HEADER TOXIN 11-JUN-25 9RIU TITLE CO-CRYSTAL OF BROADLY NEUTRALIZING VHH IN COMPLEX WITH SHORT TITLE 2 NEUROTOXIN 1 (P01426) NAJA PALLIDA COMPND MOL_ID: 1; COMPND 2 MOLECULE: VARIABLE DOMAIN OF HEAVY-CHAIN ONLY ANTIBODY (VHH); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: PROTEIN. VARIABLE DOMAIN OF HEAVY-CHAIN ONLY ANTIBODY COMPND 6 (VHH); COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: SHORT NEUROTOXIN 1; COMPND 9 CHAIN: B, D; COMPND 10 SYNONYM: NEUROTOXIN ALPHA,TOXIN ALPHA; COMPND 11 OTHER_DETAILS: SHORT NEUROTOXIN 1 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_TAXID: 30538; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: NAJA PALLIDA; SOURCE 8 ORGANISM_COMMON: RED SPITTING COBRA; SOURCE 9 ORGANISM_TAXID: 8658 KEYWDS NANOBODY, VHH, ANTIBODY, TOXIN, SNAKE TOXIN, SNAKE VENOM, KEYWDS 2 NEUTRALIZING EXPDTA X-RAY DIFFRACTION AUTHOR N.J.BURLET,A.H.LAUSTSEN,J.P.MORTH REVDAT 1 05-NOV-25 9RIU 0 JRNL AUTH S.AHMADHI,N.J.BURLET,M.BENARD-VALLE,A.GUADARRAMA-MARTINEZ, JRNL AUTH 2 S.KERWIN,S.K.MENZIES,I.A.CARDOSO,A.MARRIOTT,R.EDGE, JRNL AUTH 3 E.CRITTENDEN,E.NERI,G.T.T.NGUYEN,C.O'BRIEN,Y.WOUTERS, JRNL AUTH 4 K.KALOGEROPOULOS,S.THUMTECHO,T.W.EBERSOLE,C.H.DAHL, JRNL AUTH 5 E.U.GLEGG-SORENSEN,T.JANSEN,K.BODDUM,E.MANOUSAKI, JRNL AUTH 6 E.RIVERA-DE-TORRE,J.P.MORTH,A.ALAGON,T.P.JENKINS, JRNL AUTH 7 S.P.MACKESSY,S.AINSWORTH,N.CASEWELL,A.LJUNGARS,A.H.LAUSTSEN JRNL TITL NANOBODY-BASED RECOMBINANT ANTIVENOM FOR COBRA, MAMBA, AND JRNL TITL 2 RINKHALS BITES JRNL REF TO BE PUBLISHED 2025 JRNL REFN JRNL DOI 10.1038/S41586-025-09661-0 REMARK 2 REMARK 2 RESOLUTION. 2.50 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 15225 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.326 REMARK 3 R VALUE (WORKING SET) : 0.324 REMARK 3 FREE R VALUE : 0.361 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 760 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 23.2900 - 4.2700 1.00 2997 157 0.2771 0.3243 REMARK 3 2 4.2700 - 3.3900 1.00 2898 152 0.3159 0.3587 REMARK 3 3 3.3900 - 2.9600 1.00 2861 151 0.3925 0.4157 REMARK 3 4 2.9600 - 2.6900 1.00 2868 150 0.4106 0.3878 REMARK 3 5 2.6900 - 2.5000 1.00 2841 150 0.4406 0.4955 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) : 0.596 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 47.276 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.01 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 : 0.005 2902 REMARK 3 ANGLE : 0.891 3932 REMARK 3 CHIRALITY : 0.060 430 REMARK 3 PLANARITY : 0.006 524 REMARK 3 DIHEDRAL : 5.613 406 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 : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "C" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "D" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9RIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1292148328. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-FEB-25 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MAX IV REMARK 200 BEAMLINE : BIOMAX REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.72931 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 REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28844 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 23.290 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.150 REMARK 200 R MERGE (I) : 0.05600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.8600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.22 REMARK 200 R MERGE FOR SHELL (I) : 0.49800 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 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.62 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M SODIUM REMARK 280 ACETATE, PH 4.6, 30% V/V MPD. 25% (V/V) GLYCEROL AS REMARK 280 CRYPRESERVATIVE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 39.67000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.67000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 52.07500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.04500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 52.07500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.04500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.67000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 52.07500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.04500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.67000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 52.07500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 52.04500 REMARK 290 SMTRY3 8 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 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 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 NI NI C 203 LIES ON A SPECIAL POSITION. 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 PHE A 128 REMARK 465 GLN A 129 REMARK 465 PHE C 128 REMARK 465 GLN C 129 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 H GLU B 2 OD1 ASP B 57 1.56 REMARK 500 OD2 ASP C 50 NI NI C 201 1.66 REMARK 500 OD2 ASP C 59 O HOH C 301 1.69 REMARK 500 NI NI C 203 O HOH C 301 1.69 REMARK 500 O HOH A 309 O HOH D 201 1.97 REMARK 500 OE1 GLU B 20 O HOH B 201 1.98 REMARK 500 OD1 ASN D 5 OG1 THR D 13 1.98 REMARK 500 OD1 ASN B 5 OG1 THR B 13 2.04 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 NI NI A 201 NI NI A 201 4555 1.13 REMARK 500 HA3 GLY A 46 HD3 ARG D 29 6555 1.21 REMARK 500 OD2 ASP B 57 O HOH C 301 6555 1.89 REMARK 500 OD1 ASN C 34 OD1 ASN C 34 3654 2.11 REMARK 500 OD2 ASP C 59 OD2 ASP C 59 3654 2.16 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 LEU A 4 CB - CG - CD1 ANGL. DEV. = 15.5 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 LEU A 18 139.03 -174.68 REMARK 500 GLN A 43 39.18 -95.90 REMARK 500 ASP A 44 -147.26 63.54 REMARK 500 THR A 47 152.37 68.34 REMARK 500 ASP A 77 79.57 -118.70 REMARK 500 ASN A 81 63.76 61.27 REMARK 500 TYR A 110 97.06 -66.23 REMARK 500 SER A 122 -38.91 -152.20 REMARK 500 ASN B 5 -9.95 -148.05 REMARK 500 SER B 8 -131.73 56.15 REMARK 500 SER B 9 36.26 -99.31 REMARK 500 ASP B 30 175.75 66.09 REMARK 500 ARG B 32 41.46 -98.17 REMARK 500 ASN B 60 53.06 -91.10 REMARK 500 LEU C 18 138.93 -174.54 REMARK 500 VAL C 27 36.64 38.48 REMARK 500 SER C 30 32.84 70.57 REMARK 500 ILE C 31 51.62 -117.58 REMARK 500 GLN C 43 38.59 -95.20 REMARK 500 ASP C 44 -147.46 63.14 REMARK 500 THR C 47 151.33 68.36 REMARK 500 ASP C 77 78.29 -119.39 REMARK 500 TYR C 110 97.08 -66.16 REMARK 500 SER C 122 -39.14 -152.43 REMARK 500 ASN D 5 -10.99 -147.52 REMARK 500 SER D 8 -131.20 56.86 REMARK 500 SER D 9 36.98 -96.42 REMARK 500 ASP D 30 173.26 60.97 REMARK 500 ARG D 32 42.50 -99.24 REMARK 500 LYS D 46 -172.32 -68.76 REMARK 500 ASN D 60 56.61 -93.11 REMARK 500 REMARK 500 REMARK: NULL 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 NI A 203 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 50 OD2 REMARK 620 2 HIS D 31 NE2 92.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI A 201 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 59 OD1 REMARK 620 2 ASP A 59 OD2 56.3 REMARK 620 3 ASP A 59 OD2 56.3 0.0 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI A 206 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 60 OE2 REMARK 620 2 HOH A 303 O 64.6 REMARK 620 3 HOH A 309 O 117.1 167.4 REMARK 620 4 HOH A 312 O 121.3 77.6 91.9 REMARK 620 5 HOH A 313 O 113.6 75.1 113.3 96.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI D 101 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 60 OE1 REMARK 620 2 HIS D 4 NE2 117.0 REMARK 620 3 ASN D 61 OD1 99.3 100.1 REMARK 620 4 HOH D 201 O 128.3 100.9 107.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI A 202 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 93 OE1 REMARK 620 2 HOH A 311 O 113.8 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI A 205 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 57 OD2 REMARK 620 2 HOH D 203 O 78.7 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI B 101 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 4 NE2 REMARK 620 2 ASN B 61 ND2 76.7 REMARK 620 3 HOH B 203 O 92.8 71.4 REMARK 620 4 GLU C 60 OE1 47.4 37.6 59.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI C 201 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 31 ND1 REMARK 620 2 HIS B 31 NE2 50.2 REMARK 620 3 THR C 47 OG1 104.7 118.1 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI B 102 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 57 OD2 REMARK 620 2 HOH B 205 O 87.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI C 203 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH B 205 O REMARK 620 2 ASP C 59 OD2 110.5 REMARK 620 3 ASP C 59 OD2 110.5 0.0 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI C 202 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 60 OE2 REMARK 620 2 HOH C 307 O 87.4 REMARK 620 3 HOH C 311 O 109.8 77.7 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NI D 102 NI REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU D 20 OE1 REMARK 620 2 GLU D 20 OE2 56.5 REMARK 620 N 1 DBREF 9RIU A 1 129 PDB 9RIU 9RIU 1 129 DBREF 9RIU B 1 61 UNP P01426 3S11_NAJPA 1 61 DBREF 9RIU C 1 129 PDB 9RIU 9RIU 1 129 DBREF 9RIU D 1 61 UNP P01426 3S11_NAJPA 1 61 SEQRES 1 A 129 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL ARG SEQRES 2 A 129 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 A 129 VAL SER GLU SER ILE PHE ALA ASN TYR VAL VAL GLY TRP SEQRES 4 A 129 PHE ARG GLN GLN ASP SER GLY THR GLY ARG ASP LEU VAL SEQRES 5 A 129 ALA GLN SER SER SER ASP ASP GLU TYR ASN HIS VAL SER SEQRES 6 A 129 GLY SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7 A 129 ALA LYS ASN THR VAL SER LEU GLN MET ASP ASN LEU LYS SEQRES 8 A 129 PRO GLU ASP THR ALA ILE TYR ILE CYS ALA ALA ALA ILE SEQRES 9 A 129 GLY PRO GLY ASP ASN TYR ILE TYR TRP GLY GLN GLY THR SEQRES 10 A 129 GLN VAL THR VAL SER SER GLU ASN LEU TYR PHE GLN SEQRES 1 B 61 LEU GLU CYS HIS ASN GLN GLN SER SER GLN PRO PRO THR SEQRES 2 B 61 THR LYS THR CYS PRO GLY GLU THR ASN CYS TYR LYS LYS SEQRES 3 B 61 VAL TRP ARG ASP HIS ARG GLY THR ILE ILE GLU ARG GLY SEQRES 4 B 61 CYS GLY CYS PRO THR VAL LYS PRO GLY ILE LYS LEU ASN SEQRES 5 B 61 CYS CYS THR THR ASP LYS CYS ASN ASN SEQRES 1 C 129 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL ARG SEQRES 2 C 129 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 C 129 VAL SER GLU SER ILE PHE ALA ASN TYR VAL VAL GLY TRP SEQRES 4 C 129 PHE ARG GLN GLN ASP SER GLY THR GLY ARG ASP LEU VAL SEQRES 5 C 129 ALA GLN SER SER SER ASP ASP GLU TYR ASN HIS VAL SER SEQRES 6 C 129 GLY SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7 C 129 ALA LYS ASN THR VAL SER LEU GLN MET ASP ASN LEU LYS SEQRES 8 C 129 PRO GLU ASP THR ALA ILE TYR ILE CYS ALA ALA ALA ILE SEQRES 9 C 129 GLY PRO GLY ASP ASN TYR ILE TYR TRP GLY GLN GLY THR SEQRES 10 C 129 GLN VAL THR VAL SER SER GLU ASN LEU TYR PHE GLN SEQRES 1 D 61 LEU GLU CYS HIS ASN GLN GLN SER SER GLN PRO PRO THR SEQRES 2 D 61 THR LYS THR CYS PRO GLY GLU THR ASN CYS TYR LYS LYS SEQRES 3 D 61 VAL TRP ARG ASP HIS ARG GLY THR ILE ILE GLU ARG GLY SEQRES 4 D 61 CYS GLY CYS PRO THR VAL LYS PRO GLY ILE LYS LEU ASN SEQRES 5 D 61 CYS CYS THR THR ASP LYS CYS ASN ASN HET NI A 201 1 HET NI A 202 1 HET NI A 203 1 HET NI A 204 1 HET NI A 205 1 HET NI A 206 1 HET NI B 101 1 HET NI B 102 1 HET NI B 103 1 HET NI C 201 1 HET NI C 202 1 HET NI C 203 1 HET NI C 204 1 HET NI C 205 1 HET NI D 101 1 HET NI D 102 1 HETNAM NI NICKEL (II) ION FORMUL 5 NI 16(NI 2+) FORMUL 21 HOH *35(H2 O) HELIX 1 AA1 ASP A 58 ASN A 62 5 5 HELIX 2 AA2 LYS A 91 THR A 95 5 5 HELIX 3 AA3 ASP C 58 ASN C 62 5 5 HELIX 4 AA4 LYS C 91 THR C 95 5 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N GLN A 5 SHEET 3 AA1 4 THR A 82 MET A 87 -1 O LEU A 85 N LEU A 20 SHEET 4 AA1 4 PHE A 72 ASP A 77 -1 N THR A 73 O GLN A 86 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 117 VAL A 121 1 O THR A 120 N VAL A 12 SHEET 3 AA2 6 ALA A 96 ALA A 103 -1 N TYR A 98 O THR A 117 SHEET 4 AA2 6 VAL A 36 GLN A 43 -1 N GLN A 42 O ILE A 97 SHEET 5 AA2 6 GLY A 46 SER A 55 -1 O ASP A 50 N ARG A 41 SHEET 6 AA2 6 TYR A 110 TRP A 113 0 SHEET 1 AA3 7 HIS A 63 VAL A 64 0 SHEET 2 AA3 7 GLY A 46 SER A 55 -1 N GLN A 54 O HIS A 63 SHEET 3 AA3 7 VAL A 36 GLN A 43 -1 N ARG A 41 O ASP A 50 SHEET 4 AA3 7 ALA A 96 ALA A 103 -1 O ILE A 97 N GLN A 42 SHEET 5 AA3 7 LYS B 50 CYS B 54 0 SHEET 6 AA3 7 CYS B 23 TRP B 28 -1 N VAL B 27 O LYS B 50 SHEET 7 AA3 7 ILE B 35 CYS B 40 -1 O GLU B 37 N LYS B 26 SHEET 1 AA4 2 GLU B 2 HIS B 4 0 SHEET 2 AA4 2 THR B 14 THR B 16 -1 O LYS B 15 N CYS B 3 SHEET 1 AA5 4 GLN C 3 SER C 7 0 SHEET 2 AA5 4 LEU C 18 SER C 25 -1 O ALA C 23 N GLN C 5 SHEET 3 AA5 4 THR C 82 MET C 87 -1 O LEU C 85 N LEU C 20 SHEET 4 AA5 4 PHE C 72 ASP C 77 -1 N THR C 73 O GLN C 86 SHEET 1 AA6 6 GLY C 10 VAL C 12 0 SHEET 2 AA6 6 THR C 117 VAL C 121 1 O THR C 120 N VAL C 12 SHEET 3 AA6 6 ALA C 96 ALA C 103 -1 N TYR C 98 O THR C 117 SHEET 4 AA6 6 VAL C 36 GLN C 43 -1 N GLN C 42 O ILE C 97 SHEET 5 AA6 6 GLY C 46 SER C 55 -1 O ASP C 50 N ARG C 41 SHEET 6 AA6 6 TYR C 110 TRP C 113 0 SHEET 1 AA7 7 HIS C 63 VAL C 64 0 SHEET 2 AA7 7 GLY C 46 SER C 55 -1 N GLN C 54 O HIS C 63 SHEET 3 AA7 7 VAL C 36 GLN C 43 -1 N ARG C 41 O ASP C 50 SHEET 4 AA7 7 ALA C 96 ALA C 103 -1 O ILE C 97 N GLN C 42 SHEET 5 AA7 7 ILE D 49 CYS D 54 0 SHEET 6 AA7 7 CYS D 23 TRP D 28 -1 N VAL D 27 O LYS D 50 SHEET 7 AA7 7 ILE D 35 CYS D 40 -1 O GLU D 37 N LYS D 26 SHEET 1 AA8 2 GLU D 2 HIS D 4 0 SHEET 2 AA8 2 THR D 14 THR D 16 -1 O LYS D 15 N CYS D 3 SSBOND 1 CYS A 22 CYS A 100 1555 1555 2.03 SSBOND 2 CYS B 3 CYS B 23 1555 1555 2.01 SSBOND 3 CYS B 17 CYS B 40 1555 1555 2.04 SSBOND 4 CYS B 42 CYS B 53 1555 1555 2.03 SSBOND 5 CYS B 54 CYS B 59 1555 1555 2.02 SSBOND 6 CYS C 22 CYS C 100 1555 1555 2.03 SSBOND 7 CYS D 3 CYS D 23 1555 1555 2.04 SSBOND 8 CYS D 17 CYS D 40 1555 1555 2.04 SSBOND 9 CYS D 42 CYS D 53 1555 1555 2.03 SSBOND 10 CYS D 54 CYS D 59 1555 1555 2.02 LINK OD2 ASP A 50 NI NI A 203 1555 1555 1.77 LINK OD1 ASP A 59 NI NI A 201 1555 1555 2.60 LINK OD2 ASP A 59 NI NI A 201 1555 1555 1.83 LINK OD2 ASP A 59 NI NI A 201 1555 4555 1.76 LINK OE2 GLU A 60 NI NI A 206 1555 1555 2.37 LINK OE1 GLU A 60 NI NI D 101 1555 1555 2.25 LINK OE1 GLU A 93 NI NI A 202 1555 1555 2.20 LINK NI NI A 202 O HOH A 311 1555 1555 2.28 LINK NI NI A 203 NE2 HIS D 31 6554 1555 1.96 LINK NI NI A 205 OD2 ASP D 57 4555 1555 2.67 LINK NI NI A 205 O HOH D 203 1555 4555 2.22 LINK NI NI A 206 O HOH A 303 1555 1555 2.08 LINK NI NI A 206 O HOH A 309 1555 1555 1.83 LINK NI NI A 206 O HOH A 312 1555 1555 2.44 LINK NI NI A 206 O HOH A 313 1555 1555 2.59 LINK NE2 HIS B 4 NI NI B 101 1555 1555 2.57 LINK ND1 HIS B 31 NI NI C 201 1555 1555 2.78 LINK NE2 HIS B 31 NI NI C 201 1555 1555 1.96 LINK OD2 ASP B 57 NI NI B 102 1555 1555 2.34 LINK ND2 ASN B 61 NI NI B 101 1555 1555 2.26 LINK NI NI B 101 O HOH B 203 1555 1555 2.05 LINK NI NI B 101 OE1 GLU C 60 6554 1555 2.18 LINK NI NI B 102 O HOH B 205 1555 1555 2.76 LINK O HOH B 205 NI NI C 203 8555 1555 2.70 LINK OG1 THR C 47 NI NI C 201 1555 1555 2.49 LINK OD2 ASP C 59 NI NI C 203 1555 1555 2.06 LINK OD2 ASP C 59 NI NI C 203 1555 3654 2.06 LINK OE2 GLU C 60 NI NI C 202 1555 1555 2.39 LINK OE1 GLU C 93 NI NI C 204 1555 1555 2.22 LINK OD2 ASP C 108 NI NI C 205 1555 1555 1.85 LINK NI NI C 202 O HOH C 307 1555 1555 1.87 LINK NI NI C 202 O HOH C 311 1555 1555 1.98 LINK NE2 HIS D 4 NI NI D 101 1555 1555 2.43 LINK OE1 GLU D 20 NI NI D 102 1555 1555 2.57 LINK OE2 GLU D 20 NI NI D 102 1555 1555 1.91 LINK OD1 ASN D 61 NI NI D 101 1555 1555 2.36 LINK NI NI D 101 O HOH D 201 1555 1555 2.13 CRYST1 104.150 104.090 79.340 90.00 90.00 90.00 C 2 2 21 16 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 0.009602 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009607 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012604 0.00000 MTRIX1 1 -0.000103 -0.999996 -0.002822 52.13679 1 MTRIX2 1 0.999993 -0.000114 0.003868 -0.15735 1 MTRIX3 1 -0.003868 -0.002822 0.999989 -19.79166 1 MTRIX1 2 0.012382 -0.999919 -0.002835 51.98679 1 MTRIX2 2 0.999920 0.012375 0.002548 -0.29653 1 MTRIX3 2 -0.002513 -0.002866 0.999993 -19.73055 1