HEADER IMMUNE SYSTEM 11-DEC-23 8REL TITLE FAB OF AN ANTI-PVAMA1 MONOCLONAL ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 8.1.1 HEAVY CHAIN; COMPND 3 CHAIN: H, M; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: FAB 8.1.1 LIGHT CHAIN; COMPND 6 CHAIN: L, N SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090 KEYWDS MONOCLONAL ANTOBODY, ANTI-AMA-1, FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR G.A.BENTLEY,F.A.SAUL,B.VULLIEZ-LENORMAND REVDAT 1 16-OCT-24 8REL 0 JRNL AUTH F.A.SAUL,B.VULLIEZ-LE NORMAND,A.BOES,H.SPIEGEL,C.H.M.KOCKEN, JRNL AUTH 2 B.W.FABER,G.A.BENTLEY JRNL TITL CONFORMATIONAL VARIABILITY IN THE D2 LOOP OF PLASMODIUM JRNL TITL 2 APICAL MEMBRANE ANTIGEN 1. JRNL REF J STRUCT BIOL X V. 10 00110 2024 JRNL REFN ESSN 2590-1524 JRNL PMID 39324028 JRNL DOI 10.1016/J.YJSBX.2024.100110 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0415 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.24 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 3 NUMBER OF REFLECTIONS : 40631 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1231 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2137 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.03 REMARK 3 BIN R VALUE (WORKING SET) : 0.3070 REMARK 3 BIN FREE R VALUE SET COUNT : 65 REMARK 3 BIN FREE R VALUE : 0.3420 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6344 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 1 REMARK 3 SOLVENT ATOMS : 438 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.77 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.94000 REMARK 3 B22 (A**2) : 0.71000 REMARK 3 B33 (A**2) : 0.21000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.03000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.307 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.213 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.307 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6515 ; 0.013 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 5856 ; 0.004 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8879 ; 1.065 ; 1.663 REMARK 3 BOND ANGLES OTHERS (DEGREES): 13580 ; 0.386 ; 1.572 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 822 ; 6.846 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 27 ; 5.069 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1007 ;13.850 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 988 ; 0.052 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7589 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1459 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3318 ; 1.437 ; 2.441 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3318 ; 1.436 ; 2.441 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4130 ; 2.419 ; 4.378 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4131 ; 2.419 ; 4.377 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3197 ; 1.549 ; 2.626 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3196 ; 1.547 ; 2.626 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4750 ; 2.587 ; 4.742 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7085 ; 5.095 ;28.650 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7011 ; 5.018 ;28.190 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 : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 114 REMARK 3 RESIDUE RANGE : L 1 L 107 REMARK 3 ORIGIN FOR THE GROUP (A): 19.9457 -3.6809 -11.3549 REMARK 3 T TENSOR REMARK 3 T11: 0.0511 T22: 0.1007 REMARK 3 T33: 0.0469 T12: -0.0003 REMARK 3 T13: -0.0200 T23: -0.0012 REMARK 3 L TENSOR REMARK 3 L11: 1.3086 L22: 0.1113 REMARK 3 L33: 0.2004 L12: 0.0130 REMARK 3 L13: 0.2977 L23: -0.0434 REMARK 3 S TENSOR REMARK 3 S11: -0.0153 S12: 0.0252 S13: -0.0010 REMARK 3 S21: -0.0380 S22: 0.0184 S23: -0.0286 REMARK 3 S31: -0.0177 S32: -0.0359 S33: -0.0030 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 115 H 213 REMARK 3 RESIDUE RANGE : L 108 L 213 REMARK 3 ORIGIN FOR THE GROUP (A): 10.1338 -4.5576 20.3068 REMARK 3 T TENSOR REMARK 3 T11: 0.0187 T22: 0.1544 REMARK 3 T33: 0.0353 T12: -0.0113 REMARK 3 T13: -0.0218 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 0.9734 L22: 0.0626 REMARK 3 L33: 0.4574 L12: -0.2093 REMARK 3 L13: -0.1293 L23: -0.0401 REMARK 3 S TENSOR REMARK 3 S11: 0.0477 S12: -0.0663 S13: 0.0278 REMARK 3 S21: -0.0147 S22: -0.0192 S23: 0.0032 REMARK 3 S31: 0.0070 S32: 0.0335 S33: -0.0285 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : M 1 M 114 REMARK 3 RESIDUE RANGE : N 2 N 107 REMARK 3 ORIGIN FOR THE GROUP (A): 27.7647 -4.3072 71.6663 REMARK 3 T TENSOR REMARK 3 T11: 0.0045 T22: 0.2084 REMARK 3 T33: 0.0053 T12: -0.0229 REMARK 3 T13: 0.0003 T23: 0.0076 REMARK 3 L TENSOR REMARK 3 L11: 1.7525 L22: 0.1043 REMARK 3 L33: 0.6622 L12: -0.1410 REMARK 3 L13: 0.5670 L23: -0.1688 REMARK 3 S TENSOR REMARK 3 S11: 0.0376 S12: -0.2088 S13: 0.0024 REMARK 3 S21: 0.0108 S22: 0.0011 S23: -0.0010 REMARK 3 S31: -0.0063 S32: -0.1317 S33: -0.0387 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : M 115 M 213 REMARK 3 RESIDUE RANGE : N 108 N 213 REMARK 3 ORIGIN FOR THE GROUP (A): 37.3311 -3.2405 39.7986 REMARK 3 T TENSOR REMARK 3 T11: 0.0094 T22: 0.2035 REMARK 3 T33: 0.0122 T12: 0.0113 REMARK 3 T13: -0.0059 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 0.6441 L22: 0.1822 REMARK 3 L33: 0.9327 L12: 0.2001 REMARK 3 L13: -0.0600 L23: -0.0237 REMARK 3 S TENSOR REMARK 3 S11: -0.0207 S12: -0.0719 S13: -0.0396 REMARK 3 S21: -0.0300 S22: -0.0019 S23: -0.0028 REMARK 3 S31: 0.0111 S32: -0.0776 S33: 0.0226 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 8REL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1292134887. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-DEC-06 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 : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9340 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41875 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 46.020 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.13900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21 REMARK 200 COMPLETENESS FOR SHELL (%) : 74.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 0.60800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 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 (%): 37.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF FAB8.1.1 WERE OBTAINED BY REMARK 280 MIXING 1 MICRO-L OF PROTEIN AND 1 MICRO-L OF RESERVOIR REMARK 280 CONTAINING 24% PEG 4000, 80 MM SODIUM ACETATE PH 4.6 AND 0.16 M REMARK 280 AMMONIUM ACETATE. THE FINAL PROTEIN CONCENTRATION WAS 3.6 MG/ML. REMARK 280 CRYO-PROTECTING BUFFER FOR FABF8.1.1 CONSISTED OF THE REMARK 280 CRYSTALLISATION BUFFER WHERE PEG WAS INCREASED TO 30% ADDED WITH REMARK 280 15% OF GLYCEROL (V/V)., VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 290K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.76000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY H 127 REMARK 465 CYS H 128 REMARK 465 GLY H 129 REMARK 465 ASP H 130 REMARK 465 THR H 131 REMARK 465 THR H 132 REMARK 465 GLY H 133 REMARK 465 SER H 134 REMARK 465 LYS L 199 REMARK 465 THR L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 CYS L 214 REMARK 465 LEU M 98 REMARK 465 GLY M 99 REMARK 465 GLY M 127 REMARK 465 CYS M 128 REMARK 465 GLY M 129 REMARK 465 ASP M 130 REMARK 465 THR M 131 REMARK 465 THR M 132 REMARK 465 GLY M 133 REMARK 465 SER M 134 REMARK 465 SER M 156 REMARK 465 GLY M 157 REMARK 465 SER M 158 REMARK 465 LEU M 159 REMARK 465 SER M 160 REMARK 465 PCA N 1 REMARK 465 LYS N 199 REMARK 465 THR N 200 REMARK 465 SER N 201 REMARK 465 THR N 202 REMARK 465 CYS N 214 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 TYR H 56 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU M 1 CG CD OE1 OE2 REMARK 470 TYR M 56 CG CD1 CD2 CE1 CE2 CZ OH 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 HOH N 312 O HOH N 378 2.18 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 GLU H 148 CD GLU H 148 OE1 0.079 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 ALA H 88 162.25 178.68 REMARK 500 ARG H 100 -11.47 85.82 REMARK 500 SER H 112 149.30 -171.71 REMARK 500 ASN H 155 54.46 39.39 REMARK 500 TRP L 47 -52.95 -130.61 REMARK 500 THR L 51 -48.26 73.65 REMARK 500 ALA L 84 175.58 171.16 REMARK 500 TRP L 91 57.50 -151.04 REMARK 500 ARG L 108 -178.17 -171.62 REMARK 500 ASP M 31 42.68 -96.70 REMARK 500 LYS M 64 114.46 -31.23 REMARK 500 SER M 162 43.51 -85.52 REMARK 500 PRO M 189 30.43 -88.68 REMARK 500 HIS M 199 78.06 -117.97 REMARK 500 SER M 203 45.07 36.81 REMARK 500 TRP N 47 -50.99 -128.09 REMARK 500 THR N 51 -53.05 79.05 REMARK 500 ALA N 84 173.25 173.83 REMARK 500 TRP N 91 51.61 -153.99 REMARK 500 ASN N 138 62.96 65.79 REMARK 500 GLN N 156 -62.82 -91.07 REMARK 500 REMARK 500 REMARK: NULL DBREF 8REL H 1 213 PDB 8REL 8REL 1 213 DBREF 8REL L 1 214 PDB 8REL 8REL 1 214 DBREF 8REL M 1 213 PDB 8REL 8REL 1 213 DBREF 8REL N 1 214 PDB 8REL 8REL 1 214 SEQRES 1 H 220 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 220 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 220 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 H 220 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA THR ILE ASN SEQRES 5 H 220 ASP GLY GLY THR TYR THR TYR TYR PRO ASP SER VAL LYS SEQRES 6 H 220 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN ASN SEQRES 7 H 220 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 H 220 ALA MET TYR PHE CYS ALA ARG GLY SER GLN LEU GLY ARG SEQRES 9 H 220 GLY GLU PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 220 VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 H 220 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL SEQRES 12 H 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER SEQRES 13 H 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER SEQRES 14 H 220 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR SEQRES 15 H 220 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 H 220 PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA SEQRES 17 H 220 SER SER THR THR VAL ASP LYS LYS LEU GLU PRO SER SEQRES 1 L 213 PCA ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA SEQRES 2 L 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 L 213 SER SER VAL SER TYR MET HIS TRP TYR GLN GLN LYS PRO SEQRES 4 L 213 GLY SER SER PRO LYS PRO TRP ILE TYR ALA THR PHE ASN SEQRES 5 L 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 213 SER GLY THR SER TYR SER LEU THR ILE SER ARG VAL GLU SEQRES 7 L 213 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 L 213 SER ASN PRO PRO THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 9 L 213 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 L 213 ASN ARG ASN GLU CYS SEQRES 1 M 220 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 M 220 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 M 220 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 M 220 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA THR ILE ASN SEQRES 5 M 220 ASP GLY GLY THR TYR THR TYR TYR PRO ASP SER VAL LYS SEQRES 6 M 220 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN ASN SEQRES 7 M 220 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 M 220 ALA MET TYR PHE CYS ALA ARG GLY SER GLN LEU GLY ARG SEQRES 9 M 220 GLY GLU PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 M 220 VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 M 220 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL SEQRES 12 M 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER SEQRES 13 M 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER SEQRES 14 M 220 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR SEQRES 15 M 220 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 M 220 PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA SEQRES 17 M 220 SER SER THR THR VAL ASP LYS LYS LEU GLU PRO SER SEQRES 1 N 213 PCA ILE VAL LEU SER GLN SER PRO ALA ILE LEU SER ALA SEQRES 2 N 213 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 N 213 SER SER VAL SER TYR MET HIS TRP TYR GLN GLN LYS PRO SEQRES 4 N 213 GLY SER SER PRO LYS PRO TRP ILE TYR ALA THR PHE ASN SEQRES 5 N 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 N 213 SER GLY THR SER TYR SER LEU THR ILE SER ARG VAL GLU SEQRES 7 N 213 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 N 213 SER ASN PRO PRO THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 9 N 213 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 N 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 N 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 N 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 N 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 N 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 N 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 N 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 N 213 ASN ARG ASN GLU CYS HET PCA L 1 8 HET CL H 301 1 HETNAM PCA PYROGLUTAMIC ACID HETNAM CL CHLORIDE ION FORMUL 2 PCA C5 H7 N O3 FORMUL 5 CL CL 1- FORMUL 6 HOH *438(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 LYS H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 SER H 158 5 3 HELIX 4 AA4 LEU H 159 SER H 161 5 3 HELIX 5 AA5 PRO H 200 SER H 203 5 4 HELIX 6 AA6 GLU L 79 ALA L 83 5 5 HELIX 7 AA7 SER L 121 SER L 127 1 7 HELIX 8 AA8 LYS L 183 GLU L 187 1 5 HELIX 9 AA9 THR M 28 TYR M 32 5 5 HELIX 10 AB1 LYS M 83 THR M 87 5 5 HELIX 11 AB2 PRO M 200 SER M 203 5 4 HELIX 12 AB3 GLU N 79 ALA N 83 5 5 HELIX 13 AB4 SER N 121 SER N 127 1 7 HELIX 14 AB5 LYS N 183 ARG N 188 1 6 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 ASN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA2 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O PHE H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 58 -1 O TYR H 58 N THR H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA3 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 VAL H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 LEU H 174 VAL H 183 -1 O TYR H 175 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 VAL H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA5 4 LEU H 174 VAL H 183 -1 O TYR H 175 N TYR H 145 SHEET 4 AA5 4 LEU H 169 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 THR H 194 HIS H 199 -1 O SER H 196 N THR H 153 SHEET 3 AA6 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197 SHEET 1 AA7 3 LEU L 4 SER L 7 0 SHEET 2 AA7 3 VAL L 19 VAL L 30 -1 O ARG L 24 N SER L 5 SHEET 3 AA7 3 PHE L 62 ILE L 75 -1 O TYR L 71 N CYS L 23 SHEET 1 AA8 6 ILE L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 6 HIS L 34 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA8 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA9 4 ILE L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 THR L 114 PHE L 118 0 SHEET 2 AB1 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114 SHEET 3 AB1 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB1 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB2 4 SER L 153 ARG L 155 0 SHEET 2 AB2 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AB2 4 SER L 191 THR L 197 -1 O THR L 197 N ASN L 145 SHEET 4 AB2 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 AB3 4 GLN M 3 SER M 7 0 SHEET 2 AB3 4 LEU M 18 SER M 25 -1 O SER M 21 N SER M 7 SHEET 3 AB3 4 ASN M 77 MET M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 AB3 4 PHE M 67 ASP M 72 -1 N SER M 70 O TYR M 79 SHEET 1 AB4 6 LEU M 11 VAL M 12 0 SHEET 2 AB4 6 THR M 107 VAL M 111 1 O THR M 110 N VAL M 12 SHEET 3 AB4 6 ALA M 88 ARG M 94 -1 N ALA M 88 O VAL M 109 SHEET 4 AB4 6 MET M 34 GLN M 39 -1 N VAL M 37 O PHE M 91 SHEET 5 AB4 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AB4 6 THR M 57 TYR M 58 -1 O TYR M 58 N THR M 50 SHEET 1 AB5 4 LEU M 11 VAL M 12 0 SHEET 2 AB5 4 THR M 107 VAL M 111 1 O THR M 110 N VAL M 12 SHEET 3 AB5 4 ALA M 88 ARG M 94 -1 N ALA M 88 O VAL M 109 SHEET 4 AB5 4 TYR M 102 TRP M 103 -1 O TYR M 102 N ARG M 94 SHEET 1 AB6 4 SER M 120 LEU M 124 0 SHEET 2 AB6 4 VAL M 136 TYR M 145 -1 O GLY M 139 N LEU M 124 SHEET 3 AB6 4 LEU M 174 VAL M 183 -1 O TYR M 175 N TYR M 145 SHEET 4 AB6 4 VAL M 163 GLN M 171 -1 N PHE M 166 O SER M 178 SHEET 1 AB7 3 THR M 151 TRP M 154 0 SHEET 2 AB7 3 VAL M 193 HIS M 199 -1 O SER M 196 N THR M 153 SHEET 3 AB7 3 THR M 204 LEU M 210 -1 O LEU M 210 N VAL M 193 SHEET 1 AB8 3 LEU N 4 SER N 7 0 SHEET 2 AB8 3 VAL N 19 VAL N 30 -1 O THR N 22 N SER N 7 SHEET 3 AB8 3 PHE N 62 ILE N 75 -1 O TYR N 71 N CYS N 23 SHEET 1 AB9 6 ILE N 10 ALA N 13 0 SHEET 2 AB9 6 THR N 102 LEU N 106 1 O GLU N 105 N ALA N 13 SHEET 3 AB9 6 ALA N 84 GLN N 90 -1 N ALA N 84 O LEU N 104 SHEET 4 AB9 6 HIS N 34 GLN N 38 -1 N TYR N 36 O TYR N 87 SHEET 5 AB9 6 LYS N 45 TYR N 49 -1 O LYS N 45 N GLN N 37 SHEET 6 AB9 6 ASN N 53 LEU N 54 -1 O ASN N 53 N TYR N 49 SHEET 1 AC1 4 ILE N 10 ALA N 13 0 SHEET 2 AC1 4 THR N 102 LEU N 106 1 O GLU N 105 N ALA N 13 SHEET 3 AC1 4 ALA N 84 GLN N 90 -1 N ALA N 84 O LEU N 104 SHEET 4 AC1 4 THR N 97 PHE N 98 -1 O THR N 97 N GLN N 90 SHEET 1 AC2 4 THR N 114 PHE N 118 0 SHEET 2 AC2 4 GLY N 129 PHE N 139 -1 O ASN N 137 N THR N 114 SHEET 3 AC2 4 TYR N 173 THR N 182 -1 O LEU N 181 N ALA N 130 SHEET 4 AC2 4 VAL N 159 TRP N 163 -1 N SER N 162 O SER N 176 SHEET 1 AC3 4 SER N 153 GLU N 154 0 SHEET 2 AC3 4 ASN N 145 ILE N 150 -1 N ILE N 150 O SER N 153 SHEET 3 AC3 4 SER N 191 THR N 197 -1 O GLU N 195 N LYS N 147 SHEET 4 AC3 4 ILE N 205 ASN N 210 -1 O ILE N 205 N ALA N 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.12 SSBOND 2 CYS H 140 CYS H 195 1555 1555 1.96 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.10 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.05 SSBOND 5 CYS M 22 CYS M 92 1555 1555 2.07 SSBOND 6 CYS M 140 CYS M 195 1555 1555 2.02 SSBOND 7 CYS N 23 CYS N 88 1555 1555 2.11 SSBOND 8 CYS N 134 CYS N 194 1555 1555 2.01 LINK C PCA L 1 N ILE L 2 1555 1555 1.35 CISPEP 1 PHE H 146 PRO H 147 0 -12.94 CISPEP 2 GLU H 148 SER H 149 0 1.52 CISPEP 3 TRP H 188 PRO H 189 0 5.14 CISPEP 4 SER L 7 PRO L 8 0 -14.17 CISPEP 5 ASN L 94 PRO L 95 0 -1.45 CISPEP 6 TYR L 140 PRO L 141 0 -1.96 CISPEP 7 PHE M 146 PRO M 147 0 -9.36 CISPEP 8 GLU M 148 SER M 149 0 2.00 CISPEP 9 TRP M 188 PRO M 189 0 3.61 CISPEP 10 SER N 7 PRO N 8 0 -0.25 CISPEP 11 ASN N 94 PRO N 95 0 1.25 CISPEP 12 TYR N 140 PRO N 141 0 0.70 CRYST1 53.490 61.520 116.990 90.00 97.49 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.018695 0.000000 0.002457 0.00000 SCALE2 0.000000 0.016255 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008621 0.00000