HEADER IMMUNE SYSTEM 22-APR-24 8Z95 TITLE HUMANIZED ANTI-PEG H6.3 FAB IN COMPLEX WITH PEG COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF ANTI-PEG ANTIBODY H6-3 FAB FRAGMENT; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: HEAVY CHAIN; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LIGHT CHAIN OF ANTI-PEG ANTIBODY H6-3 FAB FRAGMENT; COMPND 8 CHAIN: B, L; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: LIGHT CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTI-PEG, FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.C.LIN,C.Y.CHANG,Y.C.SU REVDAT 1 12-FEB-25 8Z95 0 JRNL AUTH J.L.MENG,Z.X.DONG,Y.R.CHEN,M.H.LIN,Y.C.LIU,S.R.ROFFLER, JRNL AUTH 2 W.W.LIN,C.Y.CHANG,S.C.TZOU,T.L.CHENG,H.C.HUANG,Z.Q.LI, JRNL AUTH 3 Y.C.LIN,Y.C.SU JRNL TITL PH-RESPONSIVE POLYETHYLENE GLYCOL ENGAGERS FOR ENHANCED JRNL TITL 2 BRAIN DELIVERY OF PEGYLATED NANOMEDICINE TO TREAT JRNL TITL 3 GLIOBLASTOMA. JRNL REF ACS NANO V. 19 307 2025 JRNL REFN ESSN 1936-086X JRNL PMID 39749925 JRNL DOI 10.1021/ACSNANO.4C05906 REMARK 2 REMARK 2 RESOLUTION. 2.26 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0411 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) : 2.26 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.81 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 48044 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) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.209 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 2611 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) : 2.27 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3387 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.45 REMARK 3 BIN R VALUE (WORKING SET) : 0.2570 REMARK 3 BIN FREE R VALUE SET COUNT : 176 REMARK 3 BIN FREE R VALUE : 0.3200 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6536 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 74 REMARK 3 SOLVENT ATOMS : 180 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.15 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.27000 REMARK 3 B22 (A**2) : -0.09000 REMARK 3 B33 (A**2) : -0.07000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.10000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.276 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.227 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.606 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6776 ; 0.008 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 6224 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9206 ; 1.494 ; 1.652 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14422 ; 0.532 ; 1.591 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 848 ; 8.069 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 20 ;10.565 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1065 ;16.166 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1024 ; 0.064 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7702 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1506 ; 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): 3410 ; 3.172 ; 3.816 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3410 ; 3.172 ; 3.816 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4252 ; 4.761 ; 6.840 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4253 ; 4.761 ; 6.840 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3366 ; 3.426 ; 4.003 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3367 ; 3.426 ; 4.005 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4955 ; 5.308 ; 7.233 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7070 ; 7.160 ;35.880 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7055 ; 7.158 ;35.820 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 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 8Z95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300047055. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-APR-20 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 : NSRRC REMARK 200 BEAMLINE : BL13B1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50690 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.33300 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: MOLREP REMARK 200 STARTING MODEL: 6VL9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 18% (W/V) PEG-6000, 1% (W/V) PEG-2000 REMARK 280 -METHYL ETHER, 0.15 M LITHIUM SULFATE MONOHYDRATE, AND 0.1 M REMARK 280 CITRIC ACID, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 122.68250 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.78700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 122.68250 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.78700 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2970 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL 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 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 LYS A 130 REMARK 465 SER A 131 REMARK 465 THR A 132 REMARK 465 SER A 133 REMARK 465 GLY A 134 REMARK 465 LYS A 215 REMARK 465 SER A 216 REMARK 465 CYS A 217 REMARK 465 ASP A 218 REMARK 465 LYS A 219 REMARK 465 GLU B 218 REMARK 465 CYS B 219 REMARK 465 THR H 132 REMARK 465 SER H 133 REMARK 465 GLY H 134 REMARK 465 SER H 216 REMARK 465 CYS H 217 REMARK 465 ASP H 218 REMARK 465 LYS H 219 REMARK 465 GLY L 217 REMARK 465 GLU L 218 REMARK 465 CYS L 219 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 H 98 NE - CZ - NH2 ANGL. DEV. = -3.3 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 TRP A 100 102.29 72.86 REMARK 500 ALA B 57 -34.89 75.27 REMARK 500 SER B 58 -0.49 -142.54 REMARK 500 ALA B 90 175.78 174.56 REMARK 500 SER B 100 -171.30 56.87 REMARK 500 ASN B 163 15.66 -140.77 REMARK 500 LYS B 195 -64.65 -128.71 REMARK 500 ARG B 216 88.85 -51.20 REMARK 500 TRP H 100 101.39 75.69 REMARK 500 LYS H 130 96.56 -43.14 REMARK 500 ASP H 145 66.65 61.66 REMARK 500 THR H 192 -74.65 -97.56 REMARK 500 ALA L 57 -34.95 76.77 REMARK 500 ALA L 90 175.39 179.56 REMARK 500 SER L 100 -161.05 64.65 REMARK 500 PRO L 146 -163.85 -106.70 REMARK 500 ASN L 157 0.00 81.06 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 98 0.11 SIDE CHAIN REMARK 500 ARG H 98 0.08 SIDE CHAIN REMARK 500 ARG L 18 0.11 SIDE CHAIN REMARK 500 ARG L 60 0.08 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 H 368 DISTANCE = 6.19 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PEU A 301 DBREF 8Z95 A 1 219 PDB 8Z95 8Z95 1 219 DBREF 8Z95 B 1 219 PDB 8Z95 8Z95 1 219 DBREF 8Z95 H 1 219 PDB 8Z95 8Z95 1 219 DBREF 8Z95 L 1 219 PDB 8Z95 8Z95 1 219 SEQRES 1 A 219 GLN VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS SEQRES 2 A 219 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 219 TYR THR PHE THR ASN TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 A 219 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 A 219 THR TYR THR GLY GLN PRO ILE TYR ALA ASN ASP PHE LYS SEQRES 6 A 219 GLY ARG PHE VAL PHE SER LEU ASP THR SER VAL SER THR SEQRES 7 A 219 ALA TYR LEU GLN ILE SER SER LEU LYS ALA GLU ASP THR SEQRES 8 A 219 ALA VAL TYR TYR CYS ALA ARG ASP TRP GLY PRO TYR TRP SEQRES 9 A 219 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 10 A 219 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 A 219 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 A 219 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 A 219 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 A 219 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 A 219 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 A 219 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 A 219 ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS SEQRES 1 B 219 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 B 219 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 B 219 GLN SER VAL LEU TYR SER SER ASN GLN MET ASN TYR LEU SEQRES 4 B 219 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 B 219 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 B 219 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 B 219 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 B 219 TYR TYR CYS LEU GLN TYR LEU SER SER TRP THR PHE GLY SEQRES 9 B 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 B 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 B 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 B 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 B 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 B 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 B 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 B 219 LEU TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 B 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 219 GLN VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS SEQRES 2 H 219 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 219 TYR THR PHE THR ASN TYR GLY MET ASN TRP VAL ARG GLN SEQRES 4 H 219 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 219 THR TYR THR GLY GLN PRO ILE TYR ALA ASN ASP PHE LYS SEQRES 6 H 219 GLY ARG PHE VAL PHE SER LEU ASP THR SER VAL SER THR SEQRES 7 H 219 ALA TYR LEU GLN ILE SER SER LEU LYS ALA GLU ASP THR SEQRES 8 H 219 ALA VAL TYR TYR CYS ALA ARG ASP TRP GLY PRO TYR TRP SEQRES 9 H 219 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 10 H 219 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 H 219 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 H 219 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 H 219 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 H 219 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 H 219 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 H 219 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 H 219 ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS SEQRES 1 L 219 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 L 219 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 L 219 GLN SER VAL LEU TYR SER SER ASN GLN MET ASN TYR LEU SEQRES 4 L 219 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 219 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 219 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 219 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 L 219 TYR TYR CYS LEU GLN TYR LEU SER SER TRP THR PHE GLY SEQRES 9 L 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 LEU TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET PEU A 301 70 HET IPA B 301 4 HETNAM PEU 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56, HETNAM 2 PEU 59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL HETNAM IPA ISOPROPYL ALCOHOL HETSYN PEU PEG 8000 HETSYN IPA 2-PROPANOL FORMUL 5 PEU C55 H112 O28 FORMUL 6 IPA C3 H8 O FORMUL 7 HOH *180(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASN A 62 LYS A 65 5 4 HELIX 3 AA3 THR A 74 VAL A 76 5 3 HELIX 4 AA4 LYS A 87 THR A 91 5 5 HELIX 5 AA5 SER A 188 GLN A 193 1 6 HELIX 6 AA6 LYS A 202 ASN A 205 5 4 HELIX 7 AA7 GLN B 85 VAL B 89 5 5 HELIX 8 AA8 SER B 126 GLY B 133 1 8 HELIX 9 AA9 LYS B 188 LYS B 193 1 6 HELIX 10 AB1 THR H 28 TYR H 32 5 5 HELIX 11 AB2 THR H 74 VAL H 76 5 3 HELIX 12 AB3 LYS H 87 THR H 91 5 5 HELIX 13 AB4 SER H 157 ALA H 159 5 3 HELIX 14 AB5 SER H 188 LEU H 190 5 3 HELIX 15 AB6 LYS H 202 ASN H 205 5 4 HELIX 16 AB7 GLN L 85 VAL L 89 5 5 HELIX 17 AB8 SER L 126 SER L 132 1 7 HELIX 18 AB9 LYS L 188 LYS L 193 1 6 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 ILE A 83 -1 O LEU A 81 N VAL A 20 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA2 6 GLU A 10 LYS A 12 0 SHEET 2 AA2 6 THR A 108 VAL A 112 1 O THR A 111 N LYS A 12 SHEET 3 AA2 6 ALA A 92 ARG A 98 -1 N ALA A 92 O VAL A 110 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 GLU A 46 ILE A 51 -1 O MET A 48 N TRP A 36 SHEET 6 AA2 6 PRO A 58 TYR A 60 -1 O ILE A 59 N TRP A 50 SHEET 1 AA3 4 SER A 121 LEU A 125 0 SHEET 2 AA3 4 THR A 136 TYR A 146 -1 O LEU A 142 N PHE A 123 SHEET 3 AA3 4 TYR A 177 PRO A 186 -1 O LEU A 179 N VAL A 143 SHEET 4 AA3 4 VAL A 164 THR A 166 -1 N HIS A 165 O VAL A 182 SHEET 1 AA4 4 SER A 121 LEU A 125 0 SHEET 2 AA4 4 THR A 136 TYR A 146 -1 O LEU A 142 N PHE A 123 SHEET 3 AA4 4 TYR A 177 PRO A 186 -1 O LEU A 179 N VAL A 143 SHEET 4 AA4 4 VAL A 170 LEU A 171 -1 N VAL A 170 O SER A 178 SHEET 1 AA5 3 THR A 152 TRP A 155 0 SHEET 2 AA5 3 ILE A 196 HIS A 201 -1 O ASN A 200 N THR A 152 SHEET 3 AA5 3 THR A 206 ARG A 211 -1 O VAL A 208 N VAL A 199 SHEET 1 AA6 4 MET B 4 SER B 7 0 SHEET 2 AA6 4 ALA B 19 SER B 25 -1 O ASN B 22 N SER B 7 SHEET 3 AA6 4 ASP B 76 ILE B 81 -1 O ILE B 81 N ALA B 19 SHEET 4 AA6 4 PHE B 68 SER B 73 -1 N SER B 69 O THR B 80 SHEET 1 AA7 6 SER B 10 SER B 14 0 SHEET 2 AA7 6 THR B 107 LYS B 112 1 O GLU B 110 N LEU B 11 SHEET 3 AA7 6 ALA B 90 GLN B 96 -1 N ALA B 90 O LEU B 109 SHEET 4 AA7 6 LEU B 39 GLN B 44 -1 N GLN B 44 O VAL B 91 SHEET 5 AA7 6 LYS B 51 TYR B 55 -1 O LEU B 53 N TRP B 41 SHEET 6 AA7 6 THR B 59 ARG B 60 -1 O THR B 59 N TYR B 55 SHEET 1 AA8 4 SER B 10 SER B 14 0 SHEET 2 AA8 4 THR B 107 LYS B 112 1 O GLU B 110 N LEU B 11 SHEET 3 AA8 4 ALA B 90 GLN B 96 -1 N ALA B 90 O LEU B 109 SHEET 4 AA8 4 THR B 102 PHE B 103 -1 O THR B 102 N GLN B 96 SHEET 1 AA9 4 SER B 119 PHE B 123 0 SHEET 2 AA9 4 THR B 134 PHE B 144 -1 O LEU B 140 N PHE B 121 SHEET 3 AA9 4 TYR B 178 SER B 187 -1 O LEU B 186 N ALA B 135 SHEET 4 AA9 4 SER B 164 VAL B 168 -1 N SER B 167 O SER B 181 SHEET 1 AB1 4 ALA B 158 LEU B 159 0 SHEET 2 AB1 4 LYS B 150 VAL B 155 -1 N VAL B 155 O ALA B 158 SHEET 3 AB1 4 LEU B 196 THR B 202 -1 O GLU B 200 N GLN B 152 SHEET 4 AB1 4 VAL B 210 ASN B 215 -1 O PHE B 214 N TYR B 197 SHEET 1 AB2 4 GLN H 3 GLN H 6 0 SHEET 2 AB2 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AB2 4 THR H 78 ILE H 83 -1 O LEU H 81 N VAL H 20 SHEET 4 AB2 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB3 6 GLU H 10 LYS H 12 0 SHEET 2 AB3 6 THR H 108 VAL H 112 1 O THR H 111 N LYS H 12 SHEET 3 AB3 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 110 SHEET 4 AB3 6 MET H 34 GLN H 39 -1 N GLN H 39 O VAL H 93 SHEET 5 AB3 6 GLU H 46 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AB3 6 PRO H 58 TYR H 60 -1 O ILE H 59 N TRP H 50 SHEET 1 AB4 4 SER H 121 LEU H 125 0 SHEET 2 AB4 4 THR H 136 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AB4 4 TYR H 177 PRO H 186 -1 O LEU H 179 N VAL H 143 SHEET 4 AB4 4 VAL H 164 THR H 166 -1 N HIS H 165 O VAL H 182 SHEET 1 AB5 4 SER H 121 LEU H 125 0 SHEET 2 AB5 4 THR H 136 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AB5 4 TYR H 177 PRO H 186 -1 O LEU H 179 N VAL H 143 SHEET 4 AB5 4 VAL H 170 LEU H 171 -1 N VAL H 170 O SER H 178 SHEET 1 AB6 3 THR H 152 TRP H 155 0 SHEET 2 AB6 3 ILE H 196 HIS H 201 -1 O ASN H 200 N THR H 152 SHEET 3 AB6 3 THR H 206 ARG H 211 -1 O VAL H 208 N VAL H 199 SHEET 1 AB7 4 MET L 4 SER L 7 0 SHEET 2 AB7 4 ALA L 19 SER L 25 -1 O ASN L 22 N SER L 7 SHEET 3 AB7 4 ASP L 76 ILE L 81 -1 O LEU L 79 N ILE L 21 SHEET 4 AB7 4 PHE L 68 SER L 73 -1 N SER L 69 O THR L 80 SHEET 1 AB8 6 SER L 10 VAL L 13 0 SHEET 2 AB8 6 THR L 107 ILE L 111 1 O GLU L 110 N LEU L 11 SHEET 3 AB8 6 ALA L 90 GLN L 96 -1 N ALA L 90 O LEU L 109 SHEET 4 AB8 6 LEU L 39 GLN L 44 -1 N GLN L 44 O VAL L 91 SHEET 5 AB8 6 LYS L 51 TYR L 55 -1 O LYS L 51 N GLN L 43 SHEET 6 AB8 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55 SHEET 1 AB9 4 SER L 10 VAL L 13 0 SHEET 2 AB9 4 THR L 107 ILE L 111 1 O GLU L 110 N LEU L 11 SHEET 3 AB9 4 ALA L 90 GLN L 96 -1 N ALA L 90 O LEU L 109 SHEET 4 AB9 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 96 SHEET 1 AC1 4 SER L 119 PHE L 123 0 SHEET 2 AC1 4 THR L 134 PHE L 144 -1 O VAL L 138 N PHE L 123 SHEET 3 AC1 4 TYR L 178 SER L 187 -1 O TYR L 178 N PHE L 144 SHEET 4 AC1 4 SER L 164 VAL L 168 -1 N GLN L 165 O THR L 183 SHEET 1 AC2 4 ALA L 158 LEU L 159 0 SHEET 2 AC2 4 ALA L 149 VAL L 155 -1 N VAL L 155 O ALA L 158 SHEET 3 AC2 4 LEU L 196 HIS L 203 -1 O GLU L 200 N GLN L 152 SHEET 4 AC2 4 VAL L 210 ASN L 215 -1 O VAL L 210 N VAL L 201 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05 SSBOND 2 CYS A 141 CYS A 197 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 94 1555 1555 2.22 SSBOND 4 CYS B 139 CYS B 199 1555 1555 2.08 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.09 SSBOND 6 CYS H 141 CYS H 197 1555 1555 2.04 SSBOND 7 CYS L 23 CYS L 94 1555 1555 2.23 SSBOND 8 CYS L 139 CYS L 199 1555 1555 2.06 CISPEP 1 PHE A 147 PRO A 148 0 -11.77 CISPEP 2 GLU A 149 PRO A 150 0 -7.52 CISPEP 3 SER B 7 PRO B 8 0 -6.89 CISPEP 4 TYR B 145 PRO B 146 0 -6.87 CISPEP 5 PHE H 147 PRO H 148 0 -12.31 CISPEP 6 GLU H 149 PRO H 150 0 -2.36 CISPEP 7 SER L 7 PRO L 8 0 -6.70 CISPEP 8 TYR L 145 PRO L 146 0 13.67 CRYST1 245.365 43.574 110.148 90.00 111.70 90.00 C 1 2 1 8 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 0.004076 0.000000 0.001622 0.00000 SCALE2 0.000000 0.022949 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009771 0.00000