HEADER IMMUNE SYSTEM 15-JAN-24 8RPE TITLE CRYSTAL STRUCTURE OF THE SMA:VH1 COMPLEX AT 1.2 A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: VH1; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SMA; COMPND 7 CHAIN: E; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA; SOURCE 3 ORGANISM_TAXID: 9839; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SHUFFLE; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET11A(+); SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: SHUFFLE; SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PET11A(+) KEYWDS STABILISATION OF AMYLOIDOGENIC LIGHT CHAINS; THERAPEUTICS KEYWDS 2 DEVELOPMENT, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.MAERIVOET,T.CRABBE,S.V.ANTONYUK,J.MADINE REVDAT 1 29-JAN-25 8RPE 0 JRNL AUTH A.MAERIVOET,S.GALMICHE,A.SCOTT-TUCKER,T.CRABBE,S.ANTONYUK, JRNL AUTH 2 J.MADINE JRNL TITL STABILISATION OF AMYLOIDOGENIC LIGHT CHAINS BY DISPLACING JRNL TITL 2 NATIVE DIMER BINDING INTERFACE WITH THE VARIABLE HEAVY JRNL TITL 3 DOMAIN HAVE POTENTIAL FOR THERAPEUTICS DEVELOPMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0419 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) : 1.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.15 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 63861 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.112 REMARK 3 FREE R VALUE : 0.144 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.033 REMARK 3 FREE R VALUE TEST SET COUNT : 3214 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) : 1.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3634 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.74 REMARK 3 BIN R VALUE (WORKING SET) : 0.1220 REMARK 3 BIN FREE R VALUE SET COUNT : 190 REMARK 3 BIN FREE R VALUE : 0.1520 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1779 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 359 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 9.04 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.04 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.29100 REMARK 3 B22 (A**2) : 0.04100 REMARK 3 B33 (A**2) : -0.33200 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): 0.034 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.035 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.019 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.899 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2071 ; 0.014 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 1899 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2843 ; 1.976 ; 1.813 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4420 ; 0.725 ; 1.755 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 297 ; 7.109 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 13 ; 9.307 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 347 ;10.397 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 301 ; 0.110 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2577 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 509 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 333 ; 0.254 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 77 ; 0.203 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 939 ; 0.179 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 205 ; 0.250 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.321 ; 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): 1011 ; 3.519 ; 1.012 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1010 ; 3.514 ; 1.010 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1278 ; 5.067 ; 1.821 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1279 ; 5.068 ; 1.822 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1060 ; 5.012 ; 1.231 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1061 ; 5.010 ; 1.231 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1533 ; 6.937 ; 2.159 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1534 ; 6.934 ; 2.159 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): 3970 ; 4.221 ; 3.000 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 8RPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1292135771. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUL-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95373 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63942 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200 REMARK 200 RESOLUTION RANGE LOW (A) : 49.540 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 200 DATA REDUNDANCY : 6.200 REMARK 200 R MERGE (I) : 0.03600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22 REMARK 200 COMPLETENESS FOR SHELL (%) : 79.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.16700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS BUFFER AT PH 5.5 AND 20% REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 19.40650 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.53500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.77200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.53500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.40650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.77200 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E 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 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 HIS B -10 REMARK 465 HIS B -9 REMARK 465 HIS B -8 REMARK 465 GLU B -7 REMARK 465 ASN B -6 REMARK 465 LEU B -5 REMARK 465 TYR B -4 REMARK 465 PHE B -3 REMARK 465 GLN B -2 REMARK 465 GLY B -1 REMARK 465 ALA B 0 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 ALA B 55 CB 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 HG1 THR B 91 H VAL B 116 1.34 REMARK 500 O HOH E 430 O HOH E 436 2.16 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 SER B 63 CA SER B 63 CB -0.096 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 ARG E 18 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES REMARK 500 THR E 20 OG1 - CB - CG2 ANGL. DEV. = 14.4 DEGREES REMARK 500 ARG E 60 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES REMARK 500 ARG E 60 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES REMARK 500 ARG E 60 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG E 114 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES REMARK 500 ARG E 114 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 ARG E 114 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES REMARK 500 ARG E 114 NE - CZ - NH2 ANGL. DEV. = 6.2 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 ARG B 53 162.32 -49.45 REMARK 500 ALA B 92 167.14 178.46 REMARK 500 ALA E 57 -34.42 65.69 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 E 18 0.11 SIDE CHAIN REMARK 500 ARG E 114 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 486 DISTANCE = 6.24 ANGSTROMS REMARK 525 HOH B 487 DISTANCE = 7.40 ANGSTROMS REMARK 525 HOH E 470 DISTANCE = 6.01 ANGSTROMS REMARK 525 HOH E 471 DISTANCE = 6.62 ANGSTROMS REMARK 525 HOH E 472 DISTANCE = 7.08 ANGSTROMS DBREF 8RPE B -13 118 PDB 8RPE 8RPE -13 118 DBREF 8RPE E 1 114 PDB 8RPE 8RPE 1 114 SEQRES 1 B 132 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN GLY SEQRES 2 B 132 ALA GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 3 B 132 LEU PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER SEQRES 4 B 132 GLY PHE ASN PHE GLY SER SER ASP MET ASN TRP VAL ARG SEQRES 5 B 132 GLN ALA ALA GLY LYS GLY PRO GLU TRP VAL ALA SER ILE SEQRES 6 B 132 GLU ARG GLY ALA GLY GLY THR ASP TYR ALA ASP SER VAL SEQRES 7 B 132 GLN GLY ARG PHE THR VAL SER ARG ASP ASN ALA LYS SER SEQRES 8 B 132 THR LEU TRP LEU GLN MET ASN SER LEU LYS ALA GLU ASP SEQRES 9 B 132 THR ALA VAL TYR TYR CYS VAL VAL SER ASP ASN SER GLY SEQRES 10 B 132 TYR TYR LYS TYR TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 11 B 132 SER SER SEQRES 1 E 114 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 E 114 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 E 114 GLN SER VAL LEU TYR SER SER ASN ASN ARG ASN TYR LEU SEQRES 4 E 114 ALA TRP TYR GLN GLN LYS LEU GLY GLN PRO PRO LYS LEU SEQRES 5 E 114 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 E 114 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 E 114 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 E 114 TYR TYR CYS HIS GLN TYR TYR SER HIS PRO GLN THR PHE SEQRES 9 E 114 GLY GLN GLY THR LYS LEU GLU LEU LYS ARG HET EDO B 201 10 HET EDO E 201 10 HET EDO E 202 10 HET EDO E 203 10 HET EDO E 204 10 HET EDO E 205 20 HET EDO E 206 10 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 EDO 7(C2 H6 O2) FORMUL 10 HOH *359(H2 O) HELIX 1 AA1 ASN B 28 SER B 32 5 5 HELIX 2 AA2 LYS B 87 THR B 91 5 5 HELIX 3 AA3 GLN E 85 VAL E 89 5 5 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 LEU B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA1 4 THR B 78 MET B 83 -1 O LEU B 81 N LEU B 20 SHEET 4 AA1 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA2 6 LEU B 11 VAL B 12 0 SHEET 2 AA2 6 THR B 112 VAL B 116 1 O THR B 115 N VAL B 12 SHEET 3 AA2 6 ALA B 92 SER B 99 -1 N ALA B 92 O VAL B 114 SHEET 4 AA2 6 ASP B 33 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA2 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 THR B 58 TYR B 60 -1 O ASP B 59 N SER B 50 SHEET 1 AA3 4 LEU B 11 VAL B 12 0 SHEET 2 AA3 4 THR B 112 VAL B 116 1 O THR B 115 N VAL B 12 SHEET 3 AA3 4 ALA B 92 SER B 99 -1 N ALA B 92 O VAL B 114 SHEET 4 AA3 4 TYR B 105 TRP B 108 -1 O TYR B 107 N VAL B 98 SHEET 1 AA4 4 MET E 4 SER E 7 0 SHEET 2 AA4 4 ALA E 19 SER E 25 -1 O ASN E 22 N SER E 7 SHEET 3 AA4 4 ASP E 76 ILE E 81 -1 O PHE E 77 N CYS E 23 SHEET 4 AA4 4 PHE E 68 SER E 73 -1 N SER E 69 O THR E 80 SHEET 1 AA5 6 SER E 10 VAL E 13 0 SHEET 2 AA5 6 THR E 108 LEU E 112 1 O GLU E 111 N VAL E 13 SHEET 3 AA5 6 ALA E 90 GLN E 96 -1 N ALA E 90 O LEU E 110 SHEET 4 AA5 6 LEU E 39 GLN E 44 -1 N GLN E 44 O VAL E 91 SHEET 5 AA5 6 LYS E 51 TYR E 55 -1 O LEU E 53 N TRP E 41 SHEET 6 AA5 6 THR E 59 ARG E 60 -1 O THR E 59 N TYR E 55 SHEET 1 AA6 4 SER E 10 VAL E 13 0 SHEET 2 AA6 4 THR E 108 LEU E 112 1 O GLU E 111 N VAL E 13 SHEET 3 AA6 4 ALA E 90 GLN E 96 -1 N ALA E 90 O LEU E 110 SHEET 4 AA6 4 THR E 103 PHE E 104 -1 O THR E 103 N GLN E 96 SSBOND 1 CYS B 22 CYS B 96 1555 1555 1.91 SSBOND 2 CYS E 23 CYS E 94 1555 1555 2.09 CISPEP 1 SER E 7 PRO E 8 0 -14.90 CISPEP 2 HIS E 100 PRO E 101 0 -3.37 CRYST1 38.813 53.544 99.070 90.00 90.00 90.00 P 21 21 21 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 0.025765 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018676 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010094 0.00000