5.715 ; 9.213 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 13694 ; 5.715 ; 9.213 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 20176 ; 9.588 ;13.678 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 20177 ; 9.588 ;13.678 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 : 18 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 149 A 594 NULL REMARK 3 1 A 149 A 594 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 2 A 149 A 593 NULL REMARK 3 2 A 149 A 593 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 A 149 A 594 NULL REMARK 3 3 A 149 A 594 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 8 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 9 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 10 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 11 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 12 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 13 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 14 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 15 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 16 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 17 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 18 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT 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 : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8IVW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ. REMARK 100 THE DEPOSITION ID IS D_1300036613. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-MAY-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 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) : 0.97853 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66035 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : 0.27400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.3300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : 1.24700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG1000, 0.1M SODIUM CITRATE REMARK 280 TRIBASIC DIHYDRATE PH 5.5, 0.05M LITHIUM SULFATE MONOHYDRATE, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K 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 112.58200 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, 3, 4 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: A, B, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, 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 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 HIS A 13 REMARK 465 HIS A 14 REMARK 465 HIS A 15 REMARK 465 HIS A 16 REMARK 465 HIS A 17 REMARK 465 HIS A 18 REMARK 465 GLU A 19 REMARK 465 ASN A 20 REMARK 465 LEU A 21 REMARK 465 TYR A 22 REMARK 465 PHE A 23 REMARK 465 GLN A 24 REMARK 465 ASP A 25 REMARK 465 PRO A 26 REMARK 465 PRO A 27 REMARK 465 CYS A 28 REMARK 465 GLY A 29 REMARK 465 GLY A 30 REMARK 465 ARG A 31 REMARK 465 LEU A 32 REMARK 465 ASN A 33 REMARK 465 SER A 34 REMARK 465 LYS A 35 REMARK 465 ASP A 36 REMARK 465 ALA A 37 REMARK 465 GLY A 38 REMARK 465 TYR A 39 REMARK 465 ILE A 40 REMARK 465 THR A 41 REMARK 465 SER A 42 REMARK 465 PRO A 43 REMARK 465 GLY A 44 REMARK 465 TYR A 45 REMARK 465 PRO A 46 REMARK 465 GLN A 47 REMARK 465 ASP A 48 REMARK 465 TYR A 49 REMARK 465 PRO A 50 REMARK 465 SER A 51 REMARK 465 HIS A 52 REMARK 465 GLN A 53 REMARK 465 ASN A 54 REMARK 465 CYS A 55 REMARK 465 GLU A 56 REMARK 465 TRP A 57 REMARK 465 ILE A 58 REMARK 465 VAL A 59 REMARK 465 TYR A 60 REMARK 465 ALA A 61 REMARK 465 PRO A 62 REMARK 465 GLU A 63 REMARK 465 PRO A 64 REMARK 465 ASN A 65 REMARK 465 GLN A 66 REMARK 465 LYS A 67 REMARK 465 ILE A 68 REMARK 465 VAL A 69 REMARK 465 LEU A 70 REMARK 465 ASN A 71 REMARK 465 PHE A 72 REMARK 465 ASN A 73 REMARK 465 PRO A 74 REMARK 465 HIS A 75 REMARK 465 PHE A 76 REMARK 465 GLU A 77 REMARK 465 ILE A 78 REMARK 465 GLU A 79 REMARK 465 LYS A 80 REMARK 465 HIS A 81 REMARK 465 ASP A 82 REMARK 465 CYS A 83 REMARK 465 LYS A 84 REMARK 465 TYR A 85 REMARK 465 ASP A 86 REMARK 465 PHE A 87 REMARK 465 ILE A 88 REMARK 465 GLU A 89 REMARK 465 ILE A 90 REMARK 465 ARG A 91 REMARK 465 ASP A 92 REMARK 465 GLY A 93 REMARK 465 ASP A 94 REMARK 465 SER A 95 REMARK 465 GLU A 96 REMARK 465 SER A 97 REMARK 465 ALA A 98 REMARK 465 ASP A 99 REMARK 465 LEU A 100 REMARK 465 LEU A 101 REMARK 465 GLY A 102 REMARK 465 LYS A 103 REMARK 465 HIS A 104 REMARK 465 CYS A 105 REMARK 465 GLY A 106 REMARK 465 ASN A 107 REMARK 465 ILE A 108 REMARK 465 ALA A 109 REMARK 465 PRO A 110 REMARK 465 PRO A 111 REMARK 465 THR A 112 REMARK 465 ILE A 113 REMARK 465 ILE A 114 REMARK 465 SER A 115 REMARK 465 SER A 116 REMARK 465 GLY A 117 REMARK 465 SER A 118 REMARK 465 MET A 119 REMARK 465 LEU A 120 REMARK 465 TYR A 121 REMARK 465 ILE A 122 REMARK 465 LYS A 123 REMARK 465 PHE A 124 REMARK 465 THR A 125 REMARK 465 SER A 126 REMARK 465 ASP A 127 REMARK 465 TYR A 128 REMARK 465 ALA A 129 REMARK 465 ARG A 130 REMARK 465 GLN A 131 REMARK 465 GLY A 132 REMARK 465 ALA A 133 REMARK 465 GLY A 134 REMARK 465 PHE A 135 REMARK 465 SER A 136 REMARK 465 LEU A 137 REMARK 465 ARG A 138 REMARK 465 TYR A 139 REMARK 465 GLU A 140 REMARK 465 ILE A 141 REMARK 465 PHE A 142 REMARK 465 LYS A 143 REMARK 465 THR A 144 REMARK 465 GLY A 145 REMARK 465 SER A 146 REMARK 465 GLU A 147 REMARK 465 ASP A 148 REMARK 465 ASP A 199 REMARK 465 PRO A 200 REMARK 465 LEU A 201 REMARK 465 GLN A 202 REMARK 465 VAL A 203 REMARK 465 GLY A 204 REMARK 465 GLU A 205 REMARK 465 GLY A 206 REMARK 465 GLY A 493 REMARK 465 THR A 494 REMARK 465 PRO A 495 REMARK 465 GLY A 508 REMARK 465 GLY A 509 REMARK 465 ASP A 510 REMARK 465 SER A 511 REMARK 465 ILE A 512 REMARK 465 THR A 513 REMARK 465 ALA A 514 REMARK 465 VAL A 515 REMARK 465 GLU A 516 REMARK 465 THR A 595 REMARK 465 GLY B 220 REMARK 465 GLY B 221 REMARK 465 SER B 222 REMARK 465 HIS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 HIS D 13 REMARK 465 HIS D 14 REMARK 465 HIS D 15 REMARK 465 HIS D 16 REMARK 465 HIS D 17 REMARK 465 HIS D 18 REMARK 465 GLU D 19 REMARK 465 ASN D 20 REMARK 465 LEU D 21 REMARK 465 TYR D 22 REMARK 465 PHE D 23 REMARK 465 GLN D 24 REMARK 465 ASP D 25 REMARK 465 PRO D 26 REMARK 465 PRO D 27 REMARK 465 CYS D 28 REMARK 465 GLY D 29 REMARK 465 GLY D 30 REMARK 465 ARG D 31 REMARK 465 LEU D 32 REMARK 465 ASN D 33 REMARK 465 SER D 34 REMARK 465 LYS D 35 REMARK 465 ASP D 36 REMARK 465 ALA D 37 REMARK 465 GLY D 38 REMARK 465 TYR D 39 REMARK 465 ILE D 40 REMARK 465 THR D 41 REMARK 465 SER D 42 REMARK 465 PRO D 43 REMARK 465 GLY D 44 REMARK 465 TYR D 45 REMARK 465 PRO D 46 REMARK 465 GLN D 47 REMARK 465 ASP D 48 REMARK 465 TYR D 49 REMARK 465 PRO D 50 REMARK 465 SER D 51 REMARK 465 HIS D 52 REMARK 465 GLN D 53 REMARK 465 ASN D 54 REMARK 465 CYS D 55 REMARK 465 GLU D 56 REMARK 465 TRP D 57 REMARK 465 ILE D 58 REMARK 465 VAL D 59 REMARK 465 TYR D 60 REMARK 465 ALA D 61 REMARK 465 PRO D 62 REMARK 465 GLU D 63 REMARK 465 PRO D 64 REMARK 465 ASN D 65 REMARK 465 GLN D 66 REMARK 465 LYS D 67 REMARK 465 ILE D 68 REMARK 465 VAL D 69 REMARK 465 LEU D 70 REMARK 465 ASN D 71 REMARK 465 PHE D 72 REMARK 465 ASN D 73 REMARK 465 PRO D 74 REMARK 465 HIS D 75 REMARK 465 PHE D 76 REMARK 465 GLU D 77 REMARK 465 ILE D 78 REMARK 465 GLU D 79 REMARK 465 LYS D 80 REMARK 465 HIS D 81 REMARK 465 ASP D 82 REMARK 465 CYS D 83 REMARK 465 LYS D 84 REMARK 465 TYR D 85 REMARK 465 ASP D 86 REMARK 465 PHE D 87 REMARK 465 ILE D 88 REMARK 465 GLU D 89 REMARK 465 ILE D 90 REMARK 465 ARG D 91 REMARK 465 ASP D 92 REMARK 465 GLY D 93 REMARK 465 ASP D 94 REMARK 465 SER D 95 REMARK 465 GLU D 96 REMARK 465 SER D 97 REMARK 465 ALA D 98 REMARK 465 ASP D 99 REMARK 465 LEU D 100 REMARK 465 LEU D 101 REMARK 465 GLY D 102 REMARK 465 LYS D 103 REMARK 465 HIS D 104 REMARK 465 CYS D 105 REMARK 465 GLY D 106 REMARK 465 ASN D 107 REMARK 465 ILE D 108 REMARK 465 ALA D 109 REMARK 465 PRO D 110 REMARK 465 PRO D 111 REMARK 465 THR D 112 REMARK 465 ILE D 113 REMARK 465 ILE D 114 REMARK 465 SER D 115 REMARK 465 SER D 116 REMARK 465 GLY D 117 REMARK 465 SER D 118 REMARK 465 MET D 119 REMARK 465 LEU D 120 REMARK 465 TYR D 121 REMARK 465 ILE D 122 REMARK 465 LYS D 123 REMARK 465 PHE D 124 REMARK 465 THR D 125 REMARK 465 SER D 126 REMARK 465 ASP D 127 REMARK 465 TYR D 128 REMARK 465 ALA D 129 REMARK 465 ARG D 130 REMARK 465 GLN D 131 REMARK 465 GLY D 132 REMARK 465 ALA D 133 REMARK 465 GLY D 134 REMARK 465 PHE D 135 REMARK 465 SER D 136 REMARK 465 LEU D 137 REMARK 465 ARG D 138 REMARK 465 TYR D 139 REMARK 465 GLU D 140 REMARK 465 ILE D 141 REMARK 465 PHE D 142 REMARK 465 LYS D 143 REMARK 465 THR D 144 REMARK 465 GLY D 145 REMARK 465 SER D 146 REMARK 465 GLU D 147 REMARK 465 ASP D 199 REMARK 465 PRO D 200 REMARK 465 LEU D 201 REMARK 465 GLN D 202 REMARK 465 VAL D 203 REMARK 465 GLY D 204 REMARK 465 GLU D 205 REMARK 465 GLY D 206 REMARK 465 VAL D 267 REMARK 465 HIS D 268 REMARK 465 GLN D 269 REMARK 465 GLU D 270 REMARK 465 PRO D 271 REMARK 465 LEU D 272 REMARK 465 GLU D 273 REMARK 465 ASN D 274 REMARK 465 PHE D 275 REMARK 465 ARG D 507 REMARK 465 GLY D 508 REMARK 465 GLY D 509 REMARK 465 ASP D 510 REMARK 465 SER D 511 REMARK 465 ILE D 512 REMARK 465 THR D 513 REMARK 465 ALA D 514 REMARK 465 VAL D 515 REMARK 465 GLU D 516 REMARK 465 THR D 595 REMARK 465 GLY E 221 REMARK 465 SER E 222 REMARK 465 HIS E 223 REMARK 465 HIS E 224 REMARK 465 HIS E 225 REMARK 465 HIS E 226 REMARK 465 HIS E 227 REMARK 465 HIS E 228 REMARK 465 HIS G 13 REMARK 465 HIS G 14 REMARK 465 HIS G 15 REMARK 465 HIS G 16 REMARK 465 HIS G 17 REMARK 465 HIS G 18 REMARK 465 GLU G 19 REMARK 465 ASN G 20 REMARK 465 LEU G 21 REMARK 465 TYR G 22 REMARK 465 PHE G 23 REMARK 465 GLN G 24 REMARK 465 ASP G 25 REMARK 465 PRO G 26 REMARK 465 PRO G 27 REMARK 465 CYS G 28 REMARK 465 GLY G 29 REMARK 465 GLY G 30 REMARK 465 ARG G 31 REMARK 465 LEU G 32 REMARK 465 ASN G 33 REMARK 465 SER G 34 REMARK 465 LYS G 35 REMARK 465 ASP G 36 REMARK 465 ALA G 37 REMARK 465 GLY G 38 REMARK 465 TYR G 39 REMARK 465 ILE G 40 REMARK 465 THR G 41 REMARK 465 SER G 42 REMARK 465 PRO G 43 REMARK 465 GLY G 44 REMARK 465 TYR G 45 REMARK 465 PRO G 46 REMARK 465 GLN G 47 REMARK 465 ASP G 48 REMARK 465 TYR G 49 REMARK 465 PRO G 50 REMARK 465 SER G 51 REMARK 465 HIS G 52 REMARK 465 GLN G 53 REMARK 465 ASN G 54 REMARK 465 CYS G 55 REMARK 465 GLU G 56 REMARK 465 TRP G 57 REMARK 465 ILE G 58 REMARK 465 VAL G 59 REMARK 465 TYR G 60 REMARK 465 ALA G 61 REMARK 465 PRO G 62 REMARK 465 GLU G 63 REMARK 465 PRO G 64 REMARK 465 ASN G 65 REMARK 465 GLN G 66 REMARK 465 LYS G 67 REMARK 465 ILE G 68 REMARK 465 VAL G 69 REMARK 465 LEU G 70 REMARK 465 ASN G 71 REMARK 465 PHE G 72 REMARK 465 ASN G 73 REMARK 465 PRO G 74 REMARK 465 HIS G 75 REMARK 465 PHE G 76 REMARK 465 GLU G 77 REMARK 465 ILE G 78 REMARK 465 GLU G 79 REMARK 465 LYS G 80 REMARK 465 HIS G 81 REMARK 465 ASP G 82 REMARK 465 CYS G 83 REMARK 465 LYS G 84 REMARK 465 TYR G 85 REMARK 465 ASP G 86 REMARK 465 PHE G 87 REMARK 465 ILE G 88 REMARK 465 GLU G 89 REMARK 465 ILE G 90 REMARK 465 ARG G 91 REMARK 465 ASP G 92 REMARK 465 GLY G 93 REMARK 465 ASP G 94 REMARK 465 SER G 95 REMARK 465 GLU G 96 REMARK 465 SER G 97 REMARK 465 ALA G 98 REMARK 465 ASP G 99 REMARK 465 LEU G 100 REMARK 465 LEU G 101 REMARK 465 GLY G 102 REMARK 465 LYS G 103 REMARK 465 HIS G 104 REMARK 465 CYS G 105 REMARK 465 GLY G 106 REMARK 465 ASN G 107 REMARK 465 ILE G 108 REMARK 465 ALA G 109 REMARK 465 PRO G 110 REMARK 465 PRO G 111 REMARK 465 THR G 112 REMARK 465 ILE G 113 REMARK 465 ILE G 114 REMARK 465 SER G 115 REMARK 465 SER G 116 REMARK 465 GLY G 117 REMARK 465 SER G 118 REMARK 465 MET G 119 REMARK 465 LEU G 120 REMARK 465 TYR G 121 REMARK 465 ILE G 122 REMARK 465 LYS G 123 REMARK 465 PHE G 124 REMARK 465 THR G 125 REMARK 465 SER G 126 REMARK 465 ASP G 127 REMARK 465 TYR G 128 REMARK 465 ALA G 129 REMARK 465 ARG G 130 REMARK 465 GLN G 131 REMARK 465 GLY G 132 REMARK 465 ALA G 133 REMARK 465 GLY G 134 REMARK 465 PHE G 135 REMARK 465 SER G 136 REMARK 465 LEU G 137 REMARK 465 ARG G 138 REMARK 465 TYR G 139 REMARK 465 GLU G 140 REMARK 465 ILE G 141 REMARK 465 PHE G 142 REMARK 465 LYS G 143 REMARK 465 THR G 144 REMARK 465 GLY G 145 REMARK 465 SER G 146 REMARK 465 GLU G 147 REMARK 465 LEU G 180 REMARK 465 ALA G 181 REMARK 465 LYS G 182 REMARK 465 PRO G 183 REMARK 465 LYS G 184 REMARK 465 MET G 185 REMARK 465 GLU G 186 REMARK 465 ILE G 187 REMARK 465 ILE G 188 REMARK 465 ASP G 199 REMARK 465 PRO G 200 REMARK 465 LEU G 201 REMARK 465 GLN G 202 REMARK 465 VAL G 203 REMARK 465 GLY G 204 REMARK 465 GLU G 205 REMARK 465 GLY G 206 REMARK 465 PRO G 271 REMARK 465 LEU G 272 REMARK 465 GLU G 273 REMARK 465 ASN G 274 REMARK 465 SER G 454 REMARK 465 THR G 455 REMARK 465 GLN G 456 REMARK 465 GLU G 457 REMARK 465 TYR G 458 REMARK 465 LEU G 459 REMARK 465 TRP G 460 REMARK 465 GLY G 493 REMARK 465 THR G 494 REMARK 465 PRO G 495 REMARK 465 LYS G 496 REMARK 465 ARG G 507 REMARK 465 GLY G 508 REMARK 465 GLY G 509 REMARK 465 ASP G 510 REMARK 465 SER G 511 REMARK 465 ILE G 512 REMARK 465 THR G 513 REMARK 465 ALA G 514 REMARK 465 VAL G 515 REMARK 465 GLU G 516 REMARK 465 ALA G 517 REMARK 465 ARG G 518 REMARK 465 TRP G 594 REMARK 465 THR G 595 REMARK 465 GLY H 221 REMARK 465 SER H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 HIS J 13 REMARK 465 HIS J 14 REMARK 465 HIS J 15 REMARK 465 HIS J 16 REMARK 465 HIS J 17 REMARK 465 HIS J 18 REMARK 465 GLU J 19 REMARK 465 ASN J 20 REMARK 465 LEU J 21 REMARK 465 TYR J 22 REMARK 465 PHE J 23 REMARK 465 GLN J 24 REMARK 465 ASP J 25 REMARK 465 PRO J 26 REMARK 465 PRO J 27 REMARK 465 CYS J 28 REMARK 465 GLY J 29 REMARK 465 GLY J 30 REMARK 465 ARG J 31 REMARK 465 LEU J 32 REMARK 465 ASN J 33 REMARK 465 SER J 34 REMARK 465 LYS J 35 REMARK 465 ASP J 36 REMARK 465 ALA J 37 REMARK 465 GLY J 38 REMARK 465 TYR J 39 REMARK 465 ILE J 40 REMARK 465 THR J 41 REMARK 465 SER J 42 REMARK 465 PRO J 43 REMARK 465 GLY J 44 REMARK 465 TYR J 45 REMARK 465 PRO J 46 REMARK 465 GLN J 47 REMARK 465 ASP J 48 REMARK 465 TYR J 49 REMARK 465 PRO J 50 REMARK 465 SER J 51 REMARK 465 HIS J 52 REMARK 465 GLN J 53 REMARK 465 ASN J 54 REMARK 465 CYS J 55 REMARK 465 GLU J 56 REMARK 465 TRP J 57 REMARK 465 ILE J 58 REMARK 465 VAL J 59 REMARK 465 TYR J 60 REMARK 465 ALA J 61 REMARK 465 PRO J 62 REMARK 465 GLU J 63 REMARK 465 PRO J 64 REMARK 465 ASN J 65 REMARK 465 GLN J 66 REMARK 465 LYS J 67 REMARK 465 ILE J 68 REMARK 465 VAL J 69 REMARK 465 LEU J 70 REMARK 465 ASN J 71 REMARK 465 PHE J 72 REMARK 465 ASN J 73 REMARK 465 PRO J 74 REMARK 465 HIS J 75 REMARK 465 PHE J 76 REMARK 465 GLU J 77 REMARK 465 ILE J 78 REMARK 465 GLU J 79 REMARK 465 LYS J 80 REMARK 465 HIS J 81 REMARK 465 ASP J 82 REMARK 465 CYS J 83 REMARK 465 LYS J 84 REMARK 465 TYR J 85 REMARK 465 ASP J 86 REMARK 465 PHE J 87 REMARK 465 ILE J 88 REMARK 465 GLU J 89 REMARK 465 ILE J 90 REMARK 465 ARG J 91 REMARK 465 ASP J 92 REMARK 465 GLY J 93 REMARK 465 ASP J 94 REMARK 465 SER J 95 REMARK 465 GLU J 96 REMARK 465 SER J 97 REMARK 465 ALA J 98 REMARK 465 ASP J 99 REMARK 465 LEU J 100 REMARK 465 LEU J 101 REMARK 465 GLY J 102 REMARK 465 LYS J 103 REMARK 465 HIS J 104 REMARK 465 CYS J 105 REMARK 465 GLY J 106 REMARK 465 ASN J 107 REMARK 465 ILE J 108 REMARK 465 ALA J 109 REMARK 465 PRO J 110 REMARK 465 PRO J 111 REMARK 465 THR J 112 REMARK 465 ILE J 113 REMARK 465 ILE J 114 REMARK 465 SER J 115 REMARK 465 SER J 116 REMARK 465 GLY J 117 REMARK 465 SER J 118 REMARK 465 MET J 119 REMARK 465 LEU J 120 REMARK 465 TYR J 121 REMARK 465 ILE J 122 REMARK 465 LYS J 123 REMARK 465 PHE J 124 REMARK 465 THR J 125 REMARK 465 SER J 126 REMARK 465 ASP J 127 REMARK 465 TYR J 128 REMARK 465 ALA J 129 REMARK 465 ARG J 130 REMARK 465 GLN J 131 REMARK 465 GLY J 132 REMARK 465 ALA J 133 REMARK 465 GLY J 134 REMARK 465 PHE J 135 REMARK 465 SER J 136 REMARK 465 LEU J 137 REMARK 465 ARG J 138 REMARK 465 TYR J 139 REMARK 465 GLU J 140 REMARK 465 ILE J 141 REMARK 465 PHE J 142 REMARK 465 LYS J 143 REMARK 465 THR J 144 REMARK 465 GLY J 145 REMARK 465 SER J 146 REMARK 465 GLU J 147 REMARK 465 ASP J 199 REMARK 465 PRO J 200 REMARK 465 LEU J 201 REMARK 465 GLN J 202 REMARK 465 VAL J 203 REMARK 465 GLY J 204 REMARK 465 GLU J 205 REMARK 465 GLY J 206 REMARK 465 ARG J 507 REMARK 465 GLY J 508 REMARK 465 GLY J 509 REMARK 465 ASP J 510 REMARK 465 SER J 511 REMARK 465 ILE J 512 REMARK 465 THR J 513 REMARK 465 ALA J 514 REMARK 465 VAL J 515 REMARK 465 GLU J 516 REMARK 465 LYS J 547 REMARK 465 LEU J 548 REMARK 465 THR J 595 REMARK 465 GLY K 221 REMARK 465 SER K 222 REMARK 465 HIS K 223 REMARK 465 HIS K 224 REMARK 465 HIS K 225 REMARK 465 HIS K 226 REMARK 465 HIS K 227 REMARK 465 HIS K 228 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG D 239 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 477 CG CD NE CZ NH1 NH2 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 NE2 GLN J 449 O ASP J 491 1.71 REMARK 500 OG SER G 236 NH2 ARG G 334 1.86 REMARK 500 O ASP J 540 N GLN J 544 1.94 REMARK 500 O ASP D 540 N GLN D 544 1.99 REMARK 500 O ILE J 445 NH2 ARG J 466 2.00 REMARK 500 O ILE D 445 NH2 ARG D 466 2.11 REMARK 500 OG SER A 297 OE1 GLU A 327 2.11 REMARK 500 NE2 GLN G 449 O ASP G 491 2.11 REMARK 500 OG SER A 360 OG1 THR A 413 2.11 REMARK 500 O MET J 440 NH1 ARG J 466 2.13 REMARK 500 NE2 GLN A 449 O ASP A 491 2.14 REMARK 500 OG SER G 236 OE1 GLU G 291 2.17 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 PHE E 27 OD1 ASN G 531 2546 1.96 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 LYS A 184 3.88 80.49 REMARK 500 CYS A 208 87.48 -69.63 REMARK 500 TYR A 210 -79.32 -109.22 REMARK 500 VAL A 222 -56.67 -123.61 REMARK 500 CYS A 230 58.26 -152.09 REMARK 500 ASP A 252 -147.97 -95.34 REMARK 500 VAL A 255 77.02 43.10 REMARK 500 GLU A 273 -72.79 62.21 REMARK 500 ASN A 274 -117.22 -114.24 REMARK 500 ASN A 316 -141.00 58.90 REMARK 500 ARG A 334 -29.17 85.66 REMARK 500 TYR A 375 98.66 -63.70 REMARK 500 ALA A 386 -133.97 -107.46 REMARK 500 THR A 455 107.86 -171.58 REMARK 500 GLU A 457 144.57 83.02 REMARK 500 VAL A 468 -65.41 69.07 REMARK 500 SER A 472 -90.52 -151.25 REMARK 500 ASN B 28 -122.37 47.76 REMARK 500 ILE B 29 154.44 77.78 REMARK 500 LYS B 43 -173.77 159.07 REMARK 500 ASP B 56 86.09 -68.83 REMARK 500 SER B 85 68.52 35.31 REMARK 500 SER B 123 176.48 78.52 REMARK 500 TRP B 162 -112.14 -96.83 REMARK 500 SER B 180 -127.92 54.74 REMARK 500 SER C 27 -160.56 -112.76 REMARK 500 TYR C 141 -63.60 -95.61 REMARK 500 LYS C 170 -69.76 -92.02 REMARK 500 LYS D 184 -14.04 85.30 REMARK 500 TYR D 210 -78.74 -109.07 REMARK 500 VAL D 222 -57.19 -124.00 REMARK 500 CYS D 230 57.14 -152.53 REMARK 500 ASP D 252 -147.97 -94.64 REMARK 500 VAL D 255 77.24 42.93 REMARK 500 ASN D 316 -141.13 58.82 REMARK 500 ARG D 334 -28.87 84.79 REMARK 500 ALA D 386 -130.87 -113.24 REMARK 500 SER D 416 -63.22 64.82 REMARK 500 THR D 455 100.31 -165.86 REMARK 500 GLU D 457 110.08 75.40 REMARK 500 VAL D 468 -65.54 68.78 REMARK 500 SER D 472 -104.21 -129.34 REMARK 500 GLN D 544 61.22 37.32 REMARK 500 PRO D 546 93.71 -52.80 REMARK 500 ASN E 28 -122.47 46.92 REMARK 500 ILE E 29 156.62 77.18 REMARK 500 LYS E 43 -174.88 160.54 REMARK 500 ASP E 56 87.07 -67.44 REMARK 500 SER E 85 68.35 35.18 REMARK 500 SER E 123 174.85 79.63 REMARK 500 REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS. 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 SER B 123 THR B 124 -143.13 REMARK 500 SER E 123 THR E 124 -143.24 REMARK 500 SER H 123 THR H 124 -144.20 REMARK 500 SER K 123 THR K 124 -143.31 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 D 542 0.23 SIDE_CHAIN REMARK 500 ARG F 18 0.09 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 8IVW A 25 595 UNP O60462 NRP2_HUMAN 25 595 DBREF 8IVW B 1 228 PDB 8IVW 8IVW 1 228 DBREF 8IVW C 1 215 PDB 8IVW 8IVW 1 215 DBREF 8IVW D 25 595 UNP O60462 NRP2_HUMAN 25 595 DBREF 8IVW E 1 228 PDB 8IVW 8IVW 1 228 DBREF 8IVW F 1 215 PDB 8IVW 8IVW 1 215 DBREF 8IVW G 25 595 UNP O60462 NRP2_HUMAN 25 595 DBREF 8IVW H 1 228 PDB 8IVW 8IVW 1 228 DBREF 8IVW I 1 215 PDB 8IVW 8IVW 1 215 DBREF 8IVW J 25 595 UNP O60462 NRP2_HUMAN 25 595 DBREF 8IVW K 1 228 PDB 8IVW 8IVW 1 228 DBREF 8IVW L 1 215 PDB 8IVW 8IVW 1 215 SEQADV 8IVW HIS A 13 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS A 14 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS A 15 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS A 16 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS A 17 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS A 18 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLU A 19 UNP O60462 EXPRESSION TAG SEQADV 8IVW ASN A 20 UNP O60462 EXPRESSION TAG SEQADV 8IVW LEU A 21 UNP O60462 EXPRESSION TAG SEQADV 8IVW TYR A 22 UNP O60462 EXPRESSION TAG SEQADV 8IVW PHE A 23 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLN A 24 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS D 13 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS D 14 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS D 15 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS D 16 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS D 17 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS D 18 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLU D 19 UNP O60462 EXPRESSION TAG SEQADV 8IVW ASN D 20 UNP O60462 EXPRESSION TAG SEQADV 8IVW LEU D 21 UNP O60462 EXPRESSION TAG SEQADV 8IVW TYR D 22 UNP O60462 EXPRESSION TAG SEQADV 8IVW PHE D 23 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLN D 24 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS G 13 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS G 14 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS G 15 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS G 16 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS G 17 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS G 18 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLU G 19 UNP O60462 EXPRESSION TAG SEQADV 8IVW ASN G 20 UNP O60462 EXPRESSION TAG SEQADV 8IVW LEU G 21 UNP O60462 EXPRESSION TAG SEQADV 8IVW TYR G 22 UNP O60462 EXPRESSION TAG SEQADV 8IVW PHE G 23 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLN G 24 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS J 13 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS J 14 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS J 15 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS J 16 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS J 17 UNP O60462 EXPRESSION TAG SEQADV 8IVW HIS J 18 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLU J 19 UNP O60462 EXPRESSION TAG SEQADV 8IVW ASN J 20 UNP O60462 EXPRESSION TAG SEQADV 8IVW LEU J 21 UNP O60462 EXPRESSION TAG SEQADV 8IVW TYR J 22 UNP O60462 EXPRESSION TAG SEQADV 8IVW PHE J 23 UNP O60462 EXPRESSION TAG SEQADV 8IVW GLN J 24 UNP O60462 EXPRESSION TAG SEQRES 1 A 583 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN ASP SEQRES 2 A 583 PRO PRO CYS GLY GLY ARG LEU ASN SER LYS ASP ALA GLY SEQRES 3 A 583 TYR ILE THR SER PRO GLY TYR PRO GLN ASP TYR PRO SER SEQRES 4 A 583 HIS GLN ASN CYS GLU TRP ILE VAL TYR ALA PRO GLU PRO SEQRES 5 A 583 ASN GLN LYS ILE VAL LEU ASN PHE ASN PRO HIS PHE GLU SEQRES 6 A 583 ILE GLU LYS HIS ASP CYS LYS TYR ASP PHE ILE GLU ILE SEQRES 7 A 583 ARG ASP GLY ASP SER GLU SER ALA ASP LEU LEU GLY LYS SEQRES 8 A 583 HIS CYS GLY ASN ILE ALA PRO PRO THR ILE ILE SER SER SEQRES 9 A 583 GLY SER MET LEU TYR ILE LYS PHE THR SER ASP TYR ALA SEQRES 10 A 583 ARG GLN GLY ALA GLY PHE SER LEU ARG TYR GLU ILE PHE SEQRES 11 A 583 LYS THR GLY SER GLU ASP CYS SER LYS ASN PHE THR SER SEQRES 12 A 583 PRO ASN GLY THR ILE GLU SER PRO GLY PHE PRO GLU LYS SEQRES 13 A 583 TYR PRO HIS ASN LEU ASP CYS THR PHE THR ILE LEU ALA SEQRES 14 A 583 LYS PRO LYS MET GLU ILE ILE LEU GLN PHE LEU ILE PHE SEQRES 15 A 583 ASP LEU GLU HIS ASP PRO LEU GLN VAL GLY GLU GLY ASP SEQRES 16 A 583 CYS LYS TYR ASP TRP LEU ASP ILE TRP ASP GLY ILE PRO SEQRES 17 A 583 HIS VAL GLY PRO LEU ILE GLY LYS TYR CYS GLY THR LYS SEQRES 18 A 583 THR PRO SER GLU LEU ARG SER SER THR GLY ILE LEU SER SEQRES 19 A 583 LEU THR PHE HIS THR ASP MET ALA VAL ALA LYS ASP GLY SEQRES 20 A 583 PHE SER ALA ARG TYR TYR LEU VAL HIS GLN GLU PRO LEU SEQRES 21 A 583 GLU ASN PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER SEQRES 22 A 583 GLY ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR SEQRES 23 A 583 TYR SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU SEQRES 24 A 583 HIS GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER SEQRES 25 A 583 ASN LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR SEQRES 26 A 583 MET LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG SEQRES 27 A 583 GLU THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU SEQRES 28 A 583 GLU VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG SEQRES 29 A 583 HIS GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP SEQRES 30 A 583 ALA THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU SEQRES 31 A 583 LEU THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SEQRES 32 A 583 SER GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG SEQRES 33 A 583 VAL THR ASP ALA PRO CYS SER ASN MET LEU GLY MET LEU SEQRES 34 A 583 SER GLY LEU ILE ALA ASP SER GLN ILE SER ALA SER SER SEQRES 35 A 583 THR GLN GLU TYR LEU TRP SER PRO SER ALA ALA ARG LEU SEQRES 36 A 583 VAL SER SER ARG SER GLY TRP PHE PRO ARG ILE PRO GLN SEQRES 37 A 583 ALA GLN PRO GLY GLU GLU TRP LEU GLN VAL ASP LEU GLY SEQRES 38 A 583 THR PRO LYS THR VAL LYS GLY VAL ILE ILE GLN GLY ALA SEQRES 39 A 583 ARG GLY GLY ASP SER ILE THR ALA VAL GLU ALA ARG ALA SEQRES 40 A 583 PHE VAL ARG LYS PHE LYS VAL SER TYR SER LEU ASN GLY SEQRES 41 A 583 LYS ASP TRP GLU TYR ILE GLN ASP PRO ARG THR GLN GLN SEQRES 42 A 583 PRO LYS LEU PHE GLU GLY ASN MET HIS TYR ASP THR PRO SEQRES 43 A 583 ASP ILE ARG ARG PHE ASP PRO ILE PRO ALA GLN TYR VAL SEQRES 44 A 583 ARG VAL TYR PRO GLU ARG TRP SER PRO ALA GLY ILE GLY SEQRES 45 A 583 MET ARG LEU GLU VAL LEU GLY CYS ASP TRP THR SEQRES 1 B 228 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 B 228 PRO GLY ALA THR VAL LYS ILE SER CYS LYS VAL SER GLY SEQRES 3 B 228 PHE ASN ILE LYS ASP TYR TYR ILE HIS TRP VAL GLN GLN SEQRES 4 B 228 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 B 228 VAL GLU ASP ASP GLU THR LYS TYR ALA PRO LYS PHE GLN SEQRES 6 B 228 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASP THR SEQRES 7 B 228 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 B 228 ALA VAL TYR TYR CYS ALA THR PRO ILE TYR GLY SER ARG SEQRES 9 B 228 GLU ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 B 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 B 228 PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR SEQRES 12 B 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 B 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 B 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 B 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 B 228 SER LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS SEQRES 17 B 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLY GLY SEQRES 18 B 228 SER HIS HIS HIS HIS HIS HIS SEQRES 1 C 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 C 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS THR ALA SER SEQRES 3 C 215 SER SER VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 C 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG THR SEQRES 5 C 215 SER ASN LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 C 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 C 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS HIS GLN SEQRES 8 C 215 TYR TYR ARG SER PRO PRO THR PHE GLY GLY GLY THR LYS SEQRES 9 C 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 C 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 C 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 C 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 C 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 C 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 C 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 C 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 C 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 583 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN ASP SEQRES 2 D 583 PRO PRO CYS GLY GLY ARG LEU ASN SER LYS ASP ALA GLY SEQRES 3 D 583 TYR ILE THR SER PRO GLY TYR PRO GLN ASP TYR PRO SER SEQRES 4 D 583 HIS GLN ASN CYS GLU TRP ILE VAL TYR ALA PRO GLU PRO SEQRES 5 D 583 ASN GLN LYS ILE VAL LEU ASN PHE ASN PRO HIS PHE GLU SEQRES 6 D 583 ILE GLU LYS HIS ASP CYS LYS TYR ASP PHE ILE GLU ILE SEQRES 7 D 583 ARG ASP GLY ASP SER GLU SER ALA ASP LEU LEU GLY LYS SEQRES 8 D 583 HIS CYS GLY ASN ILE ALA PRO PRO THR ILE ILE SER SER SEQRES 9 D 583 GLY SER MET LEU TYR ILE LYS PHE THR SER ASP TYR ALA SEQRES 10 D 583 ARG GLN GLY ALA GLY PHE SER LEU ARG TYR GLU ILE PHE SEQRES 11 D 583 LYS THR GLY SER GLU ASP CYS SER LYS ASN PHE THR SER SEQRES 12 D 583 PRO ASN GLY THR ILE GLU SER PRO GLY PHE PRO GLU LYS SEQRES 13 D 583 TYR PRO HIS ASN LEU ASP CYS THR PHE THR ILE LEU ALA SEQRES 14 D 583 LYS PRO LYS MET GLU ILE ILE LEU GLN PHE LEU ILE PHE SEQRES 15 D 583 ASP LEU GLU HIS ASP PRO LEU GLN VAL GLY GLU GLY ASP SEQRES 16 D 583 CYS LYS TYR ASP TRP LEU ASP ILE TRP ASP GLY ILE PRO SEQRES 17 D 583 HIS VAL GLY PRO LEU ILE GLY LYS TYR CYS GLY THR LYS SEQRES 18 D 583 THR PRO SER GLU LEU ARG SER SER THR GLY ILE LEU SER SEQRES 19 D 583 LEU THR PHE HIS THR ASP MET ALA VAL ALA LYS ASP GLY SEQRES 20 D 583 PHE SER ALA ARG TYR TYR LEU VAL HIS GLN GLU PRO LEU SEQRES 21 D 583 GLU ASN PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER SEQRES 22 D 583 GLY ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR SEQRES 23 D 583 TYR SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU SEQRES 24 D 583 HIS GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER SEQRES 25 D 583 ASN LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR SEQRES 26 D 583 MET LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG SEQRES 27 D 583 GLU THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU SEQRES 28 D 583 GLU VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG SEQRES 29 D 583 HIS GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP SEQRES 30 D 583 ALA THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU SEQRES 31 D 583 LEU THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SEQRES 32 D 583 SER GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG SEQRES 33 D 583 VAL THR ASP ALA PRO CYS SER ASN MET LEU GLY MET LEU SEQRES 34 D 583 SER GLY LEU ILE ALA ASP SER GLN ILE SER ALA SER SER SEQRES 35 D 583 THR GLN GLU TYR LEU TRP SER PRO SER ALA ALA ARG LEU SEQRES 36 D 583 VAL SER SER ARG SER GLY TRP PHE PRO ARG ILE PRO GLN SEQRES 37 D 583 ALA GLN PRO GLY GLU GLU TRP LEU GLN VAL ASP LEU GLY SEQRES 38 D 583 THR PRO LYS THR VAL LYS GLY VAL ILE ILE GLN GLY ALA SEQRES 39 D 583 ARG GLY GLY ASP SER ILE THR ALA VAL GLU ALA ARG ALA SEQRES 40 D 583 PHE VAL ARG LYS PHE LYS VAL SER TYR SER LEU ASN GLY SEQRES 41 D 583 LYS ASP TRP GLU TYR ILE GLN ASP PRO ARG THR GLN GLN SEQRES 42 D 583 PRO LYS LEU PHE GLU GLY ASN MET HIS TYR ASP THR PRO SEQRES 43 D 583 ASP ILE ARG ARG PHE ASP PRO ILE PRO ALA GLN TYR VAL SEQRES 44 D 583 ARG VAL TYR PRO GLU ARG TRP SER PRO ALA GLY ILE GLY SEQRES 45 D 583 MET ARG LEU GLU VAL LEU GLY CYS ASP TRP THR SEQRES 1 E 228 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 E 228 PRO GLY ALA THR VAL LYS ILE SER CYS LYS VAL SER GLY SEQRES 3 E 228 PHE ASN ILE LYS ASP TYR TYR ILE HIS TRP VAL GLN GLN SEQRES 4 E 228 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 E 228 VAL GLU ASP ASP GLU THR LYS TYR ALA PRO LYS PHE GLN SEQRES 6 E 228 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASP THR SEQRES 7 E 228 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 E 228 ALA VAL TYR TYR CYS ALA THR PRO ILE TYR GLY SER ARG SEQRES 9 E 228 GLU ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 E 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 E 228 PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR SEQRES 12 E 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 E 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 E 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 E 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 E 228 SER LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS SEQRES 17 E 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLY GLY SEQRES 18 E 228 SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 F 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS THR ALA SER SEQRES 3 F 215 SER SER VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 F 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG THR SEQRES 5 F 215 SER ASN LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 F 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 F 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS HIS GLN SEQRES 8 F 215 TYR TYR ARG SER PRO PRO THR PHE GLY GLY GLY THR LYS SEQRES 9 F 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 F 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 F 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 F 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 F 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 F 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 F 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 F 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 F 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 583 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN ASP SEQRES 2 G 583 PRO PRO CYS GLY GLY ARG LEU ASN SER LYS ASP ALA GLY SEQRES 3 G 583 TYR ILE THR SER PRO GLY TYR PRO GLN ASP TYR PRO SER SEQRES 4 G 583 HIS GLN ASN CYS GLU TRP ILE VAL TYR ALA PRO GLU PRO SEQRES 5 G 583 ASN GLN LYS ILE VAL LEU ASN PHE ASN PRO HIS PHE GLU SEQRES 6 G 583 ILE GLU LYS HIS ASP CYS LYS TYR ASP PHE ILE GLU ILE SEQRES 7 G 583 ARG ASP GLY ASP SER GLU SER ALA ASP LEU LEU GLY LYS SEQRES 8 G 583 HIS CYS GLY ASN ILE ALA PRO PRO THR ILE ILE SER SER SEQRES 9 G 583 GLY SER MET LEU TYR ILE LYS PHE THR SER ASP TYR ALA SEQRES 10 G 583 ARG GLN GLY ALA GLY PHE SER LEU ARG TYR GLU ILE PHE SEQRES 11 G 583 LYS THR GLY SER GLU ASP CYS SER LYS ASN PHE THR SER SEQRES 12 G 583 PRO ASN GLY THR ILE GLU SER PRO GLY PHE PRO GLU LYS SEQRES 13 G 583 TYR PRO HIS ASN LEU ASP CYS THR PHE THR ILE LEU ALA SEQRES 14 G 583 LYS PRO LYS MET GLU ILE ILE LEU GLN PHE LEU ILE PHE SEQRES 15 G 583 ASP LEU GLU HIS ASP PRO LEU GLN VAL GLY GLU GLY ASP SEQRES 16 G 583 CYS LYS TYR ASP TRP LEU ASP ILE TRP ASP GLY ILE PRO SEQRES 17 G 583 HIS VAL GLY PRO LEU ILE GLY LYS TYR CYS GLY THR LYS SEQRES 18 G 583 THR PRO SER GLU LEU ARG SER SER THR GLY ILE LEU SER SEQRES 19 G 583 LEU THR PHE HIS THR ASP MET ALA VAL ALA LYS ASP GLY SEQRES 20 G 583 PHE SER ALA ARG TYR TYR LEU VAL HIS GLN GLU PRO LEU SEQRES 21 G 583 GLU ASN PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER SEQRES 22 G 583 GLY ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR SEQRES 23 G 583 TYR SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU SEQRES 24 G 583 HIS GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER SEQRES 25 G 583 ASN LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR SEQRES 26 G 583 MET LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG SEQRES 27 G 583 GLU THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU SEQRES 28 G 583 GLU VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG SEQRES 29 G 583 HIS GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP SEQRES 30 G 583 ALA THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU SEQRES 31 G 583 LEU THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SEQRES 32 G 583 SER GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG SEQRES 33 G 583 VAL THR ASP ALA PRO CYS SER ASN MET LEU GLY MET LEU SEQRES 34 G 583 SER GLY LEU ILE ALA ASP SER GLN ILE SER ALA SER SER SEQRES 35 G 583 THR GLN GLU TYR LEU TRP SER PRO SER ALA ALA ARG LEU SEQRES 36 G 583 VAL SER SER ARG SER GLY TRP PHE PRO ARG ILE PRO GLN SEQRES 37 G 583 ALA GLN PRO GLY GLU GLU TRP LEU GLN VAL ASP LEU GLY SEQRES 38 G 583 THR PRO LYS THR VAL LYS GLY VAL ILE ILE GLN GLY ALA SEQRES 39 G 583 ARG GLY GLY ASP SER ILE THR ALA VAL GLU ALA ARG ALA SEQRES 40 G 583 PHE VAL ARG LYS PHE LYS VAL SER TYR SER LEU ASN GLY SEQRES 41 G 583 LYS ASP TRP GLU TYR ILE GLN ASP PRO ARG THR GLN GLN SEQRES 42 G 583 PRO LYS LEU PHE GLU GLY ASN MET HIS TYR ASP THR PRO SEQRES 43 G 583 ASP ILE ARG ARG PHE ASP PRO ILE PRO ALA GLN TYR VAL SEQRES 44 G 583 ARG VAL TYR PRO GLU ARG TRP SER PRO ALA GLY ILE GLY SEQRES 45 G 583 MET ARG LEU GLU VAL LEU GLY CYS ASP TRP THR SEQRES 1 H 228 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 228 PRO GLY ALA THR VAL LYS ILE SER CYS LYS VAL SER GLY SEQRES 3 H 228 PHE ASN ILE LYS ASP TYR TYR ILE HIS TRP VAL GLN GLN SEQRES 4 H 228 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 H 228 VAL GLU ASP ASP GLU THR LYS TYR ALA PRO LYS PHE GLN SEQRES 6 H 228 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASP THR SEQRES 7 H 228 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 228 ALA VAL TYR TYR CYS ALA THR PRO ILE TYR GLY SER ARG SEQRES 9 H 228 GLU ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 228 PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR SEQRES 12 H 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 228 SER LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS SEQRES 17 H 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLY GLY SEQRES 18 H 228 SER HIS HIS HIS HIS HIS HIS SEQRES 1 I 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 I 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS THR ALA SER SEQRES 3 I 215 SER SER VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 I 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG THR SEQRES 5 I 215 SER ASN LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 I 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 I 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS HIS GLN SEQRES 8 I 215 TYR TYR ARG SER PRO PRO THR PHE GLY GLY GLY THR LYS SEQRES 9 I 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 I 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 I 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 I 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 I 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 I 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 I 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 I 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 I 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 J 583 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN ASP SEQRES 2 J 583 PRO PRO CYS GLY GLY ARG LEU ASN SER LYS ASP ALA GLY SEQRES 3 J 583 TYR ILE THR SER PRO GLY TYR PRO GLN ASP TYR PRO SER SEQRES 4 J 583 HIS GLN ASN CYS GLU TRP ILE VAL TYR ALA PRO GLU PRO SEQRES 5 J 583 ASN GLN LYS ILE VAL LEU ASN PHE ASN PRO HIS PHE GLU SEQRES 6 J 583 ILE GLU LYS HIS ASP CYS LYS TYR ASP PHE ILE GLU ILE SEQRES 7 J 583 ARG ASP GLY ASP SER GLU SER ALA ASP LEU LEU GLY LYS SEQRES 8 J 583 HIS CYS GLY ASN ILE ALA PRO PRO THR ILE ILE SER SER SEQRES 9 J 583 GLY SER MET LEU TYR ILE LYS PHE THR SER ASP TYR ALA SEQRES 10 J 583 ARG GLN GLY ALA GLY PHE SER LEU ARG TYR GLU ILE PHE SEQRES 11 J 583 LYS THR GLY SER GLU ASP CYS SER LYS ASN PHE THR SER SEQRES 12 J 583 PRO ASN GLY THR ILE GLU SER PRO GLY PHE PRO GLU LYS SEQRES 13 J 583 TYR PRO HIS ASN LEU ASP CYS THR PHE THR ILE LEU ALA SEQRES 14 J 583 LYS PRO LYS MET GLU ILE ILE LEU GLN PHE LEU ILE PHE SEQRES 15 J 583 ASP LEU GLU HIS ASP PRO LEU GLN VAL GLY GLU GLY ASP SEQRES 16 J 583 CYS LYS TYR ASP TRP LEU ASP ILE TRP ASP GLY ILE PRO SEQRES 17 J 583 HIS VAL GLY PRO LEU ILE GLY LYS TYR CYS GLY THR LYS SEQRES 18 J 583 THR PRO SER GLU LEU ARG SER SER THR GLY ILE LEU SER SEQRES 19 J 583 LEU THR PHE HIS THR ASP MET ALA VAL ALA LYS ASP GLY SEQRES 20 J 583 PHE SER ALA ARG TYR TYR LEU VAL HIS GLN GLU PRO LEU SEQRES 21 J 583 GLU ASN PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER SEQRES 22 J 583 GLY ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR SEQRES 23 J 583 TYR SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU SEQRES 24 J 583 HIS GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER SEQRES 25 J 583 ASN LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR SEQRES 26 J 583 MET LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG SEQRES 27 J 583 GLU THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU SEQRES 28 J 583 GLU VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG SEQRES 29 J 583 HIS GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP SEQRES 30 J 583 ALA THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU SEQRES 31 J 583 LEU THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SEQRES 32 J 583 SER GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG SEQRES 33 J 583 VAL THR ASP ALA PRO CYS SER ASN MET LEU GLY MET LEU SEQRES 34 J 583 SER GLY LEU ILE ALA ASP SER GLN ILE SER ALA SER SER SEQRES 35 J 583 THR GLN GLU TYR LEU TRP SER PRO SER ALA ALA ARG LEU SEQRES 36 J 583 VAL SER SER ARG SER GLY TRP PHE PRO ARG ILE PRO GLN SEQRES 37 J 583 ALA GLN PRO GLY GLU GLU TRP LEU GLN VAL ASP LEU GLY SEQRES 38 J 583 THR PRO LYS THR VAL LYS GLY VAL ILE ILE GLN GLY ALA SEQRES 39 J 583 ARG GLY GLY ASP SER ILE THR ALA VAL GLU ALA ARG ALA SEQRES 40 J 583 PHE VAL ARG LYS PHE LYS VAL SER TYR SER LEU ASN GLY SEQRES 41 J 583 LYS ASP TRP GLU TYR ILE GLN ASP PRO ARG THR GLN GLN SEQRES 42 J 583 PRO LYS LEU PHE GLU GLY ASN MET HIS TYR ASP THR PRO SEQRES 43 J 583 ASP ILE ARG ARG PHE ASP PRO ILE PRO ALA GLN TYR VAL SEQRES 44 J 583 ARG VAL TYR PRO GLU ARG TRP SER PRO ALA GLY ILE GLY SEQRES 45 J 583 MET ARG LEU GLU VAL LEU GLY CYS ASP TRP THR SEQRES 1 K 228 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 K 228 PRO GLY ALA THR VAL LYS ILE SER CYS LYS VAL SER GLY SEQRES 3 K 228 PHE ASN ILE LYS ASP TYR TYR ILE HIS TRP VAL GLN GLN SEQRES 4 K 228 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 K 228 VAL GLU ASP ASP GLU THR LYS TYR ALA PRO LYS PHE GLN SEQRES 6 K 228 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASP THR SEQRES 7 K 228 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 K 228 ALA VAL TYR TYR CYS ALA THR PRO ILE TYR GLY SER ARG SEQRES 9 K 228 GLU ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 K 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 K 228 PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR SEQRES 12 K 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 K 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 K 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 K 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 K 228 SER LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS SEQRES 17 K 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLY GLY SEQRES 18 K 228 SER HIS HIS HIS HIS HIS HIS SEQRES 1 L 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS THR ALA SER SEQRES 3 L 215 SER SER VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG THR SEQRES 5 L 215 SER ASN LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS HIS GLN SEQRES 8 L 215 TYR TYR ARG SER PRO PRO THR PHE GLY GLY GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HELIX 1 AA1 ALA A 289 GLU A 291 5 3 HELIX 2 AA2 THR A 305 SER A 309 5 5 HELIX 3 AA3 ARG A 428 ALA A 432 5 5 HELIX 4 AA4 ALA A 446 SER A 448 5 3 HELIX 5 AA5 SER A 461 ALA A 465 5 5 HELIX 6 AA6 PRO B 62 GLN B 65 5 4 HELIX 7 AA7 ARG B 87 THR B 91 5 5 HELIX 8 AA8 SER B 195 LYS B 200 1 6 HELIX 9 AA9 LYS B 209 ASN B 212 5 4 HELIX 10 AB1 SER C 30 SER C 32 5 3 HELIX 11 AB2 GLN C 80 PHE C 84 5 5 HELIX 12 AB3 SER C 122 GLY C 129 1 8 HELIX 13 AB4 LYS C 184 HIS C 190 1 7 HELIX 14 AB5 ALA D 289 GLU D 291 5 3 HELIX 15 AB6 THR D 305 SER D 309 5 5 HELIX 16 AB7 ARG D 428 ALA D 432 5 5 HELIX 17 AB8 SER D 461 ARG D 466 5 6 HELIX 18 AB9 PRO E 62 GLN E 65 5 4 HELIX 19 AC1 ARG E 87 THR E 91 5 5 HELIX 20 AC2 SER E 194 LYS E 200 1 7 HELIX 21 AC3 LYS E 209 ASN E 212 5 4 HELIX 22 AC4 SER F 30 SER F 32 5 3 HELIX 23 AC5 GLN F 80 PHE F 84 5 5 HELIX 24 AC6 SER F 122 GLY F 129 1 8 HELIX 25 AC7 LYS F 184 HIS F 190 1 7 HELIX 26 AC8 ALA G 289 GLU G 291 5 3 HELIX 27 AC9 THR G 305 SER G 309 5 5 HELIX 28 AD1 ARG G 428 ALA G 432 5 5 HELIX 29 AD2 ALA G 446 ILE G 450 5 5 HELIX 30 AD3 PRO H 62 GLN H 65 5 4 HELIX 31 AD4 ARG H 87 THR H 91 5 5 HELIX 32 AD5 SER H 194 LYS H 200 1 7 HELIX 33 AD6 LYS H 209 ASN H 212 5 4 HELIX 34 AD7 SER I 30 SER I 32 5 3 HELIX 35 AD8 GLN I 80 PHE I 84 5 5 HELIX 36 AD9 SER I 122 GLY I 129 1 8 HELIX 37 AE1 LYS I 184 HIS I 190 1 7 HELIX 38 AE2 ALA J 289 GLU J 291 5 3 HELIX 39 AE3 THR J 305 SER J 309 5 5 HELIX 40 AE4 ARG J 428 ALA J 432 5 5 HELIX 41 AE5 SER J 461 ALA J 465 5 5 HELIX 42 AE6 PRO K 62 GLN K 65 5 4 HELIX 43 AE7 ARG K 87 THR K 91 5 5 HELIX 44 AE8 SER K 194 LYS K 200 1 7 HELIX 45 AE9 LYS K 209 ASN K 212 5 4 HELIX 46 AF1 SER L 30 SER L 32 5 3 HELIX 47 AF2 GLN L 80 PHE L 84 5 5 HELIX 48 AF3 SER L 122 GLY L 129 1 8 HELIX 49 AF4 LYS L 184 HIS L 190 1 7 SHEET 1 AA1 5 LYS A 151 PHE A 153 0 SHEET 2 AA1 5 ASP A 174 LEU A 180 1 O LEU A 180 N PHE A 153 SHEET 3 AA1 5 ILE A 244 HIS A 250 -1 O LEU A 247 N PHE A 177 SHEET 4 AA1 5 TRP A 212 TRP A 216 -1 N TRP A 216 O SER A 246 SHEET 5 AA1 5 LEU A 225 TYR A 229 -1 O ILE A 226 N ILE A 215 SHEET 1 AA2 4 ASN A 157 GLU A 161 0 SHEET 2 AA2 4 GLY A 259 HIS A 268 -1 O ALA A 262 N ILE A 160 SHEET 3 AA2 4 MET A 185 ASP A 195 -1 N GLU A 186 O VAL A 267 SHEET 4 AA2 4 LEU A 238 SER A 240 -1 O SER A 240 N ILE A 187 SHEET 1 AA3 9 VAL A 279 PRO A 280 0 SHEET 2 AA3 9 ILE A 293 ALA A 295 0 SHEET 3 AA3 9 LEU A 329 GLN A 345 -1 O GLN A 330 N SER A 294 SHEET 4 AA3 9 ALA A 347 ILE A 348 0 SHEET 5 AA3 9 GLY A 355 SER A 366 -1 O TYR A 356 N ALA A 347 SHEET 6 AA3 9 MET A 373 VAL A 374 -1 O MET A 373 N VAL A 365 SHEET 7 AA3 9 PHE A 384 GLN A 385 -1 O PHE A 384 N TYR A 361 SHEET 8 AA3 9 VAL A 394 HIS A 415 -1 O PHE A 406 N SER A 366 SHEET 9 AA3 9 ARG A 421 CYS A 427 -1 O GLU A 423 N ALA A 343 SHEET 1 AA4 4 ASN A 436 MET A 437 0 SHEET 2 AA4 4 ARG A 586 CYS A 592 -1 O GLY A 591 N ASN A 436 SHEET 3 AA4 4 THR A 497 GLN A 504 -1 N GLY A 500 O LEU A 590 SHEET 4 AA4 4 ASP A 559 PRO A 567 -1 O ARG A 561 N VAL A 501 SHEET 1 AA5 6 ILE A 450 ALA A 452 0 SHEET 2 AA5 6 LEU A 488 ASP A 491 -1 O GLN A 489 N SER A 451 SHEET 3 AA5 6 VAL A 521 SER A 529 0 SHEET 4 AA5 6 GLU A 536 TYR A 537 -1 O GLU A 536 N TYR A 528 SHEET 5 AA5 6 PHE A 549 GLU A 550 -1 O PHE A 549 N PHE A 524 SHEET 6 AA5 6 TYR A 570 TRP A 578 -1 O GLU A 576 N LYS A 523 SHEET 1 AA6 4 GLN B 3 GLN B 6 0 SHEET 2 AA6 4 VAL B 18 SER B 25 -1 O LYS B 23 N VAL B 5 SHEET 3 AA6 4 THR B 78 LEU B 83 -1 O LEU B 83 N VAL B 18 SHEET 4 AA6 4 VAL B 68 ASP B 73 -1 N THR B 71 O TYR B 80 SHEET 1 AA7 7 GLU B 10 LYS B 12 0 SHEET 2 AA7 7 TYR B 33 GLN B 39 0 SHEET 3 AA7 7 GLU B 46 ASP B 52 -1 O GLU B 46 N GLN B 38 SHEET 4 AA7 7 LYS B 59 TYR B 60 -1 O LYS B 59 N ARG B 50 SHEET 5 AA7 7 ALA B 92 THR B 98 -1 O VAL B 93 N GLN B 39 SHEET 6 AA7 7 TYR B 110 TRP B 111 -1 O TYR B 110 N THR B 98 SHEET 7 AA7 7 THR B 115 VAL B 119 -1 O THR B 115 N TYR B 94 SHEET 1 AA8 5 SER B 128 LEU B 132 0 SHEET 2 AA8 5 THR B 143 TYR B 153 -1 O LEU B 149 N PHE B 130 SHEET 3 AA8 5 VAL B 171 THR B 173 0 SHEET 4 AA8 5 VAL B 177 GLN B 179 0 SHEET 5 AA8 5 LEU B 183 PRO B 193 -1 O LEU B 183 N GLN B 179 SHEET 1 AA9 3 THR B 159 SER B 161 0 SHEET 2 AA9 3 THR B 203 HIS B 208 -1 O ASP B 207 N THR B 159 SHEET 3 AA9 3 THR B 213 ARG B 218 -1 O VAL B 215 N VAL B 206 SHEET 1 AB1 3 MET C 4 THR C 5 0 SHEET 2 AB1 3 VAL C 19 VAL C 29 -1 O THR C 24 N THR C 5 SHEET 3 AB1 3 PHE C 63 ILE C 76 -1 O LEU C 74 N ILE C 21 SHEET 1 AB212 PRO C 8 SER C 14 0 SHEET 2 AB212 LEU C 34 GLN C 39 0 SHEET 3 AB212 LYS C 46 ILE C 49 -1 O ILE C 49 N TRP C 36 SHEET 4 AB212 THR C 86 GLN C 91 -1 O THR C 86 N GLN C 39 SHEET 5 AB212 THR C 98 PHE C 99 -1 O THR C 98 N GLN C 91 SHEET 6 AB212 THR C 103 LYS C 108 -1 O THR C 103 N TYR C 87 SHEET 7 AB212 PRO L 8 SER L 14 -1 O SER L 12 N SER C 9 SHEET 8 AB212 LEU L 34 GLN L 39 0 SHEET 9 AB212 LYS L 46 ILE L 49 -1 O ILE L 49 N TRP L 36 SHEET 10 AB212 THR L 86 GLN L 91 -1 O THR L 86 N GLN L 39 SHEET 11 AB212 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 12 AB212 THR L 103 LYS L 108 -1 O THR L 103 N TYR L 87 SHEET 1 AB3 4 VAL C 116 PHE C 119 0 SHEET 2 AB3 4 THR C 130 PHE C 140 -1 O VAL C 134 N PHE C 119 SHEET 3 AB3 4 TYR C 174 SER C 183 -1 O LEU C 182 N ALA C 131 SHEET 4 AB3 4 SER C 160 VAL C 164 -1 N SER C 163 O SER C 177 SHEET 1 AB4 4 ALA C 154 LEU C 155 0 SHEET 2 AB4 4 LYS C 146 VAL C 151 -1 N VAL C 151 O ALA C 154 SHEET 3 AB4 4 VAL C 192 THR C 198 -1 O ALA C 194 N LYS C 150 SHEET 4 AB4 4 VAL C 206 ASN C 211 -1 O PHE C 210 N TYR C 193 SHEET 1 AB5 5 LYS D 151 PHE D 153 0 SHEET 2 AB5 5 ASP D 174 LEU D 180 1 O LEU D 180 N PHE D 153 SHEET 3 AB5 5 ILE D 244 HIS D 250 -1 O LEU D 247 N PHE D 177 SHEET 4 AB5 5 TRP D 212 TRP D 216 -1 N TRP D 216 O SER D 246 SHEET 5 AB5 5 LEU D 225 TYR D 229 -1 O ILE D 226 N ILE D 215 SHEET 1 AB6 4 ASN D 157 GLU D 161 0 SHEET 2 AB6 4 GLY D 259 TYR D 265 -1 O ALA D 262 N ILE D 160 SHEET 3 AB6 4 ILE D 187 ASP D 195 -1 N ASP D 195 O GLY D 259 SHEET 4 AB6 4 LEU D 238 SER D 240 -1 O SER D 240 N ILE D 187 SHEET 1 AB7 9 VAL D 279 PRO D 280 0 SHEET 2 AB7 9 ILE D 293 ALA D 295 0 SHEET 3 AB7 9 LEU D 329 GLN D 345 -1 O GLN D 330 N SER D 294 SHEET 4 AB7 9 ALA D 347 ILE D 348 0 SHEET 5 AB7 9 GLY D 355 SER D 366 -1 O TYR D 356 N ALA D 347 SHEET 6 AB7 9 MET D 373 VAL D 374 -1 O MET D 373 N VAL D 365 SHEET 7 AB7 9 PHE D 384 GLN D 385 -1 O PHE D 384 N TYR D 361 SHEET 8 AB7 9 VAL D 394 HIS D 415 -1 O PHE D 406 N SER D 366 SHEET 9 AB7 9 ARG D 421 CYS D 427 -1 O GLU D 423 N ALA D 343 SHEET 1 AB8 2 ARG D 376 HIS D 377 0 SHEET 2 AB8 2 ASN D 380 HIS D 381 -1 O ASN D 380 N HIS D 377 SHEET 1 AB9 8 ASN D 436 MET D 437 0 SHEET 2 AB9 8 ILE D 450 ALA D 452 0 SHEET 3 AB9 8 LEU D 488 GLN D 504 -1 O GLN D 489 N SER D 451 SHEET 4 AB9 8 VAL D 521 SER D 529 0 SHEET 5 AB9 8 GLU D 536 TYR D 537 -1 O GLU D 536 N TYR D 528 SHEET 6 AB9 8 PHE D 549 GLU D 550 -1 O PHE D 549 N PHE D 524 SHEET 7 AB9 8 ASP D 559 TRP D 578 -1 O GLU D 576 N LYS D 523 SHEET 8 AB9 8 ARG D 586 CYS D 592 -1 O LEU D 590 N GLY D 500 SHEET 1 AC1 4 GLN E 3 GLN E 6 0 SHEET 2 AC1 4 VAL E 18 SER E 25 -1 O LYS E 23 N VAL E 5 SHEET 3 AC1 4 THR E 78 LEU E 83 -1 O LEU E 83 N VAL E 18 SHEET 4 AC1 4 VAL E 68 ASP E 73 -1 N THR E 71 O TYR E 80 SHEET 1 AC2 7 GLU E 10 LYS E 12 0 SHEET 2 AC2 7 TYR E 33 GLN E 39 0 SHEET 3 AC2 7 GLU E 46 ASP E 52 -1 O GLU E 46 N GLN E 38 SHEET 4 AC2 7 LYS E 59 TYR E 60 -1 O LYS E 59 N ARG E 50 SHEET 5 AC2 7 ALA E 92 THR E 98 -1 O VAL E 93 N GLN E 39 SHEET 6 AC2 7 TYR E 110 TRP E 111 -1 O TYR E 110 N THR E 98 SHEET 7 AC2 7 THR E 115 VAL E 119 -1 O THR E 115 N TYR E 94 SHEET 1 AC3 5 SER E 128 LEU E 132 0 SHEET 2 AC3 5 THR E 143 TYR E 153 -1 O LYS E 151 N SER E 128 SHEET 3 AC3 5 VAL E 171 THR E 173 0 SHEET 4 AC3 5 VAL E 177 GLN E 179 0 SHEET 5 AC3 5 LEU E 183 PRO E 193 -1 O LEU E 183 N GLN E 179 SHEET 1 AC4 3 THR E 159 SER E 161 0 SHEET 2 AC4 3 THR E 203 HIS E 208 -1 O ASP E 207 N THR E 159 SHEET 3 AC4 3 THR E 213 ARG E 218 -1 O VAL E 215 N VAL E 206 SHEET 1 AC5 3 MET F 4 THR F 5 0 SHEET 2 AC5 3 VAL F 19 VAL F 29 -1 O THR F 24 N THR F 5 SHEET 3 AC5 3 PHE F 63 ILE F 76 -1 O LEU F 74 N ILE F 21 SHEET 1 AC612 PRO F 8 SER F 14 0 SHEET 2 AC612 LEU F 34 GLN F 39 0 SHEET 3 AC612 LYS F 46 ILE F 49 -1 O ILE F 49 N TRP F 36 SHEET 4 AC612 THR F 86 GLN F 91 -1 O THR F 86 N GLN F 39 SHEET 5 AC612 THR F 98 PHE F 99 -1 O THR F 98 N GLN F 91 SHEET 6 AC612 THR F 103 LYS F 108 -1 O THR F 103 N TYR F 87 SHEET 7 AC612 PRO I 8 SER I 14 -1 O SER I 12 N SER F 9 SHEET 8 AC612 LEU I 34 GLN I 39 0 SHEET 9 AC612 LYS I 46 ILE I 49 -1 O ILE I 49 N TRP I 36 SHEET 10 AC612 THR I 86 GLN I 91 -1 O THR I 86 N GLN I 39 SHEET 11 AC612 THR I 98 PHE I 99 -1 O THR I 98 N GLN I 91 SHEET 12 AC612 THR I 103 LYS I 108 -1 O THR I 103 N TYR I 87 SHEET 1 AC7 4 VAL F 116 PHE F 119 0 SHEET 2 AC7 4 THR F 130 PHE F 140 -1 O VAL F 134 N PHE F 119 SHEET 3 AC7 4 TYR F 174 SER F 183 -1 O LEU F 182 N ALA F 131 SHEET 4 AC7 4 SER F 160 VAL F 164 -1 N SER F 163 O SER F 177 SHEET 1 AC8 4 ALA F 154 LEU F 155 0 SHEET 2 AC8 4 LYS F 146 VAL F 151 -1 N VAL F 151 O ALA F 154 SHEET 3 AC8 4 VAL F 192 THR F 198 -1 O ALA F 194 N LYS F 150 SHEET 4 AC8 4 VAL F 206 ASN F 211 -1 O PHE F 210 N TYR F 193 SHEET 1 AC9 5 LYS G 151 ASN G 152 0 SHEET 2 AC9 5 ASP G 174 ILE G 179 1 O THR G 178 N LYS G 151 SHEET 3 AC9 5 LEU G 245 HIS G 250 -1 O LEU G 247 N PHE G 177 SHEET 4 AC9 5 TRP G 212 TRP G 216 -1 N TRP G 216 O SER G 246 SHEET 5 AC9 5 LEU G 225 TYR G 229 -1 O ILE G 226 N ILE G 215 SHEET 1 AD1 3 ASN G 157 GLU G 161 0 SHEET 2 AD1 3 GLY G 259 TYR G 265 -1 O ALA G 262 N ILE G 160 SHEET 3 AD1 3 GLN G 190 ASP G 195 -1 N ASP G 195 O GLY G 259 SHEET 1 AD2 9 VAL G 279 PRO G 280 0 SHEET 2 AD2 9 ILE G 293 ALA G 295 0 SHEET 3 AD2 9 LEU G 329 GLN G 345 -1 O GLN G 330 N SER G 294 SHEET 4 AD2 9 ALA G 347 ILE G 348 0 SHEET 5 AD2 9 GLY G 355 SER G 366 -1 O TYR G 356 N ALA G 347 SHEET 6 AD2 9 MET G 373 VAL G 374 -1 O MET G 373 N VAL G 365 SHEET 7 AD2 9 PHE G 384 GLN G 385 -1 O PHE G 384 N TYR G 361 SHEET 8 AD2 9 VAL G 394 HIS G 415 -1 O GLN G 412 N SER G 360 SHEET 9 AD2 9 ARG G 421 CYS G 427 -1 O CYS G 427 N MET G 338 SHEET 1 AD3 2 ARG G 376 HIS G 377 0 SHEET 2 AD3 2 ASN G 380 HIS G 381 -1 O ASN G 380 N HIS G 377 SHEET 1 AD4 4 ASN G 436 MET G 437 0 SHEET 2 AD4 4 ARG G 586 GLY G 591 -1 O GLY G 591 N ASN G 436 SHEET 3 AD4 4 VAL G 498 GLN G 504 -1 N GLY G 500 O LEU G 590 SHEET 4 AD4 4 ASP G 559 ILE G 566 -1 O ILE G 566 N VAL G 498 SHEET 1 AD5 6 SER G 451 ALA G 452 0 SHEET 2 AD5 6 LEU G 488 ASP G 491 -1 O GLN G 489 N SER G 451 SHEET 3 AD5 6 VAL G 521 SER G 529 0 SHEET 4 AD5 6 TRP G 535 TYR G 537 -1 O GLU G 536 N TYR G 528 SHEET 5 AD5 6 PHE G 549 GLU G 550 -1 O PHE G 549 N PHE G 524 SHEET 6 AD5 6 TYR G 570 TRP G 578 -1 O GLU G 576 N LYS G 523 SHEET 1 AD6 4 GLN H 3 GLN H 6 0 SHEET 2 AD6 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AD6 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AD6 4 VAL H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AD7 7 GLU H 10 LYS H 12 0 SHEET 2 AD7 7 TYR H 33 GLN H 39 0 SHEET 3 AD7 7 GLU H 46 ASP H 52 -1 O GLU H 46 N GLN H 38 SHEET 4 AD7 7 LYS H 59 TYR H 60 -1 O LYS H 59 N ARG H 50 SHEET 5 AD7 7 ALA H 92 THR H 98 -1 O VAL H 93 N GLN H 39 SHEET 6 AD7 7 TYR H 110 TRP H 111 -1 O TYR H 110 N THR H 98 SHEET 7 AD7 7 THR H 115 VAL H 119 -1 O THR H 115 N TYR H 94 SHEET 1 AD8 5 SER H 128 LEU H 132 0 SHEET 2 AD8 5 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AD8 5 VAL H 171 THR H 173 0 SHEET 4 AD8 5 VAL H 177 GLN H 179 0 SHEET 5 AD8 5 LEU H 183 PRO H 193 -1 O LEU H 183 N GLN H 179 SHEET 1 AD9 3 THR H 159 SER H 161 0 SHEET 2 AD9 3 THR H 203 HIS H 208 -1 O ASP H 207 N THR H 159 SHEET 3 AD9 3 THR H 213 ARG H 218 -1 O VAL H 215 N VAL H 206 SHEET 1 AE1 3 MET I 4 THR I 5 0 SHEET 2 AE1 3 VAL I 19 VAL I 29 -1 O THR I 24 N THR I 5 SHEET 3 AE1 3 PHE I 63 ILE I 76 -1 O LEU I 74 N ILE I 21 SHEET 1 AE2 4 VAL I 116 PHE I 119 0 SHEET 2 AE2 4 THR I 130 PHE I 140 -1 O VAL I 134 N PHE I 119 SHEET 3 AE2 4 TYR I 174 SER I 183 -1 O LEU I 182 N ALA I 131 SHEET 4 AE2 4 SER I 160 VAL I 164 -1 N SER I 163 O SER I 177 SHEET 1 AE3 4 ALA I 154 LEU I 155 0 SHEET 2 AE3 4 LYS I 146 VAL I 151 -1 N VAL I 151 O ALA I 154 SHEET 3 AE3 4 VAL I 192 THR I 198 -1 O ALA I 194 N LYS I 150 SHEET 4 AE3 4 VAL I 206 ASN I 211 -1 O PHE I 210 N TYR I 193 SHEET 1 AE4 5 LYS J 151 PHE J 153 0 SHEET 2 AE4 5 ASP J 174 LEU J 180 1 O LEU J 180 N PHE J 153 SHEET 3 AE4 5 ILE J 244 HIS J 250 -1 O LEU J 247 N PHE J 177 SHEET 4 AE4 5 TRP J 212 TRP J 216 -1 N TRP J 216 O SER J 246 SHEET 5 AE4 5 LEU J 225 TYR J 229 -1 O ILE J 226 N ILE J 215 SHEET 1 AE5 4 ASN J 157 GLU J 161 0 SHEET 2 AE5 4 GLY J 259 HIS J 268 -1 O ALA J 262 N ILE J 160 SHEET 3 AE5 4 MET J 185 ASP J 195 -1 N GLU J 186 O VAL J 267 SHEET 4 AE5 4 LEU J 238 SER J 240 -1 O SER J 240 N ILE J 187 SHEET 1 AE6 9 VAL J 279 PRO J 280 0 SHEET 2 AE6 9 ILE J 293 ALA J 295 0 SHEET 3 AE6 9 LEU J 329 GLN J 345 -1 O GLN J 330 N SER J 294 SHEET 4 AE6 9 ALA J 347 ILE J 348 0 SHEET 5 AE6 9 GLY J 355 SER J 366 -1 O TYR J 356 N ALA J 347 SHEET 6 AE6 9 MET J 373 VAL J 374 -1 O MET J 373 N VAL J 365 SHEET 7 AE6 9 PHE J 384 GLN J 385 -1 O PHE J 384 N TYR J 361 SHEET 8 AE6 9 VAL J 394 HIS J 415 -1 O PHE J 406 N SER J 366 SHEET 9 AE6 9 ARG J 421 CYS J 427 -1 O GLU J 423 N ALA J 343 SHEET 1 AE7 2 ARG J 376 HIS J 377 0 SHEET 2 AE7 2 ASN J 380 HIS J 381 -1 O ASN J 380 N HIS J 377 SHEET 1 AE8 7 ASN J 436 MET J 437 0 SHEET 2 AE8 7 SER J 451 ALA J 452 0 SHEET 3 AE8 7 LEU J 488 GLN J 504 -1 O GLN J 489 N SER J 451 SHEET 4 AE8 7 VAL J 521 SER J 529 0 SHEET 5 AE8 7 GLU J 536 TYR J 537 -1 O GLU J 536 N TYR J 528 SHEET 6 AE8 7 ASP J 559 TRP J 578 -1 O GLU J 576 N LYS J 523 SHEET 7 AE8 7 ARG J 586 CYS J 592 -1 O LEU J 590 N GLY J 500 SHEET 1 AE9 4 GLN K 3 GLN K 6 0 SHEET 2 AE9 4 VAL K 18 SER K 25 -1 O LYS K 23 N VAL K 5 SHEET 3 AE9 4 THR K 78 LEU K 83 -1 O LEU K 83 N VAL K 18 SHEET 4 AE9 4 VAL K 68 ASP K 73 -1 N THR K 71 O TYR K 80 SHEET 1 AF1 7 GLU K 10 LYS K 12 0 SHEET 2 AF1 7 TYR K 33 GLN K 39 0 SHEET 3 AF1 7 GLU K 46 ASP K 52 -1 O GLU K 46 N GLN K 38 SHEET 4 AF1 7 LYS K 59 TYR K 60 -1 O LYS K 59 N ARG K 50 SHEET 5 AF1 7 ALA K 92 THR K 98 -1 O VAL K 93 N GLN K 39 SHEET 6 AF1 7 TYR K 110 TRP K 111 -1 O TYR K 110 N THR K 98 SHEET 7 AF1 7 THR K 115 VAL K 119 -1 O THR K 115 N TYR K 94 SHEET 1 AF2 5 SER K 128 LEU K 132 0 SHEET 2 AF2 5 THR K 143 TYR K 153 -1 O LEU K 149 N PHE K 130 SHEET 3 AF2 5 VAL K 171 THR K 173 0 SHEET 4 AF2 5 VAL K 177 GLN K 179 0 SHEET 5 AF2 5 LEU K 183 PRO K 193 -1 O LEU K 183 N GLN K 179 SHEET 1 AF3 3 THR K 159 SER K 161 0 SHEET 2 AF3 3 THR K 203 HIS K 208 -1 O ASP K 207 N THR K 159 SHEET 3 AF3 3 THR K 213 ARG K 218 -1 O VAL K 215 N VAL K 206 SHEET 1 AF4 3 MET L 4 THR L 5 0 SHEET 2 AF4 3 VAL L 19 VAL L 29 -1 O THR L 24 N THR L 5 SHEET 3 AF4 3 PHE L 63 ILE L 76 -1 O LEU L 74 N ILE L 21 SHEET 1 AF5 4 VAL L 116 PHE L 119 0 SHEET 2 AF5 4 THR L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AF5 4 TYR L 174 SER L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AF5 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AF6 4 ALA L 154 LEU L 155 0 SHEET 2 AF6 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AF6 4 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 4 AF6 4 VAL L 206 ASN L 211 -1 O PHE L 210 N TYR L 193 SSBOND 1 CYS A 149 CYS A 175 1555 1555 2.02 SSBOND 2 CYS A 208 CYS A 230 1555 1555 1.99 SSBOND 3 CYS A 277 CYS A 427 1555 1555 2.04 SSBOND 4 CYS A 434 CYS A 592 1555 1555 2.06 SSBOND 5 CYS B 22 CYS B 96 1555 1555 2.07 SSBOND 6 CYS B 148 CYS B 204 1555 1555 2.03 SSBOND 7 CYS C 23 CYS C 89 1555 1555 2.07 SSBOND 8 CYS C 135 CYS C 195 1555 1555 2.04 SSBOND 9 CYS D 149 CYS D 175 1555 1555 2.03 SSBOND 10 CYS D 208 CYS D 230 1555 1555 2.01 SSBOND 11 CYS D 277 CYS D 427 1555 1555 2.05 SSBOND 12 CYS D 434 CYS D 592 1555 1555 2.05 SSBOND 13 CYS E 22 CYS E 96 1555 1555 2.07 SSBOND 14 CYS E 148 CYS E 204 1555 1555 2.05 SSBOND 15 CYS F 23 CYS F 89 1555 1555 2.06 SSBOND 16 CYS F 135 CYS F 195 1555 1555 2.05 SSBOND 17 CYS G 149 CYS G 175 1555 1555 2.02 SSBOND 18 CYS G 208 CYS G 230 1555 1555 1.99 SSBOND 19 CYS G 277 CYS G 427 1555 1555 2.06 SSBOND 20 CYS G 434 CYS G 592 1555 1555 2.05 SSBOND 21 CYS H 22 CYS H 96 1555 1555 2.06 SSBOND 22 CYS H 148 CYS H 204 1555 1555 2.03 SSBOND 23 CYS I 23 CYS I 89 1555 1555 2.08 SSBOND 24 CYS I 135 CYS I 195 1555 1555 2.04 SSBOND 25 CYS J 149 CYS J 175 1555 1555 2.04 SSBOND 26 CYS J 208 CYS J 230 1555 1555 2.01 SSBOND 27 CYS J 277 CYS J 427 1555 1555 2.04 SSBOND 28 CYS J 434 CYS J 592 1555 1555 2.05 SSBOND 29 CYS K 22 CYS K 96 1555 1555 2.07 SSBOND 30 CYS K 148 CYS K 204 1555 1555 2.05 SSBOND 31 CYS L 23 CYS L 89 1555 1555 2.05 SSBOND 32 CYS L 135 CYS L 195 1555 1555 2.05 CISPEP 1 PHE A 165 PRO A 166 0 14.95 CISPEP 2 PHE B 154 PRO B 155 0 -8.83 CISPEP 3 GLU B 156 PRO B 157 0 -1.97 CISPEP 4 SER C 95 PRO C 96 0 2.78 CISPEP 5 PHE D 165 PRO D 166 0 15.24 CISPEP 6 PHE E 154 PRO E 155 0 -8.62 CISPEP 7 GLU E 156 PRO E 157 0 -0.39 CISPEP 8 SER F 95 PRO F 96 0 1.05 CISPEP 9 PHE G 165 PRO G 166 0 15.14 CISPEP 10 PHE H 154 PRO H 155 0 -9.19 CISPEP 11 GLU H 156 PRO H 157 0 -2.85 CISPEP 12 SER I 95 PRO I 96 0 3.07 CISPEP 13 PHE J 165 PRO J 166 0 14.87 CISPEP 14 PHE K 154 PRO K 155 0 -8.72 CISPEP 15 GLU K 156 PRO K 157 0 -1.22 CISPEP 16 SER L 95 PRO L 96 0 2.65 CRYST1 70.424 225.164 142.996 90.00 91.30 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 0.014200 0.000000 0.000322 0.00000 SCALE2 0.000000 0.004441 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006995 0.00000