HEADER PROTEIN BINDING 07-FEB-24 8Y9S TITLE CRYSTAL STRUCTURE OF NANOBODY MY6321 BOUND TO HUMAN SERUM ALBUMIN TITLE 2 (HSA) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALBUMIN; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: HSA; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY MY6321; COMPND 8 CHAIN: B, D; COMPND 9 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: ALB; SOURCE 6 EXPRESSION_SYSTEM: ORYZA SATIVA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4530; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 4932 KEYWDS ANTIBODY, HUMAN SERUM ALBUMIN, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR Y.DING,P.Y.ZHONG REVDAT 2 26-FEB-25 8Y9S 1 REMARK REVDAT 1 12-FEB-25 8Y9S 0 JRNL AUTH Y.DING,P.Y.ZHONG JRNL TITL CRYSTAL STRUCTURE OF NANOBODY MY6321 BOUND TO HUMAN SERUM JRNL TITL 2 ALBUMIN (HSA) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.88 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.88 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.25 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 36434 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.233 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.293 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700 REMARK 3 FREE R VALUE TEST SET COUNT : 1808 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) : 2.88 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.96 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2675 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.26 REMARK 3 BIN R VALUE (WORKING SET) : 0.3870 REMARK 3 BIN FREE R VALUE SET COUNT : 133 REMARK 3 BIN FREE R VALUE : 0.4190 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10901 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) : 72.93 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 6.60000 REMARK 3 B22 (A**2) : -5.73000 REMARK 3 B33 (A**2) : -1.57000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 2.23000 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): 0.474 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.511 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.159 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11342 ; 0.005 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 10688 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15310 ; 1.545 ; 1.865 REMARK 3 BOND ANGLES OTHERS (DEGREES): 24774 ; 0.556 ; 1.777 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1406 ; 7.844 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 60 ; 8.568 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2046 ;17.284 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1690 ; 0.157 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13170 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2490 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): 5636 ; 6.228 ; 7.092 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5636 ; 6.227 ; 7.092 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7038 ; 9.976 ;12.740 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7039 ; 9.976 ;12.740 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5706 ; 6.234 ; 7.592 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5707 ; 6.233 ; 7.592 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8273 ;10.099 ;13.763 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13165 ;15.588 ;68.460 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 13166 ;15.589 ;68.460 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK 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 THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 8Y9S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1300045099. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-JAN-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979183 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 : XDS 0.7.7 REMARK 200 DATA SCALING SOFTWARE : XDS 0.7.7 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38264 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880 REMARK 200 RESOLUTION RANGE LOW (A) : 46.250 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.28600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 6.80 REMARK 200 R MERGE FOR SHELL (I) : 2.01800 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: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M DL-MALIC ACID PH 7.0, 20% W/V REMARK 280 POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 298K 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 71.95000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 33430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 33370 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ARG A -5 REMARK 465 GLY A -4 REMARK 465 VAL A -3 REMARK 465 PHE A -2 REMARK 465 ARG A -1 REMARK 465 ARG A 0 REMARK 465 ASP A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 78 REMARK 465 THR A 83 REMARK 465 TYR A 84 REMARK 465 GLY A 85 REMARK 465 GLU A 86 REMARK 465 GLU A 97 REMARK 465 ARG A 98 REMARK 465 PRO A 110 REMARK 465 GLN A 170 REMARK 465 ALA A 171 REMARK 465 ALA A 172 REMARK 465 ASP A 173 REMARK 465 LYS A 174 REMARK 465 ALA A 175 REMARK 465 LEU A 178 REMARK 465 LEU A 585 REMARK 465 ARG C -5 REMARK 465 GLY C -4 REMARK 465 VAL C -3 REMARK 465 PHE C -2 REMARK 465 ARG C -1 REMARK 465 ARG C 0 REMARK 465 ASP C 1 REMARK 465 ALA C 2 REMARK 465 ARG C 81 REMARK 465 GLU C 82 REMARK 465 THR C 83 REMARK 465 TYR C 84 REMARK 465 GLY C 85 REMARK 465 GLU C 86 REMARK 465 MET C 87 REMARK 465 ARG C 98 REMARK 465 GLN C 170 REMARK 465 ALA C 171 REMARK 465 ALA C 172 REMARK 465 LEU C 585 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 NH2 ARG B 93 OD2 ASP C 56 2546 1.49 REMARK 500 OE2 GLU A 119 O VAL C 77 1554 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES 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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) 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 ATM2 ATM3 REMARK 500 PHE A 19 N - CA - CB ANGL. DEV. = -11.2 DEGREES REMARK 500 GLU A 60 CB - CA - C ANGL. DEV. = -12.4 DEGREES REMARK 500 CYS A 62 CB - CA - C ANGL. DEV. = 13.6 DEGREES REMARK 500 CYS A 75 CB - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 CYS A 90 CB - CA - C ANGL. DEV. = -13.3 DEGREES REMARK 500 PHE A 134 N - CA - CB ANGL. DEV. = -11.3 DEGREES REMARK 500 TYR A 150 N - CA - CB ANGL. DEV. = -12.4 DEGREES REMARK 500 CYS A 168 CB - CA - C ANGL. DEV. = 13.3 DEGREES REMARK 500 CYS A 253 CB - CA - C ANGL. DEV. = -17.8 DEGREES REMARK 500 PHE A 309 N - CA - CB ANGL. DEV. = -15.0 DEGREES REMARK 500 TYR A 370 N - CA - CB ANGL. DEV. = 14.4 DEGREES REMARK 500 TYR A 370 CA - CB - CG ANGL. DEV. = 14.6 DEGREES REMARK 500 CYS A 461 CB - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 500 ARG A 484 CB - CA - C ANGL. DEV. = -17.0 DEGREES REMARK 500 CYS C 62 CB - CA - C ANGL. DEV. = 15.3 DEGREES REMARK 500 CYS C 90 CB - CA - C ANGL. DEV. = -13.3 DEGREES REMARK 500 GLU C 95 N - CA - CB ANGL. DEV. = -12.2 DEGREES REMARK 500 PRO C 96 N - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 CYS C 253 CB - CA - C ANGL. DEV. = -15.2 DEGREES REMARK 500 TYR C 370 CA - CB - CG ANGL. DEV. = 14.2 DEGREES REMARK 500 PRO C 447 N - CA - CB ANGL. DEV. = -8.5 DEGREES REMARK 500 PRO C 468 N - CA - CB ANGL. DEV. = -7.8 DEGREES REMARK 500 MET C 548 CG - SD - CE ANGL. DEV. = 15.3 DEGREES 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 CYS A 34 125.38 -173.97 REMARK 500 ASN A 61 -1.06 83.52 REMARK 500 GLN A 104 -9.83 79.20 REMARK 500 GLU A 131 -59.56 71.23 REMARK 500 LEU A 250 -3.45 80.32 REMARK 500 ILE A 271 -67.54 -137.25 REMARK 500 PRO A 282 171.42 -58.69 REMARK 500 ASP A 301 60.79 65.29 REMARK 500 LYS A 372 42.17 -99.04 REMARK 500 THR A 478 31.50 -149.09 REMARK 500 ASN B 74 -57.17 73.33 REMARK 500 LEU B 102 44.37 -96.20 REMARK 500 GLN C 32 -71.06 -73.91 REMARK 500 CYS C 34 127.80 -172.38 REMARK 500 ASN C 61 -4.25 85.06 REMARK 500 ARG C 114 135.02 -38.48 REMARK 500 GLU C 131 -61.28 70.69 REMARK 500 PHE C 157 -37.04 -39.42 REMARK 500 ALA C 176 4.45 80.38 REMARK 500 LEU C 250 -59.77 70.31 REMARK 500 ILE C 271 -62.99 -130.69 REMARK 500 VAL C 310 -49.88 -130.81 REMARK 500 LYS C 313 34.05 -93.94 REMARK 500 LYS C 372 37.74 -91.60 REMARK 500 CYS C 437 -7.54 85.05 REMARK 500 ARG C 484 -70.40 -70.64 REMARK 500 PRO C 537 34.98 -86.37 REMARK 500 LYS C 538 -36.01 -131.71 REMARK 500 LEU D 102 46.44 -88.85 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 ALA A 582 LEU A 583 149.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 81 0.08 SIDE CHAIN REMARK 500 ARG A 144 0.17 SIDE CHAIN REMARK 500 ARG A 186 0.13 SIDE CHAIN REMARK 500 ARG A 197 0.10 SIDE CHAIN REMARK 500 ARG A 336 0.12 SIDE CHAIN REMARK 500 ARG A 337 0.18 SIDE CHAIN REMARK 500 ARG A 472 0.11 SIDE CHAIN REMARK 500 ARG A 484 0.24 SIDE CHAIN REMARK 500 ARG A 485 0.10 SIDE CHAIN REMARK 500 ARG B 19 0.07 SIDE CHAIN REMARK 500 ARG B 72 0.21 SIDE CHAIN REMARK 500 ARG B 110 0.09 SIDE CHAIN REMARK 500 ARG C 114 0.15 SIDE CHAIN REMARK 500 ARG C 218 0.18 SIDE CHAIN REMARK 500 ARG C 484 0.11 SIDE CHAIN REMARK 500 ARG C 521 0.13 SIDE CHAIN REMARK 500 ARG D 67 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLU A 57 12.02 REMARK 500 GLU A 57 12.59 REMARK 500 GLU C 57 10.49 REMARK 500 GLU C 57 11.42 REMARK 500 REMARK 500 REMARK: NULL DBREF 8Y9S A -5 585 UNP P02768 ALBU_HUMAN 19 609 DBREF 8Y9S B 1 122 PDB 8Y9S 8Y9S 1 122 DBREF 8Y9S C -5 585 UNP P02768 ALBU_HUMAN 19 609 DBREF 8Y9S D 1 122 PDB 8Y9S 8Y9S 1 122 SEQRES 1 A 591 ARG GLY VAL PHE ARG ARG ASP ALA HIS LYS SER GLU VAL SEQRES 2 A 591 ALA HIS ARG PHE LYS ASP LEU GLY GLU GLU ASN PHE LYS SEQRES 3 A 591 ALA LEU VAL LEU ILE ALA PHE ALA GLN TYR LEU GLN GLN SEQRES 4 A 591 CYS PRO PHE GLU ASP HIS VAL LYS LEU VAL ASN GLU VAL SEQRES 5 A 591 THR GLU PHE ALA LYS THR CYS VAL ALA ASP GLU SER ALA SEQRES 6 A 591 GLU ASN CYS ASP LYS SER LEU HIS THR LEU PHE GLY ASP SEQRES 7 A 591 LYS LEU CYS THR VAL ALA THR LEU ARG GLU THR TYR GLY SEQRES 8 A 591 GLU MET ALA ASP CYS CYS ALA LYS GLN GLU PRO GLU ARG SEQRES 9 A 591 ASN GLU CYS PHE LEU GLN HIS LYS ASP ASP ASN PRO ASN SEQRES 10 A 591 LEU PRO ARG LEU VAL ARG PRO GLU VAL ASP VAL MET CYS SEQRES 11 A 591 THR ALA PHE HIS ASP ASN GLU GLU THR PHE LEU LYS LYS SEQRES 12 A 591 TYR LEU TYR GLU ILE ALA ARG ARG HIS PRO TYR PHE TYR SEQRES 13 A 591 ALA PRO GLU LEU LEU PHE PHE ALA LYS ARG TYR LYS ALA SEQRES 14 A 591 ALA PHE THR GLU CYS CYS GLN ALA ALA ASP LYS ALA ALA SEQRES 15 A 591 CYS LEU LEU PRO LYS LEU ASP GLU LEU ARG ASP GLU GLY SEQRES 16 A 591 LYS ALA SER SER ALA LYS GLN ARG LEU LYS CYS ALA SER SEQRES 17 A 591 LEU GLN LYS PHE GLY GLU ARG ALA PHE LYS ALA TRP ALA SEQRES 18 A 591 VAL ALA ARG LEU SER GLN ARG PHE PRO LYS ALA GLU PHE SEQRES 19 A 591 ALA GLU VAL SER LYS LEU VAL THR ASP LEU THR LYS VAL SEQRES 20 A 591 HIS THR GLU CYS CYS HIS GLY ASP LEU LEU GLU CYS ALA SEQRES 21 A 591 ASP ASP ARG ALA ASP LEU ALA LYS TYR ILE CYS GLU ASN SEQRES 22 A 591 GLN ASP SER ILE SER SER LYS LEU LYS GLU CYS CYS GLU SEQRES 23 A 591 LYS PRO LEU LEU GLU LYS SER HIS CYS ILE ALA GLU VAL SEQRES 24 A 591 GLU ASN ASP GLU MET PRO ALA ASP LEU PRO SER LEU ALA SEQRES 25 A 591 ALA ASP PHE VAL GLU SER LYS ASP VAL CYS LYS ASN TYR SEQRES 26 A 591 ALA GLU ALA LYS ASP VAL PHE LEU GLY MET PHE LEU TYR SEQRES 27 A 591 GLU TYR ALA ARG ARG HIS PRO ASP TYR SER VAL VAL LEU SEQRES 28 A 591 LEU LEU ARG LEU ALA LYS THR TYR GLU THR THR LEU GLU SEQRES 29 A 591 LYS CYS CYS ALA ALA ALA ASP PRO HIS GLU CYS TYR ALA SEQRES 30 A 591 LYS VAL PHE ASP GLU PHE LYS PRO LEU VAL GLU GLU PRO SEQRES 31 A 591 GLN ASN LEU ILE LYS GLN ASN CYS GLU LEU PHE GLU GLN SEQRES 32 A 591 LEU GLY GLU TYR LYS PHE GLN ASN ALA LEU LEU VAL ARG SEQRES 33 A 591 TYR THR LYS LYS VAL PRO GLN VAL SER THR PRO THR LEU SEQRES 34 A 591 VAL GLU VAL SER ARG ASN LEU GLY LYS VAL GLY SER LYS SEQRES 35 A 591 CYS CYS LYS HIS PRO GLU ALA LYS ARG MET PRO CYS ALA SEQRES 36 A 591 GLU ASP TYR LEU SER VAL VAL LEU ASN GLN LEU CYS VAL SEQRES 37 A 591 LEU HIS GLU LYS THR PRO VAL SER ASP ARG VAL THR LYS SEQRES 38 A 591 CYS CYS THR GLU SER LEU VAL ASN ARG ARG PRO CYS PHE SEQRES 39 A 591 SER ALA LEU GLU VAL ASP GLU THR TYR VAL PRO LYS GLU SEQRES 40 A 591 PHE ASN ALA GLU THR PHE THR PHE HIS ALA ASP ILE CYS SEQRES 41 A 591 THR LEU SER GLU LYS GLU ARG GLN ILE LYS LYS GLN THR SEQRES 42 A 591 ALA LEU VAL GLU LEU VAL LYS HIS LYS PRO LYS ALA THR SEQRES 43 A 591 LYS GLU GLN LEU LYS ALA VAL MET ASP ASP PHE ALA ALA SEQRES 44 A 591 PHE VAL GLU LYS CYS CYS LYS ALA ASP ASP LYS GLU THR SEQRES 45 A 591 CYS PHE ALA GLU GLU GLY LYS LYS LEU VAL ALA ALA SER SEQRES 46 A 591 GLN ALA ALA LEU GLY LEU SEQRES 1 B 122 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 122 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 B 122 TYR MET SER SER THR TYR TYR MET ALA TRP PHE ARG GLN SEQRES 4 B 122 PRO PRO GLY LYS GLY LEU GLU GLY VAL ALA LEU ILE SER SEQRES 5 B 122 PRO TYR GLY GLY ALA THR ASN TYR ALA ASP SER VAL LYS SEQRES 6 B 122 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 B 122 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 B 122 ALA ARG TYR TYR CYS ALA ALA GLY SER THR LEU THR MET SEQRES 9 B 122 VAL VAL ALA ASN TYR ARG TYR TRP GLY GLN GLY THR LEU SEQRES 10 B 122 VAL THR VAL SER SER SEQRES 1 C 591 ARG GLY VAL PHE ARG ARG ASP ALA HIS LYS SER GLU VAL SEQRES 2 C 591 ALA HIS ARG PHE LYS ASP LEU GLY GLU GLU ASN PHE LYS SEQRES 3 C 591 ALA LEU VAL LEU ILE ALA PHE ALA GLN TYR LEU GLN GLN SEQRES 4 C 591 CYS PRO PHE GLU ASP HIS VAL LYS LEU VAL ASN GLU VAL SEQRES 5 C 591 THR GLU PHE ALA LYS THR CYS VAL ALA ASP GLU SER ALA SEQRES 6 C 591 GLU ASN CYS ASP LYS SER LEU HIS THR LEU PHE GLY ASP SEQRES 7 C 591 LYS LEU CYS THR VAL ALA THR LEU ARG GLU THR TYR GLY SEQRES 8 C 591 GLU MET ALA ASP CYS CYS ALA LYS GLN GLU PRO GLU ARG SEQRES 9 C 591 ASN GLU CYS PHE LEU GLN HIS LYS ASP ASP ASN PRO ASN SEQRES 10 C 591 LEU PRO ARG LEU VAL ARG PRO GLU VAL ASP VAL MET CYS SEQRES 11 C 591 THR ALA PHE HIS ASP ASN GLU GLU THR PHE LEU LYS LYS SEQRES 12 C 591 TYR LEU TYR GLU ILE ALA ARG ARG HIS PRO TYR PHE TYR SEQRES 13 C 591 ALA PRO GLU LEU LEU PHE PHE ALA LYS ARG TYR LYS ALA SEQRES 14 C 591 ALA PHE THR GLU CYS CYS GLN ALA ALA ASP LYS ALA ALA SEQRES 15 C 591 CYS LEU LEU PRO LYS LEU ASP GLU LEU ARG ASP GLU GLY SEQRES 16 C 591 LYS ALA SER SER ALA LYS GLN ARG LEU LYS CYS ALA SER SEQRES 17 C 591 LEU GLN LYS PHE GLY GLU ARG ALA PHE LYS ALA TRP ALA SEQRES 18 C 591 VAL ALA ARG LEU SER GLN ARG PHE PRO LYS ALA GLU PHE SEQRES 19 C 591 ALA GLU VAL SER LYS LEU VAL THR ASP LEU THR LYS VAL SEQRES 20 C 591 HIS THR GLU CYS CYS HIS GLY ASP LEU LEU GLU CYS ALA SEQRES 21 C 591 ASP ASP ARG ALA ASP LEU ALA LYS TYR ILE CYS GLU ASN SEQRES 22 C 591 GLN ASP SER ILE SER SER LYS LEU LYS GLU CYS CYS GLU SEQRES 23 C 591 LYS PRO LEU LEU GLU LYS SER HIS CYS ILE ALA GLU VAL SEQRES 24 C 591 GLU ASN ASP GLU MET PRO ALA ASP LEU PRO SER LEU ALA SEQRES 25 C 591 ALA ASP PHE VAL GLU SER LYS ASP VAL CYS LYS ASN TYR SEQRES 26 C 591 ALA GLU ALA LYS ASP VAL PHE LEU GLY MET PHE LEU TYR SEQRES 27 C 591 GLU TYR ALA ARG ARG HIS PRO ASP TYR SER VAL VAL LEU SEQRES 28 C 591 LEU LEU ARG LEU ALA LYS THR TYR GLU THR THR LEU GLU SEQRES 29 C 591 LYS CYS CYS ALA ALA ALA ASP PRO HIS GLU CYS TYR ALA SEQRES 30 C 591 LYS VAL PHE ASP GLU PHE LYS PRO LEU VAL GLU GLU PRO SEQRES 31 C 591 GLN ASN LEU ILE LYS GLN ASN CYS GLU LEU PHE GLU GLN SEQRES 32 C 591 LEU GLY GLU TYR LYS PHE GLN ASN ALA LEU LEU VAL ARG SEQRES 33 C 591 TYR THR LYS LYS VAL PRO GLN VAL SER THR PRO THR LEU SEQRES 34 C 591 VAL GLU VAL SER ARG ASN LEU GLY LYS VAL GLY SER LYS SEQRES 35 C 591 CYS CYS LYS HIS PRO GLU ALA LYS ARG MET PRO CYS ALA SEQRES 36 C 591 GLU ASP TYR LEU SER VAL VAL LEU ASN GLN LEU CYS VAL SEQRES 37 C 591 LEU HIS GLU LYS THR PRO VAL SER ASP ARG VAL THR LYS SEQRES 38 C 591 CYS CYS THR GLU SER LEU VAL ASN ARG ARG PRO CYS PHE SEQRES 39 C 591 SER ALA LEU GLU VAL ASP GLU THR TYR VAL PRO LYS GLU SEQRES 40 C 591 PHE ASN ALA GLU THR PHE THR PHE HIS ALA ASP ILE CYS SEQRES 41 C 591 THR LEU SER GLU LYS GLU ARG GLN ILE LYS LYS GLN THR SEQRES 42 C 591 ALA LEU VAL GLU LEU VAL LYS HIS LYS PRO LYS ALA THR SEQRES 43 C 591 LYS GLU GLN LEU LYS ALA VAL MET ASP ASP PHE ALA ALA SEQRES 44 C 591 PHE VAL GLU LYS CYS CYS LYS ALA ASP ASP LYS GLU THR SEQRES 45 C 591 CYS PHE ALA GLU GLU GLY LYS LYS LEU VAL ALA ALA SER SEQRES 46 C 591 GLN ALA ALA LEU GLY LEU SEQRES 1 D 122 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 122 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 D 122 TYR MET SER SER THR TYR TYR MET ALA TRP PHE ARG GLN SEQRES 4 D 122 PRO PRO GLY LYS GLY LEU GLU GLY VAL ALA LEU ILE SER SEQRES 5 D 122 PRO TYR GLY GLY ALA THR ASN TYR ALA ASP SER VAL LYS SEQRES 6 D 122 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 122 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 D 122 ALA ARG TYR TYR CYS ALA ALA GLY SER THR LEU THR MET SEQRES 9 D 122 VAL VAL ALA ASN TYR ARG TYR TRP GLY GLN GLY THR LEU SEQRES 10 D 122 VAL THR VAL SER SER HELIX 1 AA1 SER A 5 GLY A 15 1 11 HELIX 2 AA2 GLY A 15 LEU A 31 1 17 HELIX 3 AA3 PRO A 35 ASP A 56 1 22 HELIX 4 AA4 SER A 65 THR A 76 1 12 HELIX 5 AA5 ALA A 88 LYS A 93 1 6 HELIX 6 AA6 GLU A 119 ASN A 130 1 12 HELIX 7 AA7 GLU A 131 HIS A 146 1 16 HELIX 8 AA8 TYR A 150 CYS A 169 1 20 HELIX 9 AA9 PRO A 180 PHE A 223 1 44 HELIX 10 AB1 GLU A 227 GLY A 248 1 22 HELIX 11 AB2 LEU A 250 ASN A 267 1 18 HELIX 12 AB3 GLN A 268 ILE A 271 5 4 HELIX 13 AB4 GLU A 277 LYS A 281 5 5 HELIX 14 AB5 PRO A 282 VAL A 293 1 12 HELIX 15 AB6 LEU A 305 VAL A 310 1 6 HELIX 16 AB7 ASP A 314 ALA A 322 1 9 HELIX 17 AB8 ALA A 322 HIS A 338 1 17 HELIX 18 AB9 SER A 342 ALA A 362 1 21 HELIX 19 AC1 ASP A 365 LYS A 372 1 8 HELIX 20 AC2 VAL A 373 VAL A 415 1 43 HELIX 21 AC3 SER A 419 CYS A 438 1 20 HELIX 22 AC4 PRO A 441 ALA A 443 5 3 HELIX 23 AC5 LYS A 444 THR A 467 1 24 HELIX 24 AC6 SER A 470 THR A 478 1 9 HELIX 25 AC7 ASN A 483 LEU A 491 1 9 HELIX 26 AC8 ALA A 504 THR A 508 5 5 HELIX 27 AC9 ALA A 511 LEU A 516 1 6 HELIX 28 AD1 SER A 517 LYS A 536 1 20 HELIX 29 AD2 GLU A 542 ALA A 561 1 20 HELIX 30 AD3 ASP A 563 ALA A 582 1 20 HELIX 31 AD4 ASP B 62 LYS B 65 5 4 HELIX 32 AD5 LYS B 87 THR B 91 5 5 HELIX 33 AD6 VAL B 105 ALA B 107 5 3 HELIX 34 AD7 SER C 5 LEU C 31 1 27 HELIX 35 AD8 PRO C 35 ASP C 56 1 22 HELIX 36 AD9 SER C 65 ALA C 78 1 14 HELIX 37 AE1 ASP C 89 LYS C 93 1 5 HELIX 38 AE2 GLU C 100 HIS C 105 1 6 HELIX 39 AE3 GLU C 119 ASN C 130 1 12 HELIX 40 AE4 GLU C 131 HIS C 146 1 16 HELIX 41 AE5 TYR C 150 CYS C 169 1 20 HELIX 42 AE6 CYS C 177 GLY C 207 1 31 HELIX 43 AE7 GLY C 207 PHE C 223 1 17 HELIX 44 AE8 GLU C 227 GLY C 248 1 22 HELIX 45 AE9 LEU C 250 ASN C 267 1 18 HELIX 46 AF1 GLN C 268 ILE C 271 5 4 HELIX 47 AF2 GLU C 277 LYS C 281 5 5 HELIX 48 AF3 PRO C 282 GLU C 292 1 11 HELIX 49 AF4 LEU C 305 VAL C 310 1 6 HELIX 50 AF5 ASP C 314 ALA C 322 1 9 HELIX 51 AF6 ALA C 322 HIS C 338 1 17 HELIX 52 AF7 SER C 342 CYS C 361 1 20 HELIX 53 AF8 ASP C 365 LYS C 372 1 8 HELIX 54 AF9 VAL C 373 VAL C 415 1 43 HELIX 55 AG1 SER C 419 LYS C 439 1 21 HELIX 56 AG2 PRO C 441 THR C 467 1 27 HELIX 57 AG3 SER C 470 GLU C 479 1 10 HELIX 58 AG4 SER C 480 VAL C 482 5 3 HELIX 59 AG5 ASN C 483 ALA C 490 1 8 HELIX 60 AG6 ASN C 503 THR C 508 1 6 HELIX 61 AG7 ALA C 511 LEU C 516 1 6 HELIX 62 AG8 SER C 517 LYS C 536 1 20 HELIX 63 AG9 GLU C 542 ALA C 561 1 20 HELIX 64 AH1 ASP C 563 ALA C 582 1 20 HELIX 65 AH2 MET D 28 TYR D 32 5 5 HELIX 66 AH3 ASP D 62 LYS D 65 5 4 HELIX 67 AH4 LYS D 87 THR D 91 5 5 HELIX 68 AH5 VAL D 105 ALA D 107 5 3 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 THR B 78 MET B 83 -1 O LEU B 79 N CYS B 22 SHEET 4 AA1 4 PHE B 68 ARG B 72 -1 N SER B 71 O TYR B 80 SHEET 1 AA2 2 LEU B 11 VAL B 12 0 SHEET 2 AA2 2 THR B 119 VAL B 120 1 O THR B 119 N VAL B 12 SHEET 1 AA3 5 THR B 58 TYR B 60 0 SHEET 2 AA3 5 GLU B 46 ILE B 51 -1 N LEU B 50 O ASN B 59 SHEET 3 AA3 5 TYR B 33 GLN B 39 -1 N TRP B 36 O ALA B 49 SHEET 4 AA3 5 ARG B 93 GLY B 99 -1 O TYR B 95 N PHE B 37 SHEET 5 AA3 5 TYR B 109 TRP B 112 -1 O TYR B 111 N ALA B 98 SHEET 1 AA4 5 THR B 58 TYR B 60 0 SHEET 2 AA4 5 GLU B 46 ILE B 51 -1 N LEU B 50 O ASN B 59 SHEET 3 AA4 5 TYR B 33 GLN B 39 -1 N TRP B 36 O ALA B 49 SHEET 4 AA4 5 ARG B 93 GLY B 99 -1 O TYR B 95 N PHE B 37 SHEET 5 AA4 5 THR B 116 LEU B 117 -1 O THR B 116 N TYR B 94 SHEET 1 AA5 4 LEU D 4 SER D 7 0 SHEET 2 AA5 4 LEU D 18 ALA D 24 -1 O SER D 21 N SER D 7 SHEET 3 AA5 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA5 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AA6 6 LEU D 11 VAL D 12 0 SHEET 2 AA6 6 THR D 116 VAL D 120 1 O THR D 119 N VAL D 12 SHEET 3 AA6 6 ALA D 92 GLY D 99 -1 N ALA D 92 O VAL D 118 SHEET 4 AA6 6 TYR D 33 GLN D 39 -1 N TYR D 33 O GLY D 99 SHEET 5 AA6 6 GLU D 46 ILE D 51 -1 O ALA D 49 N TRP D 36 SHEET 6 AA6 6 THR D 58 TYR D 60 -1 O ASN D 59 N LEU D 50 SHEET 1 AA7 4 LEU D 11 VAL D 12 0 SHEET 2 AA7 4 THR D 116 VAL D 120 1 O THR D 119 N VAL D 12 SHEET 3 AA7 4 ALA D 92 GLY D 99 -1 N ALA D 92 O VAL D 118 SHEET 4 AA7 4 TYR D 109 TRP D 112 -1 O TYR D 111 N ALA D 98 SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.06 SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.04 SSBOND 3 CYS A 90 CYS A 101 1555 1555 2.02 SSBOND 4 CYS A 124 CYS A 169 1555 1555 2.06 SSBOND 5 CYS A 168 CYS A 177 1555 1555 2.04 SSBOND 6 CYS A 200 CYS A 246 1555 1555 2.01 SSBOND 7 CYS A 245 CYS A 253 1555 1555 2.00 SSBOND 8 CYS A 265 CYS A 279 1555 1555 2.86 SSBOND 9 CYS A 316 CYS A 361 1555 1555 2.03 SSBOND 10 CYS A 360 CYS A 369 1555 1555 2.05 SSBOND 11 CYS A 392 CYS A 438 1555 1555 2.28 SSBOND 12 CYS A 437 CYS A 448 1555 1555 2.88 SSBOND 13 CYS A 461 CYS A 477 1555 1555 2.05 SSBOND 14 CYS A 514 CYS A 559 1555 1555 2.06 SSBOND 15 CYS A 558 CYS A 567 1555 1555 2.94 SSBOND 16 CYS B 22 CYS B 96 1555 1555 2.71 SSBOND 17 CYS C 53 CYS C 62 1555 1555 2.07 SSBOND 18 CYS C 75 CYS C 91 1555 1555 2.05 SSBOND 19 CYS C 124 CYS C 169 1555 1555 2.08 SSBOND 20 CYS C 168 CYS C 177 1555 1555 2.02 SSBOND 21 CYS C 200 CYS C 246 1555 1555 2.01 SSBOND 22 CYS C 245 CYS C 253 1555 1555 2.01 SSBOND 23 CYS C 265 CYS C 279 1555 1555 2.66 SSBOND 24 CYS C 316 CYS C 361 1555 1555 2.03 SSBOND 25 CYS C 360 CYS C 369 1555 1555 2.04 SSBOND 26 CYS C 392 CYS C 438 1555 1555 2.03 SSBOND 27 CYS C 437 CYS C 448 1555 1555 2.05 SSBOND 28 CYS C 461 CYS C 477 1555 1555 2.03 SSBOND 29 CYS C 514 CYS C 559 1555 1555 2.07 SSBOND 30 CYS D 22 CYS D 96 1555 1555 2.61 CRYST1 65.260 143.900 93.670 90.00 100.23 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015323 0.000000 0.002765 0.00000 SCALE2 0.000000 0.006949 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010848 0.00000