HEADER IMMUNE SYSTEM 16-DEC-22 8FIF TITLE A2.3 NANOBODY IN COMPLEX WITH MICROCYSTIN-LR CAVEAT 8FIF MAA D 7 HAS WRONG CHIRALITY AT ATOM CA MAA F 7 HAS WRONG CAVEAT 2 8FIF CHIRALITY AT ATOM CA ACB G 3 HAS WRONG CHIRALITY AT ATOM CB CAVEAT 3 8FIF MAA G 7 HAS WRONG CHIRALITY AT ATOM CA COMPND MOL_ID: 1; COMPND 2 MOLECULE: SINGLE DOMAIN CAMELID NANOBODY VHH A2.3; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MICROCYSTIN-LR; COMPND 7 CHAIN: D, F, G; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_COMMON: LLAMA; SOURCE 4 ORGANISM_TAXID: 9844; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 MOL_ID: 2; SOURCE 8 SYNTHETIC: YES; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630 KEYWDS NANOBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.ARENAS,S.TABARES-DA ROSA,G.GONZALEZ-SAPIENZA,D.K.WILSON REVDAT 1 20-DEC-23 8FIF 0 JRNL AUTH R.ARENAS,S.TABARES-DA ROSA,G.GONZALEZ-SAPIENZA,D.K.WILSON JRNL TITL A2.3 NANOBODY IN COMPLEX WITH MICROCYSTIN-LR JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0403 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.69 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 16990 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : 0.05 REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.236 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.985 REMARK 3 FREE R VALUE TEST SET COUNT : 847 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) : 2.35 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1155 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.40 REMARK 3 BIN R VALUE (WORKING SET) : 0.4250 REMARK 3 BIN FREE R VALUE SET COUNT : 73 REMARK 3 BIN FREE R VALUE : 0.4550 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2981 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 142 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.21 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.01300 REMARK 3 B22 (A**2) : 0.12500 REMARK 3 B33 (A**2) : -0.13800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.523 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.296 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.287 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.994 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3037 ; 0.009 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 2824 ; 0.002 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4098 ; 1.920 ; 1.742 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6433 ; 0.657 ; 1.671 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 354 ; 9.415 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 27 ; 9.127 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 460 ;18.555 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 432 ; 0.078 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3714 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 840 ; 0.003 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 767 ; 0.278 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 44 ; 0.200 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1427 ; 0.195 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 154 ; 0.275 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.010 ; 0.200 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): 1428 ; 7.200 ; 5.916 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1429 ; 7.198 ; 5.917 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1781 ; 9.660 ;10.592 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1781 ; 9.659 ;10.595 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1609 ; 7.561 ; 6.575 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1610 ; 7.559 ; 6.574 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2317 ;11.001 ;11.825 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2318 ;10.999 ;11.823 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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 BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8FIF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-22. REMARK 100 THE DEPOSITION ID IS D_1000270723. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-JAN-18 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 : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979460 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17031 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350 REMARK 200 RESOLUTION RANGE LOW (A) : 36.010 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.06700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.99700 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 (%): 50.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V PEG MME 3350, 200 MM AMMONIUM REMARK 280 SULFATE, 100 MM HEPES, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 19.04850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.20600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.65850 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.20600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.04850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.65850 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, G 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 400 REMARK 400 COMPOUND REMARK 400 REMARK 400 THE MICROCYSTIN-LR (MCLR) BOUND FORM IS OLIGOPEPTIDE, A MEMBER OF REMARK 400 TOXIN CLASS. REMARK 400 REMARK 400 GROUP: 1 REMARK 400 NAME: MICROCYSTIN-LR (MCLR) BOUND FORM REMARK 400 CHAIN: D, F, G REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER REMARK 400 DESCRIPTION: NULL 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 MET A 1 REMARK 465 ALA A 2 REMARK 465 GLN A 3 REMARK 465 HIS A 124 REMARK 465 HIS A 125 REMARK 465 HIS A 126 REMARK 465 HIS A 127 REMARK 465 HIS A 128 REMARK 465 HIS A 129 REMARK 465 MET B 1 REMARK 465 ALA B 2 REMARK 465 GLN B 3 REMARK 465 VAL B 121 REMARK 465 SER B 123 REMARK 465 HIS B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 GLN C 3 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS 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 O VAL C 14 O HOH C 201 1.89 REMARK 500 O TYR A 96 O HOH A 201 1.90 REMARK 500 O PRO C 43 O HOH C 202 1.93 REMARK 500 O SER A 100 O HOH A 202 1.95 REMARK 500 O FGA D 6 O HOH D 101 1.99 REMARK 500 N SER A 19 O HOH A 203 2.01 REMARK 500 OE2 GLU C 103 OH TYR C 112 2.07 REMARK 500 O HOH B 204 O HOH C 222 2.08 REMARK 500 C VAL C 14 O HOH C 201 2.10 REMARK 500 N LEU G 2 O MAA G 7 2.12 REMARK 500 C GLY A 18 O HOH A 203 2.18 REMARK 500 O TYR A 39 O HOH A 201 2.19 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 ASN B 60 CB - CA - C ANGL. DEV. = 12.6 DEGREES REMARK 500 ARG D 4 CD - NE - CZ ANGL. DEV. = 15.1 DEGREES REMARK 500 ARG F 4 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES REMARK 500 ARG G 4 NE - CZ - NH1 ANGL. DEV. = 4.3 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 PRO A 16 151.72 -42.16 REMARK 500 ARG A 73 147.53 -173.53 REMARK 500 SER A 122 -103.36 -134.67 REMARK 500 VAL B 50 -70.85 -119.09 REMARK 500 ARG B 58 87.10 -68.13 REMARK 500 LYS B 66 -141.74 -101.35 REMARK 500 LEU B 87 152.35 -48.08 REMARK 500 THR B 92 146.46 -38.44 REMARK 500 ALA B 93 -162.31 -174.26 REMARK 500 THR C 106 -162.91 -104.17 REMARK 500 LEU D 2 -41.66 -159.46 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 1ZN D 5 FGA D 6 131.32 REMARK 500 1ZN G 5 FGA G 6 128.93 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 54 0.09 SIDE CHAIN REMARK 500 ARG A 110 0.09 SIDE CHAIN REMARK 500 ARG B 40 0.08 SIDE CHAIN REMARK 500 ARG B 54 0.08 SIDE CHAIN REMARK 500 ARG C 110 0.08 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 1ZN D 5 -23.31 REMARK 500 1ZN F 5 -15.30 REMARK 500 1ZN G 5 -19.82 REMARK 500 REMARK 500 REMARK: NULL DBREF 8FIF A 1 129 PDB 8FIF 8FIF 1 129 DBREF 8FIF B 1 129 PDB 8FIF 8FIF 1 129 DBREF 8FIF C 1 129 PDB 8FIF 8FIF 1 129 DBREF 8FIF D 1 7 PDB 8FIF 8FIF 1 7 DBREF 8FIF F 1 7 PDB 8FIF 8FIF 1 7 DBREF 8FIF G 1 7 PDB 8FIF 8FIF 1 7 SEQRES 1 A 129 MET ALA GLN VAL THR LEU LYS GLU SER GLY GLY GLY LEU SEQRES 2 A 129 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 A 129 SER GLY GLY ILE SER ARG VAL ASN VAL ALA GLY TRP TYR SEQRES 4 A 129 ARG GLN ALA PRO GLY GLN GLN ARG GLU MET VAL ALA VAL SEQRES 5 A 129 ILE ARG SER GLY GLY ARG ILE ASN TYR ALA ASP PHE VAL SEQRES 6 A 129 LYS GLY ARG PHE THR PHE SER ARG ASP ASP ALA LYS GLN SEQRES 7 A 129 THR ILE TYR LEU GLN MET ASP ASN LEU LYS SER GLU ASP SEQRES 8 A 129 THR ALA VAL TYR TYR CYS TYR GLY SER LEU LEU GLU THR SEQRES 9 A 129 GLY THR PHE GLN TYR ARG GLU TYR TRP GLY GLN GLY THR SEQRES 10 A 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 129 MET ALA GLN VAL THR LEU LYS GLU SER GLY GLY GLY LEU SEQRES 2 B 129 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 B 129 SER GLY GLY ILE SER ARG VAL ASN VAL ALA GLY TRP TYR SEQRES 4 B 129 ARG GLN ALA PRO GLY GLN GLN ARG GLU MET VAL ALA VAL SEQRES 5 B 129 ILE ARG SER GLY GLY ARG ILE ASN TYR ALA ASP PHE VAL SEQRES 6 B 129 LYS GLY ARG PHE THR PHE SER ARG ASP ASP ALA LYS GLN SEQRES 7 B 129 THR ILE TYR LEU GLN MET ASP ASN LEU LYS SER GLU ASP SEQRES 8 B 129 THR ALA VAL TYR TYR CYS TYR GLY SER LEU LEU GLU THR SEQRES 9 B 129 GLY THR PHE GLN TYR ARG GLU TYR TRP GLY GLN GLY THR SEQRES 10 B 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 C 129 MET ALA GLN VAL THR LEU LYS GLU SER GLY GLY GLY LEU SEQRES 2 C 129 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 C 129 SER GLY GLY ILE SER ARG VAL ASN VAL ALA GLY TRP TYR SEQRES 4 C 129 ARG GLN ALA PRO GLY GLN GLN ARG GLU MET VAL ALA VAL SEQRES 5 C 129 ILE ARG SER GLY GLY ARG ILE ASN TYR ALA ASP PHE VAL SEQRES 6 C 129 LYS GLY ARG PHE THR PHE SER ARG ASP ASP ALA LYS GLN SEQRES 7 C 129 THR ILE TYR LEU GLN MET ASP ASN LEU LYS SER GLU ASP SEQRES 8 C 129 THR ALA VAL TYR TYR CYS TYR GLY SER LEU LEU GLU THR SEQRES 9 C 129 GLY THR PHE GLN TYR ARG GLU TYR TRP GLY GLN GLY THR SEQRES 10 C 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 7 DAL LEU ACB ARG 1ZN FGA MAA SEQRES 1 F 7 DAL LEU ACB ARG 1ZN FGA MAA SEQRES 1 G 7 DAL LEU ACB ARG 1ZN FGA MAA HET DAL D 1 5 HET ACB D 3 9 HET 1ZN D 5 23 HET FGA D 6 9 HET MAA D 7 6 HET DAL F 1 5 HET ACB F 3 9 HET 1ZN F 5 23 HET FGA F 6 9 HET MAA F 7 6 HET DAL G 1 5 HET ACB G 3 9 HET 1ZN G 5 23 HET FGA G 6 9 HET MAA G 7 6 HETNAM DAL D-ALANINE HETNAM ACB 3-METHYL-BETA-D-ASPARTIC ACID HETNAM 1ZN (2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL- HETNAM 2 1ZN 10-PHENYLDECA-4,6-DIENOIC ACID HETNAM FGA GAMMA-D-GLUTAMIC ACID HETNAM MAA N-METHYL-L-ALANINE HETSYN ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID HETSYN FGA D-GLUTAMIC ACID FORMUL 4 DAL 3(C3 H7 N O2) FORMUL 4 ACB 3(C5 H9 N O4) FORMUL 4 1ZN 3(C20 H29 N O3) FORMUL 4 FGA 3(C5 H9 N O4) FORMUL 4 MAA 3(C4 H9 N O2) FORMUL 7 HOH *142(H2 O) HELIX 1 AA1 ASP A 63 LYS A 66 5 4 HELIX 2 AA2 LYS A 88 THR A 92 5 5 HELIX 3 AA3 LYS C 88 THR C 92 5 5 SHEET 1 AA1 4 THR A 5 GLY A 10 0 SHEET 2 AA1 4 LEU A 20 SER A 27 -1 O ALA A 25 N LYS A 7 SHEET 3 AA1 4 THR A 79 MET A 84 -1 O MET A 84 N LEU A 20 SHEET 4 AA1 4 PHE A 69 ASP A 74 -1 N ASP A 74 O THR A 79 SHEET 1 AA2 6 GLY A 12 VAL A 14 0 SHEET 2 AA2 6 THR A 117 VAL A 121 1 O THR A 120 N GLY A 12 SHEET 3 AA2 6 ALA A 93 GLU A 103 -1 N TYR A 95 O THR A 117 SHEET 4 AA2 6 ILE A 30 GLN A 41 -1 N VAL A 35 O SER A 100 SHEET 5 AA2 6 GLU A 48 ARG A 54 -1 O ALA A 51 N TRP A 38 SHEET 6 AA2 6 ILE A 59 TYR A 61 -1 O ASN A 60 N VAL A 52 SHEET 1 AA3 4 GLY A 12 VAL A 14 0 SHEET 2 AA3 4 THR A 117 VAL A 121 1 O THR A 120 N GLY A 12 SHEET 3 AA3 4 ALA A 93 GLU A 103 -1 N TYR A 95 O THR A 117 SHEET 4 AA3 4 ARG A 110 TRP A 113 -1 O TYR A 112 N GLY A 99 SHEET 1 AA4 4 LEU B 6 SER B 9 0 SHEET 2 AA4 4 GLY B 18 ALA B 26 -1 O SER B 23 N SER B 9 SHEET 3 AA4 4 THR B 79 LEU B 87 -1 O ILE B 80 N CYS B 24 SHEET 4 AA4 4 PHE B 69 ASP B 74 -1 N ASP B 74 O THR B 79 SHEET 1 AA5 6 GLY B 12 LEU B 13 0 SHEET 2 AA5 6 THR B 117 THR B 120 1 O THR B 120 N GLY B 12 SHEET 3 AA5 6 ALA B 93 LEU B 102 -1 N TYR B 95 O THR B 117 SHEET 4 AA5 6 ARG B 32 GLN B 41 -1 N VAL B 35 O SER B 100 SHEET 5 AA5 6 GLU B 48 ARG B 54 -1 O GLU B 48 N ARG B 40 SHEET 6 AA5 6 ILE B 59 TYR B 61 -1 O ASN B 60 N VAL B 52 SHEET 1 AA6 4 GLY B 12 LEU B 13 0 SHEET 2 AA6 4 THR B 117 THR B 120 1 O THR B 120 N GLY B 12 SHEET 3 AA6 4 ALA B 93 LEU B 102 -1 N TYR B 95 O THR B 117 SHEET 4 AA6 4 ARG B 110 TRP B 113 -1 O TYR B 112 N GLY B 99 SHEET 1 AA7 4 THR C 5 GLY C 10 0 SHEET 2 AA7 4 LEU C 20 SER C 27 -1 O ALA C 25 N LYS C 7 SHEET 3 AA7 4 THR C 79 MET C 84 -1 O MET C 84 N LEU C 20 SHEET 4 AA7 4 PHE C 69 ASP C 74 -1 N THR C 70 O GLN C 83 SHEET 1 AA8 6 GLY C 12 VAL C 14 0 SHEET 2 AA8 6 THR C 117 VAL C 121 1 O THR C 120 N GLY C 12 SHEET 3 AA8 6 ALA C 93 LEU C 102 -1 N ALA C 93 O VAL C 119 SHEET 4 AA8 6 VAL C 33 GLN C 41 -1 N TYR C 39 O TYR C 96 SHEET 5 AA8 6 ARG C 47 ARG C 54 -1 O ALA C 51 N TRP C 38 SHEET 6 AA8 6 ILE C 59 TYR C 61 -1 O ASN C 60 N VAL C 52 SHEET 1 AA9 4 GLY C 12 VAL C 14 0 SHEET 2 AA9 4 THR C 117 VAL C 121 1 O THR C 120 N GLY C 12 SHEET 3 AA9 4 ALA C 93 LEU C 102 -1 N ALA C 93 O VAL C 119 SHEET 4 AA9 4 TYR C 109 TRP C 113 -1 O ARG C 110 N LEU C 101 SSBOND 1 CYS A 24 CYS A 97 1555 1555 2.06 SSBOND 2 CYS B 24 CYS B 97 1555 1555 2.03 SSBOND 3 CYS C 24 CYS C 97 1555 1555 2.04 LINK C DAL D 1 N LEU D 2 1555 1555 1.33 LINK N DAL D 1 C MAA D 7 1555 1555 1.32 LINK C LEU D 2 N ACB D 3 1555 1555 1.36 LINK CG ACB D 3 N ARG D 4 1555 1555 1.33 LINK C ARG D 4 N 1ZN D 5 1555 1555 1.33 LINK C 1ZN D 5 N FGA D 6 1555 1555 1.34 LINK CD FGA D 6 N MAA D 7 1555 1555 1.36 LINK C DAL F 1 N LEU F 2 1555 1555 1.35 LINK N DAL F 1 C MAA F 7 1555 1555 1.35 LINK C LEU F 2 N ACB F 3 1555 1555 1.35 LINK CG ACB F 3 N ARG F 4 1555 1555 1.33 LINK C ARG F 4 N 1ZN F 5 1555 1555 1.33 LINK C 1ZN F 5 N FGA F 6 1555 1555 1.33 LINK CD FGA F 6 N MAA F 7 1555 1555 1.35 LINK C DAL G 1 N LEU G 2 1555 1555 1.37 LINK N DAL G 1 C MAA G 7 1555 1555 1.36 LINK C LEU G 2 N ACB G 3 1555 1555 1.33 LINK CG ACB G 3 N ARG G 4 1555 1555 1.34 LINK C ARG G 4 N 1ZN G 5 1555 1555 1.34 LINK C 1ZN G 5 N FGA G 6 1555 1555 1.32 LINK CD FGA G 6 N MAA G 7 1555 1555 1.35 CRYST1 38.097 101.317 102.412 90.00 90.00 90.00 P 21 21 21 12 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 0.026249 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009870 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009764 0.00000