HEADER OXIDOREDUCTASE/IMMUNE SYSTEM 09-FEB-24 8YAF TITLE SOD1, NANOBODY1 AND NANOBODY2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN]; COMPND 3 CHAIN: A, D, H, L, P, T; COMPND 4 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1; COMPND 5 EC: 1.15.1.1; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NB1; COMPND 9 CHAIN: B, E, I, M, Q, U; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: NB2; COMPND 13 CHAIN: C, F, J, N, R, V; COMPND 14 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: SOD1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS; SOURCE 15 ORGANISM_TAXID: 996650; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY COMPLEX, OXIDOREDUCTASE, OXIDOREDUCTASE/IMMUNE SYSTEM, KEYWDS 2 OXIDOREDUCTASE-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR S.CHENG REVDAT 1 21-MAY-25 8YAF 0 JRNL AUTH S.CHENG JRNL TITL SOD1, NANOBODY1 AND NANOBODY2 COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.28 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.28 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.68 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 58593 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.201 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.410 REMARK 3 FREE R VALUE TEST SET COUNT : 1997 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 81.6800 - 7.8900 0.98 4244 150 0.1919 0.2234 REMARK 3 2 7.8900 - 6.2700 1.00 4116 146 0.2032 0.2577 REMARK 3 3 6.2700 - 5.4700 1.00 4091 144 0.1984 0.2279 REMARK 3 4 5.4700 - 4.9700 1.00 4058 143 0.1788 0.2351 REMARK 3 5 4.9700 - 4.6200 1.00 4053 144 0.1676 0.2251 REMARK 3 6 4.6200 - 4.3500 1.00 4023 142 0.1617 0.2070 REMARK 3 7 4.3500 - 4.1300 1.00 4010 141 0.1811 0.2496 REMARK 3 8 4.1300 - 3.9500 1.00 4030 141 0.1881 0.2176 REMARK 3 9 3.9500 - 3.8000 1.00 4010 141 0.2114 0.2733 REMARK 3 10 3.8000 - 3.6600 1.00 3999 141 0.2234 0.2647 REMARK 3 11 3.6600 - 3.5500 1.00 4000 142 0.2238 0.2801 REMARK 3 12 3.5500 - 3.4500 1.00 3978 141 0.2434 0.3214 REMARK 3 13 3.4500 - 3.3600 1.00 4020 141 0.2632 0.3319 REMARK 3 14 3.3600 - 3.2800 1.00 3964 140 0.2747 0.3117 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.820 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.011 NULL REMARK 3 ANGLE : 1.321 NULL REMARK 3 CHIRALITY : 0.066 2614 REMARK 3 PLANARITY : 0.011 3284 REMARK 3 DIHEDRAL : 6.760 2571 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8YAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 22-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1300045258. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-DEC-21 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 : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58709 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.280 REMARK 200 RESOLUTION RANGE LOW (A) : 117.910 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 10.20 REMARK 200 R MERGE (I) : 0.25500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.28 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.45 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 10.50 REMARK 200 R MERGE FOR SHELL (I) : 1.03400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 5% (V/V) ISOPROPANOL, 2.0 M AMMONIUM REMARK 280 SULFATE, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 69.97450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 109.44600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 69.97450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 109.44600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 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: H, I, J 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: L, M, N 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q, R 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, U, V 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 GLN A 153 REMARK 465 SER B 1 REMARK 465 GLN B 2 REMARK 465 VAL B 3 REMARK 465 SER B 118 REMARK 465 SER E 1 REMARK 465 GLN E 2 REMARK 465 VAL E 3 REMARK 465 SER I 1 REMARK 465 GLN I 2 REMARK 465 VAL I 3 REMARK 465 SER M 1 REMARK 465 GLN M 2 REMARK 465 VAL M 3 REMARK 465 SER Q 1 REMARK 465 GLN Q 2 REMARK 465 VAL Q 3 REMARK 465 SER U 1 REMARK 465 GLN U 2 REMARK 465 VAL U 3 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 ASP A 96 CG REMARK 480 GLU A 132 CD REMARK 480 ARG D 69 CZ REMARK 480 ASP D 90 C REMARK 480 ASP D 96 CG REMARK 480 GLU D 132 CD REMARK 480 GLU D 133 CD REMARK 480 GLN D 153 C REMARK 480 ASP H 96 CG REMARK 480 GLU H 132 CD REMARK 480 GLU H 133 CD REMARK 480 GLN H 153 C REMARK 480 ASP L 96 CG REMARK 480 GLU L 132 OE1 REMARK 480 GLU L 133 CD REMARK 480 GLN L 153 C REMARK 480 ASP P 96 OD2 REMARK 480 GLU P 132 CD REMARK 480 GLU P 133 CD REMARK 480 GLN P 153 C REMARK 480 ARG T 69 CZ REMARK 480 ASP T 96 CG REMARK 480 GLN T 153 C 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 CD2 HIS P 63 ZN ZN P 201 1.26 REMARK 500 OD1 ASP A 83 ZN ZN A 201 1.34 REMARK 500 OD1 ASP H 83 ZN ZN H 201 1.40 REMARK 500 OD1 ASP T 83 ZN ZN T 201 1.44 REMARK 500 OD1 ASP L 83 ZN ZN L 201 1.45 REMARK 500 OD1 ASP P 83 ZN ZN P 201 1.64 REMARK 500 CG HIS P 63 ZN ZN P 201 1.66 REMARK 500 OD2 ASP H 83 ZN ZN H 201 1.70 REMARK 500 ND1 HIS T 80 OD2 ASP T 83 1.88 REMARK 500 ND1 HIS D 63 OD1 ASP D 83 1.91 REMARK 500 ND1 HIS L 80 OD2 ASP L 83 1.98 REMARK 500 ND1 HIS D 80 OD2 ASP D 83 1.98 REMARK 500 ND1 HIS H 80 OD2 ASP H 83 2.07 REMARK 500 ND1 HIS A 80 OD2 ASP A 83 2.09 REMARK 500 ND1 HIS T 71 OD2 ASP T 83 2.09 REMARK 500 ND1 HIS H 71 OD2 ASP H 83 2.10 REMARK 500 O ASP P 52 OG SER P 59 2.11 REMARK 500 ND1 HIS P 80 OD2 ASP P 83 2.15 REMARK 500 O PRO M 90 OG1 THR M 93 2.17 REMARK 500 O PHE P 50 OG1 THR P 116 2.18 REMARK 500 ND1 HIS A 71 OD2 ASP A 83 2.18 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 OE1 GLN J 3 OG1 THR N 124 2555 2.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO R 31 CB PRO R 31 CG -0.532 REMARK 500 PRO R 31 CG PRO R 31 CD -0.265 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 PRO D 28 CA - CB - CG ANGL. DEV. = -13.0 DEGREES REMARK 500 PRO D 28 N - CD - CG ANGL. DEV. = -11.3 DEGREES REMARK 500 ASP D 83 OD1 - CG - OD2 ANGL. DEV. = -12.8 DEGREES REMARK 500 ASP D 83 CB - CG - OD1 ANGL. DEV. = 10.3 DEGREES REMARK 500 LYS F 77 CD - CE - NZ ANGL. DEV. = 17.0 DEGREES REMARK 500 ASP H 83 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES REMARK 500 ASP L 83 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES REMARK 500 LEU L 84 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 LYS N 77 CD - CE - NZ ANGL. DEV. = -23.6 DEGREES REMARK 500 ASP P 83 CB - CG - OD1 ANGL. DEV. = 9.9 DEGREES REMARK 500 PRO R 31 CA - N - CD ANGL. DEV. = -10.9 DEGREES REMARK 500 PRO R 31 CA - CB - CG ANGL. DEV. = -35.0 DEGREES REMARK 500 PRO R 31 CB - CG - CD ANGL. DEV. = 32.6 DEGREES REMARK 500 PRO R 31 N - CD - CG ANGL. DEV. = -27.1 DEGREES REMARK 500 ASP T 83 CB - CG - OD2 ANGL. DEV. = 5.5 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 GLN A 15 137.06 -171.94 REMARK 500 ASN A 26 22.07 44.36 REMARK 500 ALA A 55 41.97 -97.38 REMARK 500 LYS A 122 -151.01 -90.08 REMARK 500 SER B 8 155.67 176.68 REMARK 500 TYR B 33 56.16 27.90 REMARK 500 ASN B 87 82.95 36.95 REMARK 500 ALA B 94 -177.41 175.09 REMARK 500 ASP C 118 -60.87 -97.32 REMARK 500 SER D 25 132.00 -38.21 REMARK 500 GLU D 40 109.20 -48.42 REMARK 500 ASP D 83 102.44 -58.83 REMARK 500 ASP D 90 -168.73 -68.15 REMARK 500 LYS D 122 -158.58 -102.77 REMARK 500 ALA E 34 76.86 -152.68 REMARK 500 ALA E 63 158.15 -49.65 REMARK 500 ARG E 69 -41.31 -133.03 REMARK 500 ASN E 79 46.06 73.39 REMARK 500 ALA E 94 -172.85 -172.24 REMARK 500 THR E 103 -169.21 -166.00 REMARK 500 SER F 7 -175.81 175.59 REMARK 500 LYS F 46 -164.50 -100.89 REMARK 500 GLU F 47 -160.03 -105.50 REMARK 500 GLU F 49 -96.09 -109.83 REMARK 500 GLU F 68 -114.57 -115.76 REMARK 500 ARG F 80 72.77 31.80 REMARK 500 LEU F 112 46.75 -106.48 REMARK 500 GLN H 15 147.79 -175.59 REMARK 500 LYS H 23 -71.79 -63.35 REMARK 500 HIS H 110 34.26 -84.07 REMARK 500 LYS H 122 -165.63 -105.15 REMARK 500 LYS H 136 -60.81 -102.09 REMARK 500 SER H 142 171.30 -57.60 REMARK 500 TYR I 33 52.29 38.70 REMARK 500 ALA I 94 -178.91 -179.42 REMARK 500 TRP J 36 73.79 -113.13 REMARK 500 SER J 59 3.48 -151.66 REMARK 500 GLU J 68 -99.97 -68.77 REMARK 500 ARG J 80 60.12 26.04 REMARK 500 ASP J 88 76.67 48.75 REMARK 500 ALA J 95 178.50 178.92 REMARK 500 LEU J 112 53.24 -102.92 REMARK 500 SER L 25 178.50 -59.22 REMARK 500 ASN L 26 0.88 51.97 REMARK 500 PHE L 45 104.68 -162.28 REMARK 500 HIS L 110 32.43 -87.17 REMARK 500 LYS L 122 -149.53 -105.33 REMARK 500 LYS L 136 -77.70 -109.68 REMARK 500 TYR M 33 56.65 36.02 REMARK 500 LYS M 67 108.92 -58.00 REMARK 500 REMARK 500 THIS ENTRY HAS 98 RAMACHANDRAN OUTLIERS. 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 J 41 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 615 REMARK 615 ZERO OCCUPANCY ATOM REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 615 M RES C SSEQI REMARK 615 ZN A 201 REMARK 615 ZN D 201 REMARK 615 ZN H 201 REMARK 615 ZN L 201 REMARK 615 ZN P 201 REMARK 615 ZN T 201 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 63 ND1 REMARK 620 2 HIS A 71 ND1 108.8 REMARK 620 3 HIS A 80 ND1 112.0 83.8 REMARK 620 4 ASP A 83 OD2 168.0 63.0 59.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN D 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS D 63 ND1 REMARK 620 2 HIS D 71 ND1 86.9 REMARK 620 3 HIS D 80 ND1 88.5 99.6 REMARK 620 4 ASP D 83 OD2 83.1 52.9 46.8 REMARK 620 5 LYS D 136 O 115.1 101.7 148.8 149.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 63 ND1 REMARK 620 2 HIS H 71 ND1 73.3 REMARK 620 3 HIS H 80 ND1 119.0 83.4 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS L 63 ND1 REMARK 620 2 HIS L 71 ND1 111.9 REMARK 620 3 HIS L 80 ND1 123.9 100.6 REMARK 620 4 ASP L 83 OD2 173.1 70.7 60.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN P 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS P 63 ND1 REMARK 620 2 HIS P 63 NE2 58.4 REMARK 620 3 HIS P 71 ND1 150.8 92.6 REMARK 620 4 HIS P 80 ND1 131.8 151.6 75.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN T 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS T 63 ND1 REMARK 620 2 HIS T 71 ND1 96.9 REMARK 620 3 HIS T 80 ND1 116.2 80.6 REMARK 620 4 ASP T 83 OD2 154.9 59.9 54.5 REMARK 620 N 1 2 3 DBREF 8YAF A 1 153 UNP P00441 SODC_HUMAN 2 154 DBREF 8YAF B 1 118 PDB 8YAF 8YAF 1 118 DBREF 8YAF C 0 130 PDB 8YAF 8YAF 0 130 DBREF 8YAF D 1 153 UNP P00441 SODC_HUMAN 2 154 DBREF 8YAF E 1 118 PDB 8YAF 8YAF 1 118 DBREF 8YAF F 0 130 PDB 8YAF 8YAF 0 130 DBREF 8YAF H 1 153 UNP P00441 SODC_HUMAN 2 154 DBREF 8YAF I 1 118 PDB 8YAF 8YAF 1 118 DBREF 8YAF J 0 130 PDB 8YAF 8YAF 0 130 DBREF 8YAF L 1 153 UNP P00441 SODC_HUMAN 2 154 DBREF 8YAF M 1 118 PDB 8YAF 8YAF 1 118 DBREF 8YAF N 0 130 PDB 8YAF 8YAF 0 130 DBREF 8YAF P 1 153 UNP P00441 SODC_HUMAN 2 154 DBREF 8YAF Q 1 118 PDB 8YAF 8YAF 1 118 DBREF 8YAF R 0 130 PDB 8YAF 8YAF 0 130 DBREF 8YAF T 1 153 UNP P00441 SODC_HUMAN 2 154 DBREF 8YAF U 1 118 PDB 8YAF 8YAF 1 118 DBREF 8YAF V 0 130 PDB 8YAF 8YAF 0 130 SEQRES 1 A 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 A 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN SEQRES 3 A 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR SEQRES 4 A 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP SEQRES 5 A 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN SEQRES 6 A 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU SEQRES 7 A 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS SEQRES 8 A 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SEQRES 9 A 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU SEQRES 10 A 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY SEQRES 11 A 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG SEQRES 12 A 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN SEQRES 1 B 118 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 B 118 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ARG ALA SER SEQRES 3 B 118 GLU THR LEU PHE SER LEU TYR ALA MET GLY TRP TYR ARG SEQRES 4 B 118 GLN ALA PRO GLY LYS GLN PRO GLU LEU ILE ALA THR ILE SEQRES 5 B 118 SER GLY GLY GLY GLU GLY THR GLY ASN TYR ALA ASP PRO SEQRES 6 B 118 VAL LYS GLY ARG PHE THR ILE SER ARG ASN ASN ALA ASP SEQRES 7 B 118 ASN MET VAL PHE LEU GLN MET ASN ASN LEU LYS PRO GLU SEQRES 8 B 118 ASP THR ALA VAL TYR TYR CYS ASN VAL TYR GLY THR ASN SEQRES 9 B 118 LEU ALA PRO TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 B 118 SER SEQRES 1 C 131 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 C 131 GLN ALA GLY GLY SER LEU ARG LEU ALA CYS VAL ALA SER SEQRES 3 C 131 GLY GLY ASP THR ARG PRO TYR ILE THR TYR TRP MET GLY SEQRES 4 C 131 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SEQRES 5 C 131 ALA THR ILE TYR THR GLY GLY SER GLY THR TYR TYR SER SEQRES 6 C 131 ASP SER VAL GLU GLY ARG PHE THR ILE SER GLN ASP LYS SEQRES 7 C 131 ALA GLN ARG THR VAL TYR LEU GLN MET ASN ASP LEU LYS SEQRES 8 C 131 PRO GLU ASP THR ALA MET TYR TYR CYS ALA ALA GLY ASN SEQRES 9 C 131 GLY ALA LEU PRO PRO GLY ARG ARG LEU SER PRO GLN ASN SEQRES 10 C 131 MET ASP THR TRP GLY PRO GLY THR GLN VAL THR VAL SER SEQRES 11 C 131 SER SEQRES 1 D 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 D 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN SEQRES 3 D 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR SEQRES 4 D 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP SEQRES 5 D 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN SEQRES 6 D 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU SEQRES 7 D 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS SEQRES 8 D 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SEQRES 9 D 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU SEQRES 10 D 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY SEQRES 11 D 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG SEQRES 12 D 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN SEQRES 1 E 118 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 E 118 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ARG ALA SER SEQRES 3 E 118 GLU THR LEU PHE SER LEU TYR ALA MET GLY TRP TYR ARG SEQRES 4 E 118 GLN ALA PRO GLY LYS GLN PRO GLU LEU ILE ALA THR ILE SEQRES 5 E 118 SER GLY GLY GLY GLU GLY THR GLY ASN TYR ALA ASP PRO SEQRES 6 E 118 VAL LYS GLY ARG PHE THR ILE SER ARG ASN ASN ALA ASP SEQRES 7 E 118 ASN MET VAL PHE LEU GLN MET ASN ASN LEU LYS PRO GLU SEQRES 8 E 118 ASP THR ALA VAL TYR TYR CYS ASN VAL TYR GLY THR ASN SEQRES 9 E 118 LEU ALA PRO TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 E 118 SER SEQRES 1 F 131 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 F 131 GLN ALA GLY GLY SER LEU ARG LEU ALA CYS VAL ALA SER SEQRES 3 F 131 GLY GLY ASP THR ARG PRO TYR ILE THR TYR TRP MET GLY SEQRES 4 F 131 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SEQRES 5 F 131 ALA THR ILE TYR THR GLY GLY SER GLY THR TYR TYR SER SEQRES 6 F 131 ASP SER VAL GLU GLY ARG PHE THR ILE SER GLN ASP LYS SEQRES 7 F 131 ALA GLN ARG THR VAL TYR LEU GLN MET ASN ASP LEU LYS SEQRES 8 F 131 PRO GLU ASP THR ALA MET TYR TYR CYS ALA ALA GLY ASN SEQRES 9 F 131 GLY ALA LEU PRO PRO GLY ARG ARG LEU SER PRO GLN ASN SEQRES 10 F 131 MET ASP THR TRP GLY PRO GLY THR GLN VAL THR VAL SER SEQRES 11 F 131 SER SEQRES 1 H 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 H 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN SEQRES 3 H 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR SEQRES 4 H 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP SEQRES 5 H 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN SEQRES 6 H 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU SEQRES 7 H 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS SEQRES 8 H 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SEQRES 9 H 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU SEQRES 10 H 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY SEQRES 11 H 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG SEQRES 12 H 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN SEQRES 1 I 118 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 I 118 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ARG ALA SER SEQRES 3 I 118 GLU THR LEU PHE SER LEU TYR ALA MET GLY TRP TYR ARG SEQRES 4 I 118 GLN ALA PRO GLY LYS GLN PRO GLU LEU ILE ALA THR ILE SEQRES 5 I 118 SER GLY GLY GLY GLU GLY THR GLY ASN TYR ALA ASP PRO SEQRES 6 I 118 VAL LYS GLY ARG PHE THR ILE SER ARG ASN ASN ALA ASP SEQRES 7 I 118 ASN MET VAL PHE LEU GLN MET ASN ASN LEU LYS PRO GLU SEQRES 8 I 118 ASP THR ALA VAL TYR TYR CYS ASN VAL TYR GLY THR ASN SEQRES 9 I 118 LEU ALA PRO TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 I 118 SER SEQRES 1 J 131 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 J 131 GLN ALA GLY GLY SER LEU ARG LEU ALA CYS VAL ALA SER SEQRES 3 J 131 GLY GLY ASP THR ARG PRO TYR ILE THR TYR TRP MET GLY SEQRES 4 J 131 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SEQRES 5 J 131 ALA THR ILE TYR THR GLY GLY SER GLY THR TYR TYR SER SEQRES 6 J 131 ASP SER VAL GLU GLY ARG PHE THR ILE SER GLN ASP LYS SEQRES 7 J 131 ALA GLN ARG THR VAL TYR LEU GLN MET ASN ASP LEU LYS SEQRES 8 J 131 PRO GLU ASP THR ALA MET TYR TYR CYS ALA ALA GLY ASN SEQRES 9 J 131 GLY ALA LEU PRO PRO GLY ARG ARG LEU SER PRO GLN ASN SEQRES 10 J 131 MET ASP THR TRP GLY PRO GLY THR GLN VAL THR VAL SER SEQRES 11 J 131 SER SEQRES 1 L 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 L 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN SEQRES 3 L 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR SEQRES 4 L 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP SEQRES 5 L 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN SEQRES 6 L 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU SEQRES 7 L 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS SEQRES 8 L 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SEQRES 9 L 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU SEQRES 10 L 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY SEQRES 11 L 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG SEQRES 12 L 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN SEQRES 1 M 118 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 M 118 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ARG ALA SER SEQRES 3 M 118 GLU THR LEU PHE SER LEU TYR ALA MET GLY TRP TYR ARG SEQRES 4 M 118 GLN ALA PRO GLY LYS GLN PRO GLU LEU ILE ALA THR ILE SEQRES 5 M 118 SER GLY GLY GLY GLU GLY THR GLY ASN TYR ALA ASP PRO SEQRES 6 M 118 VAL LYS GLY ARG PHE THR ILE SER ARG ASN ASN ALA ASP SEQRES 7 M 118 ASN MET VAL PHE LEU GLN MET ASN ASN LEU LYS PRO GLU SEQRES 8 M 118 ASP THR ALA VAL TYR TYR CYS ASN VAL TYR GLY THR ASN SEQRES 9 M 118 LEU ALA PRO TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 M 118 SER SEQRES 1 N 131 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 N 131 GLN ALA GLY GLY SER LEU ARG LEU ALA CYS VAL ALA SER SEQRES 3 N 131 GLY GLY ASP THR ARG PRO TYR ILE THR TYR TRP MET GLY SEQRES 4 N 131 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SEQRES 5 N 131 ALA THR ILE TYR THR GLY GLY SER GLY THR TYR TYR SER SEQRES 6 N 131 ASP SER VAL GLU GLY ARG PHE THR ILE SER GLN ASP LYS SEQRES 7 N 131 ALA GLN ARG THR VAL TYR LEU GLN MET ASN ASP LEU LYS SEQRES 8 N 131 PRO GLU ASP THR ALA MET TYR TYR CYS ALA ALA GLY ASN SEQRES 9 N 131 GLY ALA LEU PRO PRO GLY ARG ARG LEU SER PRO GLN ASN SEQRES 10 N 131 MET ASP THR TRP GLY PRO GLY THR GLN VAL THR VAL SER SEQRES 11 N 131 SER SEQRES 1 P 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 P 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN SEQRES 3 P 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR SEQRES 4 P 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP SEQRES 5 P 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN SEQRES 6 P 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU SEQRES 7 P 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS SEQRES 8 P 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SEQRES 9 P 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU SEQRES 10 P 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY SEQRES 11 P 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG SEQRES 12 P 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN SEQRES 1 Q 118 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 Q 118 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ARG ALA SER SEQRES 3 Q 118 GLU THR LEU PHE SER LEU TYR ALA MET GLY TRP TYR ARG SEQRES 4 Q 118 GLN ALA PRO GLY LYS GLN PRO GLU LEU ILE ALA THR ILE SEQRES 5 Q 118 SER GLY GLY GLY GLU GLY THR GLY ASN TYR ALA ASP PRO SEQRES 6 Q 118 VAL LYS GLY ARG PHE THR ILE SER ARG ASN ASN ALA ASP SEQRES 7 Q 118 ASN MET VAL PHE LEU GLN MET ASN ASN LEU LYS PRO GLU SEQRES 8 Q 118 ASP THR ALA VAL TYR TYR CYS ASN VAL TYR GLY THR ASN SEQRES 9 Q 118 LEU ALA PRO TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 Q 118 SER SEQRES 1 R 131 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 R 131 GLN ALA GLY GLY SER LEU ARG LEU ALA CYS VAL ALA SER SEQRES 3 R 131 GLY GLY ASP THR ARG PRO TYR ILE THR TYR TRP MET GLY SEQRES 4 R 131 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SEQRES 5 R 131 ALA THR ILE TYR THR GLY GLY SER GLY THR TYR TYR SER SEQRES 6 R 131 ASP SER VAL GLU GLY ARG PHE THR ILE SER GLN ASP LYS SEQRES 7 R 131 ALA GLN ARG THR VAL TYR LEU GLN MET ASN ASP LEU LYS SEQRES 8 R 131 PRO GLU ASP THR ALA MET TYR TYR CYS ALA ALA GLY ASN SEQRES 9 R 131 GLY ALA LEU PRO PRO GLY ARG ARG LEU SER PRO GLN ASN SEQRES 10 R 131 MET ASP THR TRP GLY PRO GLY THR GLN VAL THR VAL SER SEQRES 11 R 131 SER SEQRES 1 T 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO SEQRES 2 T 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN SEQRES 3 T 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR SEQRES 4 T 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP SEQRES 5 T 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN SEQRES 6 T 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU SEQRES 7 T 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS SEQRES 8 T 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SEQRES 9 T 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU SEQRES 10 T 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY SEQRES 11 T 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG SEQRES 12 T 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN SEQRES 1 U 118 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL SEQRES 2 U 118 GLN PRO GLY GLY SER LEU ARG LEU SER CYS ARG ALA SER SEQRES 3 U 118 GLU THR LEU PHE SER LEU TYR ALA MET GLY TRP TYR ARG SEQRES 4 U 118 GLN ALA PRO GLY LYS GLN PRO GLU LEU ILE ALA THR ILE SEQRES 5 U 118 SER GLY GLY GLY GLU GLY THR GLY ASN TYR ALA ASP PRO SEQRES 6 U 118 VAL LYS GLY ARG PHE THR ILE SER ARG ASN ASN ALA ASP SEQRES 7 U 118 ASN MET VAL PHE LEU GLN MET ASN ASN LEU LYS PRO GLU SEQRES 8 U 118 ASP THR ALA VAL TYR TYR CYS ASN VAL TYR GLY THR ASN SEQRES 9 U 118 LEU ALA PRO TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 U 118 SER SEQRES 1 V 131 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 V 131 GLN ALA GLY GLY SER LEU ARG LEU ALA CYS VAL ALA SER SEQRES 3 V 131 GLY GLY ASP THR ARG PRO TYR ILE THR TYR TRP MET GLY SEQRES 4 V 131 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL SEQRES 5 V 131 ALA THR ILE TYR THR GLY GLY SER GLY THR TYR TYR SER SEQRES 6 V 131 ASP SER VAL GLU GLY ARG PHE THR ILE SER GLN ASP LYS SEQRES 7 V 131 ALA GLN ARG THR VAL TYR LEU GLN MET ASN ASP LEU LYS SEQRES 8 V 131 PRO GLU ASP THR ALA MET TYR TYR CYS ALA ALA GLY ASN SEQRES 9 V 131 GLY ALA LEU PRO PRO GLY ARG ARG LEU SER PRO GLN ASN SEQRES 10 V 131 MET ASP THR TRP GLY PRO GLY THR GLN VAL THR VAL SER SEQRES 11 V 131 SER HET ZN A 201 1 HET ZN D 201 1 HET ZN H 201 1 HET ZN L 201 1 HET ZN P 201 1 HET ZN T 201 1 HETNAM ZN ZINC ION FORMUL 19 ZN 6(ZN 2+) HELIX 1 AA1 ALA A 55 SER A 59 5 5 HELIX 2 AA2 SER A 107 CYS A 111 5 5 HELIX 3 AA3 ASN A 131 LYS A 136 5 6 HELIX 4 AA4 SER B 26 SER B 31 1 6 HELIX 5 AA5 ASN B 76 ASP B 78 5 3 HELIX 6 AA6 LYS B 89 THR B 93 5 5 HELIX 7 AA7 LYS C 77 GLN C 79 5 3 HELIX 8 AA8 LYS C 90 THR C 94 5 5 HELIX 9 AA9 SER C 113 MET C 117 5 5 HELIX 10 AB1 CYS D 57 GLY D 61 5 5 HELIX 11 AB2 SER D 107 CYS D 111 5 5 HELIX 12 AB3 ASN D 131 LYS D 136 5 6 HELIX 13 AB4 SER E 26 SER E 31 1 6 HELIX 14 AB5 LYS E 89 THR E 93 5 5 HELIX 15 AB6 LYS F 90 THR F 94 5 5 HELIX 16 AB7 ALA H 55 SER H 59 5 5 HELIX 17 AB8 SER I 26 SER I 31 1 6 HELIX 18 AB9 LYS I 89 THR I 93 5 5 HELIX 19 AC1 LYS J 77 GLN J 79 5 3 HELIX 20 AC2 LYS J 90 THR J 94 5 5 HELIX 21 AC3 SER J 113 MET J 117 5 5 HELIX 22 AC4 ALA L 55 GLY L 61 5 7 HELIX 23 AC5 ASN L 131 THR L 135 5 5 HELIX 24 AC6 SER M 26 SER M 31 1 6 HELIX 25 AC7 ASP M 64 LYS M 67 5 4 HELIX 26 AC8 LYS M 89 THR M 93 5 5 HELIX 27 AC9 LYS N 77 GLN N 79 5 3 HELIX 28 AD1 LYS N 90 THR N 94 5 5 HELIX 29 AD2 GLY N 109 MET N 117 5 9 HELIX 30 AD3 ALA P 55 GLY P 61 5 7 HELIX 31 AD4 ASN P 131 GLY P 138 1 8 HELIX 32 AD5 SER Q 26 SER Q 31 1 6 HELIX 33 AD6 ASP Q 64 LYS Q 67 5 4 HELIX 34 AD7 LYS Q 89 THR Q 93 5 5 HELIX 35 AD8 LYS R 90 THR R 94 5 5 HELIX 36 AD9 SER R 113 GLN R 115 5 3 HELIX 37 AE1 ALA T 55 GLY T 61 5 7 HELIX 38 AE2 SER T 107 CYS T 111 5 5 HELIX 39 AE3 ASN T 131 THR T 135 5 5 HELIX 40 AE4 SER U 26 SER U 31 1 6 HELIX 41 AE5 ASP U 64 LYS U 67 5 4 HELIX 42 AE6 LYS U 89 THR U 93 5 5 HELIX 43 AE7 LYS V 77 GLN V 79 5 3 HELIX 44 AE8 LYS V 90 THR V 94 5 5 HELIX 45 AE9 SER V 113 GLN V 115 5 3 SHEET 1 AA1 3 VAL A 94 ALA A 95 0 SHEET 2 AA1 3 VAL A 29 LYS A 36 -1 N ILE A 35 O ALA A 95 SHEET 3 AA1 3 SER A 98 ASP A 101 -1 O ILE A 99 N VAL A 31 SHEET 1 AA2 5 VAL A 94 ALA A 95 0 SHEET 2 AA2 5 VAL A 29 LYS A 36 -1 N ILE A 35 O ALA A 95 SHEET 3 AA2 5 GLN A 15 GLN A 22 -1 N ASN A 19 O TRP A 32 SHEET 4 AA2 5 THR A 2 LEU A 8 -1 N LEU A 8 O GLY A 16 SHEET 5 AA2 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5 SHEET 1 AA3 4 ASP A 83 ALA A 89 0 SHEET 2 AA3 4 GLY A 41 HIS A 48 -1 N PHE A 45 O GLY A 85 SHEET 3 AA3 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48 SHEET 4 AA3 4 ARG A 143 VAL A 148 -1 O LEU A 144 N VAL A 119 SHEET 1 AA4 4 LEU B 5 SER B 8 0 SHEET 2 AA4 4 LEU B 19 ALA B 25 -1 O SER B 22 N SER B 8 SHEET 3 AA4 4 MET B 80 MET B 85 -1 O LEU B 83 N LEU B 21 SHEET 4 AA4 4 PHE B 70 ASN B 75 -1 N THR B 71 O GLN B 84 SHEET 1 AA512 THR B 59 TYR B 62 0 SHEET 2 AA512 GLU B 47 SER B 53 -1 N THR B 51 O ASN B 61 SHEET 3 AA512 ALA B 34 GLN B 40 -1 N TRP B 37 O ALA B 50 SHEET 4 AA512 ALA B 94 VAL B 100 -1 O ASN B 99 N GLY B 36 SHEET 5 AA512 THR B 112 VAL B 116 -1 O VAL B 114 N ALA B 94 SHEET 6 AA512 GLY B 11 VAL B 13 1 N VAL B 13 O THR B 115 SHEET 7 AA512 GLY E 11 VAL E 13 -1 O LEU E 12 N LEU B 12 SHEET 8 AA512 THR E 112 VAL E 116 1 O THR E 115 N GLY E 11 SHEET 9 AA512 ALA E 94 VAL E 100 -1 N TYR E 96 O THR E 112 SHEET 10 AA512 ALA E 34 GLN E 40 -1 N TYR E 38 O TYR E 97 SHEET 11 AA512 GLU E 47 SER E 53 -1 O ILE E 49 N TRP E 37 SHEET 12 AA512 THR E 59 TYR E 62 -1 O THR E 59 N SER E 53 SHEET 1 AA6 4 GLN C 3 SER C 7 0 SHEET 2 AA6 4 SER C 17 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AA6 4 THR C 81 ASN C 87 -1 O MET C 86 N LEU C 18 SHEET 4 AA6 4 PHE C 71 ASP C 76 -1 N ASP C 76 O THR C 81 SHEET 1 AA7 6 SER C 11 GLN C 13 0 SHEET 2 AA7 6 THR C 124 SER C 129 1 O SER C 129 N VAL C 12 SHEET 3 AA7 6 ALA C 95 ALA C 101 -1 N TYR C 97 O THR C 124 SHEET 4 AA7 6 TRP C 36 GLN C 42 -1 N TYR C 40 O TYR C 98 SHEET 5 AA7 6 ALA C 52 TYR C 55 -1 O ALA C 52 N TRP C 39 SHEET 6 AA7 6 THR C 61 TYR C 63 -1 O TYR C 62 N THR C 53 SHEET 1 AA8 4 SER C 11 GLN C 13 0 SHEET 2 AA8 4 THR C 124 SER C 129 1 O SER C 129 N VAL C 12 SHEET 3 AA8 4 ALA C 95 ALA C 101 -1 N TYR C 97 O THR C 124 SHEET 4 AA8 4 THR C 119 TRP C 120 -1 O THR C 119 N ALA C 101 SHEET 1 AA9 8 ASP D 83 ALA D 89 0 SHEET 2 AA9 8 GLY D 41 HIS D 48 -1 N GLY D 41 O ALA D 89 SHEET 3 AA9 8 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48 SHEET 4 AA9 8 ARG D 143 VAL D 148 -1 O GLY D 147 N LEU D 117 SHEET 5 AA9 8 THR D 2 GLY D 10 -1 N LYS D 9 O CYS D 146 SHEET 6 AA9 8 GLN D 15 GLN D 22 -1 O GLY D 16 N LEU D 8 SHEET 7 AA9 8 VAL D 29 LYS D 36 -1 O LYS D 30 N GLU D 21 SHEET 8 AA9 8 SER D 98 ASP D 101 -1 O ILE D 99 N VAL D 31 SHEET 1 AB1 5 VAL D 94 ALA D 95 0 SHEET 2 AB1 5 VAL D 29 LYS D 36 -1 N ILE D 35 O ALA D 95 SHEET 3 AB1 5 GLN D 15 GLN D 22 -1 N GLU D 21 O LYS D 30 SHEET 4 AB1 5 THR D 2 GLY D 10 -1 N LEU D 8 O GLY D 16 SHEET 5 AB1 5 GLY D 150 GLN D 153 -1 O GLY D 150 N VAL D 5 SHEET 1 AB2 4 LEU E 5 SER E 8 0 SHEET 2 AB2 4 LEU E 19 ALA E 25 -1 O ARG E 24 N GLN E 6 SHEET 3 AB2 4 MET E 80 MET E 85 -1 O LEU E 83 N LEU E 21 SHEET 4 AB2 4 PHE E 70 ASN E 75 -1 N SER E 73 O PHE E 82 SHEET 1 AB3 2 VAL F 2 GLN F 3 0 SHEET 2 AB3 2 SER F 25 GLY F 26 -1 O SER F 25 N GLN F 3 SHEET 1 AB4 4 GLU F 6 SER F 7 0 SHEET 2 AB4 4 SER F 17 VAL F 23 -1 O ALA F 21 N SER F 7 SHEET 3 AB4 4 THR F 81 ASN F 87 -1 O LEU F 84 N LEU F 20 SHEET 4 AB4 4 PHE F 71 ASP F 76 -1 N THR F 72 O GLN F 85 SHEET 1 AB5 6 SER F 11 GLN F 13 0 SHEET 2 AB5 6 THR F 124 SER F 129 1 O SER F 129 N VAL F 12 SHEET 3 AB5 6 ALA F 95 ASN F 103 -1 N TYR F 97 O THR F 124 SHEET 4 AB5 6 TYR F 35 GLN F 42 -1 N TYR F 40 O TYR F 98 SHEET 5 AB5 6 ALA F 52 TYR F 55 -1 O ILE F 54 N MET F 37 SHEET 6 AB5 6 THR F 61 TYR F 63 -1 O TYR F 62 N THR F 53 SHEET 1 AB6 4 SER F 11 GLN F 13 0 SHEET 2 AB6 4 THR F 124 SER F 129 1 O SER F 129 N VAL F 12 SHEET 3 AB6 4 ALA F 95 ASN F 103 -1 N TYR F 97 O THR F 124 SHEET 4 AB6 4 MET F 117 TRP F 120 -1 O THR F 119 N ALA F 101 SHEET 1 AB7 5 ALA H 95 ASP H 101 0 SHEET 2 AB7 5 VAL H 29 LYS H 36 -1 N VAL H 29 O ASP H 101 SHEET 3 AB7 5 GLN H 15 GLN H 22 -1 N ASN H 19 O TRP H 32 SHEET 4 AB7 5 THR H 2 LEU H 8 -1 N ALA H 4 O PHE H 20 SHEET 5 AB7 5 GLY H 150 GLN H 153 -1 O GLY H 150 N VAL H 5 SHEET 1 AB8 4 ASP H 83 ALA H 89 0 SHEET 2 AB8 4 GLY H 41 HIS H 48 -1 N GLY H 41 O ALA H 89 SHEET 3 AB8 4 THR H 116 HIS H 120 -1 O HIS H 120 N GLY H 44 SHEET 4 AB8 4 ARG H 143 VAL H 148 -1 O GLY H 147 N LEU H 117 SHEET 1 AB9 4 LEU I 5 SER I 8 0 SHEET 2 AB9 4 LEU I 19 ALA I 25 -1 O SER I 22 N SER I 8 SHEET 3 AB9 4 MET I 80 MET I 85 -1 O LEU I 83 N LEU I 21 SHEET 4 AB9 4 PHE I 70 ASN I 75 -1 N ASN I 75 O MET I 80 SHEET 1 AC1 6 LEU I 12 VAL I 13 0 SHEET 2 AC1 6 THR I 112 VAL I 116 1 O THR I 115 N VAL I 13 SHEET 3 AC1 6 ALA I 94 VAL I 100 -1 N ALA I 94 O VAL I 114 SHEET 4 AC1 6 ALA I 34 GLN I 40 -1 N TYR I 38 O TYR I 97 SHEET 5 AC1 6 GLU I 47 SER I 53 -1 O ALA I 50 N TRP I 37 SHEET 6 AC1 6 THR I 59 TYR I 62 -1 O ASN I 61 N THR I 51 SHEET 1 AC2 4 VAL J 2 SER J 7 0 SHEET 2 AC2 4 SER J 17 GLY J 26 -1 O SER J 25 N GLN J 3 SHEET 3 AC2 4 THR J 81 ASN J 87 -1 O LEU J 84 N LEU J 20 SHEET 4 AC2 4 PHE J 71 ASP J 76 -1 N THR J 72 O GLN J 85 SHEET 1 AC3 6 GLY J 10 GLN J 13 0 SHEET 2 AC3 6 THR J 124 SER J 129 1 O SER J 129 N VAL J 12 SHEET 3 AC3 6 ALA J 95 ALA J 101 -1 N TYR J 97 O THR J 124 SHEET 4 AC3 6 TRP J 36 GLN J 42 -1 N TYR J 40 O TYR J 98 SHEET 5 AC3 6 ALA J 52 TYR J 55 -1 O ALA J 52 N TRP J 39 SHEET 6 AC3 6 THR J 61 TYR J 63 -1 O TYR J 62 N THR J 53 SHEET 1 AC4 4 GLY J 10 GLN J 13 0 SHEET 2 AC4 4 THR J 124 SER J 129 1 O SER J 129 N VAL J 12 SHEET 3 AC4 4 ALA J 95 ALA J 101 -1 N TYR J 97 O THR J 124 SHEET 4 AC4 4 THR J 119 TRP J 120 -1 O THR J 119 N ALA J 101 SHEET 1 AC5 5 ALA L 95 ASP L 101 0 SHEET 2 AC5 5 VAL L 29 LYS L 36 -1 N VAL L 29 O ASP L 101 SHEET 3 AC5 5 GLN L 15 GLN L 22 -1 N ASN L 19 O TRP L 32 SHEET 4 AC5 5 THR L 2 LEU L 8 -1 N ALA L 4 O PHE L 20 SHEET 5 AC5 5 GLY L 150 GLN L 153 -1 O GLY L 150 N VAL L 5 SHEET 1 AC6 4 ASP L 83 ALA L 89 0 SHEET 2 AC6 4 GLY L 41 HIS L 48 -1 N HIS L 43 O VAL L 87 SHEET 3 AC6 4 THR L 116 HIS L 120 -1 O THR L 116 N HIS L 48 SHEET 4 AC6 4 ARG L 143 VAL L 148 -1 O ALA L 145 N VAL L 119 SHEET 1 AC7 4 LEU M 5 SER M 8 0 SHEET 2 AC7 4 LEU M 19 ALA M 25 -1 O ARG M 24 N GLN M 6 SHEET 3 AC7 4 MET M 80 MET M 85 -1 O MET M 85 N LEU M 19 SHEET 4 AC7 4 PHE M 70 ASN M 75 -1 N ASN M 75 O MET M 80 SHEET 1 AC812 THR M 59 TYR M 62 0 SHEET 2 AC812 GLU M 47 SER M 53 -1 N THR M 51 O ASN M 61 SHEET 3 AC812 ALA M 34 GLN M 40 -1 N TRP M 37 O ALA M 50 SHEET 4 AC812 ALA M 94 VAL M 100 -1 O ASN M 99 N GLY M 36 SHEET 5 AC812 GLN M 113 VAL M 116 -1 O VAL M 114 N ALA M 94 SHEET 6 AC812 GLY M 11 VAL M 13 1 N GLY M 11 O THR M 115 SHEET 7 AC812 GLY U 11 VAL U 13 -1 O LEU U 12 N LEU M 12 SHEET 8 AC812 THR U 112 VAL U 116 1 O THR U 115 N GLY U 11 SHEET 9 AC812 ALA U 94 VAL U 100 -1 N TYR U 96 O THR U 112 SHEET 10 AC812 ALA U 34 GLN U 40 -1 N TYR U 38 O TYR U 97 SHEET 11 AC812 GLU U 47 SER U 53 -1 O ILE U 49 N TRP U 37 SHEET 12 AC812 THR U 59 TYR U 62 -1 O THR U 59 N SER U 53 SHEET 1 AC9 4 GLU N 6 SER N 7 0 SHEET 2 AC9 4 ARG N 19 VAL N 23 -1 O ALA N 21 N SER N 7 SHEET 3 AC9 4 THR N 81 MET N 86 -1 O LEU N 84 N LEU N 20 SHEET 4 AC9 4 PHE N 71 ASP N 76 -1 N THR N 72 O GLN N 85 SHEET 1 AD1 6 SER N 11 GLN N 13 0 SHEET 2 AD1 6 THR N 124 SER N 129 1 O SER N 129 N VAL N 12 SHEET 3 AD1 6 ALA N 95 ASN N 103 -1 N TYR N 97 O THR N 124 SHEET 4 AD1 6 TYR N 35 GLN N 42 -1 N TYR N 40 O TYR N 98 SHEET 5 AD1 6 ALA N 52 TYR N 55 -1 O ILE N 54 N MET N 37 SHEET 6 AD1 6 THR N 61 TYR N 63 -1 O TYR N 62 N THR N 53 SHEET 1 AD2 4 SER N 11 GLN N 13 0 SHEET 2 AD2 4 THR N 124 SER N 129 1 O SER N 129 N VAL N 12 SHEET 3 AD2 4 ALA N 95 ASN N 103 -1 N TYR N 97 O THR N 124 SHEET 4 AD2 4 THR N 119 TRP N 120 -1 O THR N 119 N ALA N 101 SHEET 1 AD3 9 LYS P 3 LYS P 9 0 SHEET 2 AD3 9 GLN P 15 GLU P 21 -1 O GLY P 16 N LEU P 8 SHEET 3 AD3 9 VAL P 29 LYS P 36 -1 O TRP P 32 N ASN P 19 SHEET 4 AD3 9 ALA P 95 ASP P 101 -1 O ASP P 101 N VAL P 29 SHEET 5 AD3 9 ASP P 83 ALA P 89 -1 N THR P 88 O ASP P 96 SHEET 6 AD3 9 GLY P 41 HIS P 48 -1 N GLY P 41 O ALA P 89 SHEET 7 AD3 9 THR P 116 HIS P 120 -1 O HIS P 120 N GLY P 44 SHEET 8 AD3 9 ARG P 143 GLN P 153 -1 O GLY P 147 N LEU P 117 SHEET 9 AD3 9 LYS P 3 LYS P 9 -1 N VAL P 5 O GLY P 150 SHEET 1 AD4 4 LEU Q 5 SER Q 8 0 SHEET 2 AD4 4 LEU Q 19 ALA Q 25 -1 O SER Q 22 N SER Q 8 SHEET 3 AD4 4 MET Q 80 MET Q 85 -1 O MET Q 85 N LEU Q 19 SHEET 4 AD4 4 PHE Q 70 ASN Q 75 -1 N THR Q 71 O GLN Q 84 SHEET 1 AD5 6 LEU Q 12 VAL Q 13 0 SHEET 2 AD5 6 GLN Q 113 VAL Q 116 1 O THR Q 115 N VAL Q 13 SHEET 3 AD5 6 ALA Q 94 VAL Q 100 -1 N ALA Q 94 O VAL Q 114 SHEET 4 AD5 6 ALA Q 34 GLN Q 40 -1 N TYR Q 38 O TYR Q 97 SHEET 5 AD5 6 GLU Q 47 SER Q 53 -1 O ILE Q 49 N TRP Q 37 SHEET 6 AD5 6 THR Q 59 TYR Q 62 -1 O THR Q 59 N SER Q 53 SHEET 1 AD6 4 GLN R 3 SER R 7 0 SHEET 2 AD6 4 SER R 17 SER R 25 -1 O SER R 25 N GLN R 3 SHEET 3 AD6 4 THR R 81 ASN R 87 -1 O LEU R 84 N LEU R 20 SHEET 4 AD6 4 PHE R 71 ASP R 76 -1 N ASP R 76 O THR R 81 SHEET 1 AD7 6 SER R 11 GLN R 13 0 SHEET 2 AD7 6 THR R 124 SER R 129 1 O SER R 129 N VAL R 12 SHEET 3 AD7 6 ALA R 95 ASN R 103 -1 N TYR R 97 O THR R 124 SHEET 4 AD7 6 TYR R 35 GLN R 42 -1 N TYR R 40 O TYR R 98 SHEET 5 AD7 6 ALA R 52 TYR R 55 -1 O ALA R 52 N TRP R 39 SHEET 6 AD7 6 THR R 61 TYR R 63 -1 O TYR R 62 N THR R 53 SHEET 1 AD8 4 SER R 11 GLN R 13 0 SHEET 2 AD8 4 THR R 124 SER R 129 1 O SER R 129 N VAL R 12 SHEET 3 AD8 4 ALA R 95 ASN R 103 -1 N TYR R 97 O THR R 124 SHEET 4 AD8 4 MET R 117 TRP R 120 -1 O THR R 119 N ALA R 101 SHEET 1 AD9 5 ALA T 95 ASP T 101 0 SHEET 2 AD9 5 VAL T 29 LYS T 36 -1 N VAL T 31 O ILE T 99 SHEET 3 AD9 5 GLN T 15 GLN T 22 -1 N ASN T 19 O TRP T 32 SHEET 4 AD9 5 THR T 2 LYS T 9 -1 N LEU T 8 O GLY T 16 SHEET 5 AD9 5 GLY T 150 GLN T 153 -1 O ALA T 152 N LYS T 3 SHEET 1 AE1 4 ASP T 83 ALA T 89 0 SHEET 2 AE1 4 GLY T 41 HIS T 48 -1 N PHE T 45 O GLY T 85 SHEET 3 AE1 4 THR T 116 HIS T 120 -1 O THR T 116 N HIS T 48 SHEET 4 AE1 4 ARG T 143 VAL T 148 -1 O GLY T 147 N LEU T 117 SHEET 1 AE2 4 LEU U 5 SER U 8 0 SHEET 2 AE2 4 LEU U 19 ALA U 25 -1 O SER U 22 N SER U 8 SHEET 3 AE2 4 MET U 80 MET U 85 -1 O VAL U 81 N CYS U 23 SHEET 4 AE2 4 PHE U 70 ASN U 75 -1 N SER U 73 O PHE U 82 SHEET 1 AE3 4 GLN V 3 SER V 7 0 SHEET 2 AE3 4 ARG V 19 SER V 25 -1 O SER V 25 N GLN V 3 SHEET 3 AE3 4 THR V 81 MET V 86 -1 O VAL V 82 N CYS V 22 SHEET 4 AE3 4 PHE V 71 ASP V 76 -1 N ASP V 76 O THR V 81 SHEET 1 AE4 6 SER V 11 GLN V 13 0 SHEET 2 AE4 6 THR V 124 SER V 129 1 O SER V 129 N VAL V 12 SHEET 3 AE4 6 ALA V 95 GLY V 102 -1 N TYR V 97 O THR V 124 SHEET 4 AE4 6 TRP V 36 GLN V 42 -1 N TYR V 40 O TYR V 98 SHEET 5 AE4 6 ALA V 52 TYR V 55 -1 O ALA V 52 N TRP V 39 SHEET 6 AE4 6 THR V 61 TYR V 63 -1 O TYR V 62 N THR V 53 SHEET 1 AE5 4 SER V 11 GLN V 13 0 SHEET 2 AE5 4 THR V 124 SER V 129 1 O SER V 129 N VAL V 12 SHEET 3 AE5 4 ALA V 95 GLY V 102 -1 N TYR V 97 O THR V 124 SHEET 4 AE5 4 MET V 117 TRP V 120 -1 O ASP V 118 N ALA V 101 SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.08 SSBOND 2 CYS D 57 CYS D 146 1555 1555 2.06 SSBOND 3 CYS H 57 CYS H 146 1555 1555 2.09 SSBOND 4 CYS L 57 CYS L 146 1555 1555 2.09 SSBOND 5 CYS P 57 CYS P 146 1555 1555 2.07 SSBOND 6 CYS T 57 CYS T 146 1555 1555 2.08 LINK ND1 HIS A 63 ZN ZN A 201 1555 1555 2.16 LINK ND1 HIS A 71 ZN ZN A 201 1555 1555 2.20 LINK ND1 HIS A 80 ZN ZN A 201 1555 1555 2.21 LINK OD2 ASP A 83 ZN ZN A 201 1555 1555 1.95 LINK ND1 HIS D 63 ZN ZN D 201 1555 1555 2.30 LINK ND1 HIS D 71 ZN ZN D 201 1555 1555 2.30 LINK ND1 HIS D 80 ZN ZN D 201 1555 1555 2.30 LINK OD2 ASP D 83 ZN ZN D 201 1555 1555 2.62 LINK O LYS D 136 ZN ZN D 201 1555 1555 1.87 LINK ND1 HIS H 63 ZN ZN H 201 1555 1555 2.14 LINK ND1 HIS H 71 ZN ZN H 201 1555 1555 2.39 LINK ND1 HIS H 80 ZN ZN H 201 1555 1555 2.14 LINK ND1 HIS L 63 ZN ZN L 201 1555 1555 2.11 LINK ND1 HIS L 71 ZN ZN L 201 1555 1555 2.17 LINK ND1 HIS L 80 ZN ZN L 201 1555 1555 2.14 LINK OD2 ASP L 83 ZN ZN L 201 1555 1555 1.70 LINK ND1 HIS P 63 ZN ZN P 201 1555 1555 2.35 LINK NE2 HIS P 63 ZN ZN P 201 1555 1555 1.93 LINK ND1 HIS P 71 ZN ZN P 201 1555 1555 2.36 LINK ND1 HIS P 80 ZN ZN P 201 1555 1555 2.32 LINK ND1 HIS T 63 ZN ZN T 201 1555 1555 2.17 LINK ND1 HIS T 71 ZN ZN T 201 1555 1555 2.28 LINK ND1 HIS T 80 ZN ZN T 201 1555 1555 2.21 LINK OD2 ASP T 83 ZN ZN T 201 1555 1555 1.83 CRYST1 139.949 218.892 122.708 90.00 90.00 90.00 P 21 21 2 24 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 0.007145 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004568 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008149 0.00000