HEADER CARBOHYDRATE 26-JAN-22 7QXD TITLE RECOGNITION OF STAPHYLOCOCCUS AUREUS WALL TEICHOIC ACID ANALOGUE SA475 TITLE 2 (COMPOUND 2) BY FAB4497 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY FAB 4497 HEAVY CHAIN; COMPND 3 CHAIN: HHH, KKK; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY FAB 4497 LIGHT CHAIN; COMPND 7 CHAIN: LLL, MMM; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, FAB FRAGMENT, TEICHOIC ACID ANALOGUE, CARBOHYDRATE EXPDTA X-RAY DIFFRACTION AUTHOR P.SORIANO-MALDONADO,M.J.VAN RAAIJ JRNL AUTH C.DI CARLUCCIO,P.SORIANO MALDONADO,F.BERNI,C.J.C.DE HAAS, JRNL AUTH 2 A.R.TEMMING,A.HENDRIKS,S.ALI,A.MOLINARO,A.SILIPO, JRNL AUTH 3 N.M.VAN SORGE,M.J.VAN RAAIJ,J.D.C.CODEE,R.MARCHETTI JRNL TITL ANTIBODY RECOGNITION OF DIFFERENT STAPHYLOCOCCUS AUREUS WALL JRNL TITL 2 TEICHOIC ACID GLYCOFORMS JRNL REF ACS CENT.SCI. 2022 JRNL REFN ESSN 2374-7951 JRNL DOI 10.1021/ACSCENTSCI.2C00125 REMARK 2 REMARK 2 RESOLUTION. 1.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 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) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.02 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0 REMARK 3 NUMBER OF REFLECTIONS : 127097 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 : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.175 REMARK 3 FREE R VALUE : 0.202 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.947 REMARK 3 FREE R VALUE TEST SET COUNT : 6287 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74 REMARK 3 REFLECTION IN BIN (WORKING SET) : 18773 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99 REMARK 3 BIN R VALUE (WORKING SET) : 0.2920 REMARK 3 BIN FREE R VALUE SET COUNT : 962 REMARK 3 BIN FREE R VALUE : 0.2990 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6636 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 125 REMARK 3 SOLVENT ATOMS : 818 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.74700 REMARK 3 B22 (A**2) : -0.59000 REMARK 3 B33 (A**2) : -0.15700 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): 0.087 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.002 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6956 ; 0.010 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6364 ; 0.001 ; 0.015 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9471 ; 1.548 ; 1.649 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14730 ; 1.394 ; 1.577 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 875 ; 7.670 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 324 ;34.184 ;22.593 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1097 ;13.049 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;22.830 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 927 ; 0.069 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7843 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1595 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1025 ; 0.196 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 75 ; 0.180 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3329 ; 0.164 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 602 ; 0.174 ; 0.200 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): 3475 ; 2.166 ; 2.478 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3474 ; 2.161 ; 2.477 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4337 ; 3.239 ; 3.699 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4338 ; 3.238 ; 3.700 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3481 ; 3.150 ; 2.805 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3474 ; 3.123 ; 2.800 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5127 ; 4.859 ; 4.041 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5116 ; 4.832 ; 4.032 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : HHH KKK REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 HH 1 HH 216 NULL REMARK 3 2 KK 1 KK 216 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : LLL MMM REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 LL 1 LL 219 NULL REMARK 3 4 MM 1 MM 219 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT 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 7QXD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292120542. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JUN-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 : ALBA REMARK 200 BEAMLINE : XALOC REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933 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 JAN 31, 2020 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127285 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.649 REMARK 200 RESOLUTION RANGE LOW (A) : 91.410 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.07700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : 1.04700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: REFMAC 5.8.0258 REMARK 200 STARTING MODEL: PDB ENTRY 5D6C REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM 2-(N-MORPHOLINO)ETHANESULFONIC REMARK 280 ACID-NAOH PH 6.2, 0.25 M SODIUM CHLORIDE, 20% (W/V) POLY- REMARK 280 ETHYLENE GLYCOL 4000, 10% (V/V) GLYCEROL, 200 MM MAGNESIUM REMARK 280 SULPHATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K 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 32.19600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.27850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.68550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.27850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.19600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.68550 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: 4300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: HHH, LLL 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: 4240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: KKK, MMM 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 SER H 133 REMARK 465 THR H 134 REMARK 465 SER H 135 REMARK 465 SER H 218 REMARK 465 CYS H 219 REMARK 465 GLY H 220 REMARK 465 GLY H 221 REMARK 465 GLY H 222 REMARK 465 GLY H 223 REMARK 465 SER H 224 REMARK 465 LEU H 225 REMARK 465 PRO H 226 REMARK 465 GLU H 227 REMARK 465 THR H 228 REMARK 465 GLY H 229 REMARK 465 GLY H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 CYS L 220 REMARK 465 SER K 133 REMARK 465 THR K 134 REMARK 465 SER K 135 REMARK 465 CYS K 219 REMARK 465 GLY K 220 REMARK 465 GLY K 221 REMARK 465 GLY K 222 REMARK 465 GLY K 223 REMARK 465 SER K 224 REMARK 465 LEU K 225 REMARK 465 PRO K 226 REMARK 465 GLU K 227 REMARK 465 THR K 228 REMARK 465 GLY K 229 REMARK 465 GLY K 230 REMARK 465 HIS K 231 REMARK 465 HIS K 232 REMARK 465 HIS K 233 REMARK 465 HIS K 234 REMARK 465 HIS K 235 REMARK 465 HIS K 236 REMARK 465 CYS M 220 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 N REMARK 470 SER H 130 OG 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 HOHKK 570 O HOHMM 485 1.90 REMARK 500 O HOHKK 456 O HOHKK 570 2.01 REMARK 500 OD1 ASPKK 104 NH2 ARGMM 51 2.08 REMARK 500 O HOHLL 538 O HOHLL 557 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O SERLL 33 OG SERKK 31 3544 2.10 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 ARGLL 31 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 ARGMM 148 NE - CZ - NH1 ANGL. DEV. = 3.0 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 ASPHH 100 -121.77 -118.44 REMARK 500 ASPHH 100 -120.09 -120.47 REMARK 500 ASPHH 147 67.15 68.66 REMARK 500 ALALL 57 -39.93 72.38 REMARK 500 ASPKK 100 -119.04 -118.45 REMARK 500 ASPKK 147 65.75 70.36 REMARK 500 ALAMM 57 -37.41 72.51 REMARK 500 ASNMM 158 -7.60 81.11 REMARK 500 REMARK 500 REMARK: NULL DBREF 7QXDHH 1 236 PDB 7QXD 7QXD 1 236 DBREF 7QXDLL 1 220 PDB 7QXD 7QXD 1 220 DBREF 7QXDKK 1 236 PDB 7QXD 7QXD 1 236 DBREF 7QXDMM 1 220 PDB 7QXD 7QXD 1 220 SEQRES 1HH 236 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2HH 236 PRO GLY GLY SER LEU ARG LEU SER CYS SER ALA SER GLY SEQRES 3HH 236 PHE SER PHE ASN SER PHE TRP MET HIS TRP VAL ARG GLN SEQRES 4HH 236 VAL PRO GLY LYS GLY LEU VAL TRP ILE SER PHE THR ASN SEQRES 5HH 236 ASN GLU GLY THR THR THR ALA TYR ALA ASP SER VAL ARG SEQRES 6HH 236 GLY ARG PHE ILE ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7HH 236 LEU TYR LEU GLU MET ASN ASN LEU ARG GLY GLU ASP THR SEQRES 8HH 236 ALA VAL TYR TYR CYS ALA ARG GLY ASP GLY GLY LEU ASP SEQRES 9HH 236 ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10HH 236 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11HH 236 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12HH 236 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13HH 236 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14HH 236 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15HH 236 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16HH 236 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17HH 236 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY GLY SEQRES 18HH 236 GLY GLY SER LEU PRO GLU THR GLY GLY HIS HIS HIS HIS SEQRES 19HH 236 HIS HIS SEQRES 1LL 220 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2LL 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3LL 220 GLN SER ILE PHE ARG THR SER ARG ASN LYS ASN LEU LEU SEQRES 4LL 220 ASN TRP TYR GLN GLN ARG PRO GLY GLN PRO PRO ARG LEU SEQRES 5LL 220 LEU ILE HIS TRP ALA SER THR ARG LYS SER GLY VAL PRO SEQRES 6LL 220 ASP ARG PHE SER GLY SER GLY PHE GLY THR ASP PHE THR SEQRES 7LL 220 LEU THR ILE THR SER LEU GLN ALA GLU ASP VAL ALA ILE SEQRES 8LL 220 TYR TYR CYS GLN GLN TYR PHE SER PRO PRO TYR THR PHE SEQRES 9LL 220 GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA SEQRES 10LL 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11LL 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12LL 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13LL 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14LL 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15LL 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16LL 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17LL 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1KK 236 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2KK 236 PRO GLY GLY SER LEU ARG LEU SER CYS SER ALA SER GLY SEQRES 3KK 236 PHE SER PHE ASN SER PHE TRP MET HIS TRP VAL ARG GLN SEQRES 4KK 236 VAL PRO GLY LYS GLY LEU VAL TRP ILE SER PHE THR ASN SEQRES 5KK 236 ASN GLU GLY THR THR THR ALA TYR ALA ASP SER VAL ARG SEQRES 6KK 236 GLY ARG PHE ILE ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7KK 236 LEU TYR LEU GLU MET ASN ASN LEU ARG GLY GLU ASP THR SEQRES 8KK 236 ALA VAL TYR TYR CYS ALA ARG GLY ASP GLY GLY LEU ASP SEQRES 9KK 236 ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10KK 236 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11KK 236 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12KK 236 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13KK 236 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14KK 236 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15KK 236 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16KK 236 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17KK 236 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY GLY SEQRES 18KK 236 GLY GLY SER LEU PRO GLU THR GLY GLY HIS HIS HIS HIS SEQRES 19KK 236 HIS HIS SEQRES 1MM 220 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2MM 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3MM 220 GLN SER ILE PHE ARG THR SER ARG ASN LYS ASN LEU LEU SEQRES 4MM 220 ASN TRP TYR GLN GLN ARG PRO GLY GLN PRO PRO ARG LEU SEQRES 5MM 220 LEU ILE HIS TRP ALA SER THR ARG LYS SER GLY VAL PRO SEQRES 6MM 220 ASP ARG PHE SER GLY SER GLY PHE GLY THR ASP PHE THR SEQRES 7MM 220 LEU THR ILE THR SER LEU GLN ALA GLU ASP VAL ALA ILE SEQRES 8MM 220 TYR TYR CYS GLN GLN TYR PHE SER PRO PRO TYR THR PHE SEQRES 9MM 220 GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA SEQRES 10MM 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11MM 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12MM 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13MM 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14MM 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15MM 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16MM 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17MM 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET G5F HH 301 47 HET GOL LL 301 6 HET SO4 LL 302 5 HET PEG KK 301 7 HET GOL KK 302 6 HET G5F MM 301 49 HET SO4 MM 302 5 HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 G5F FORMUL 6 GOL 2(C3 H8 O3) FORMUL 7 SO4 2(O4 S 2-) FORMUL 8 PEG C4 H10 O3 FORMUL 12 HOH *818(H2 O) HELIX 1 AA1 SERHH 28 PHEHH 32 5 5 HELIX 2 AA2 ASNHH 74 LYSHH 76 5 3 HELIX 3 AA3 ARGHH 87 THRHH 91 5 5 HELIX 4 AA4 SERHH 159 ALAHH 161 5 3 HELIX 5 AA5 SERHH 190 LEUHH 192 5 3 HELIX 6 AA6 LYSHH 204 ASNHH 207 5 4 HELIX 7 AA7 THRLL 32 ASNLL 35 5 4 HELIX 8 AA8 GLNLL 85 VALLL 89 5 5 HELIX 9 AA9 SERLL 127 SERLL 133 1 7 HELIX 10 AB1 LYSLL 189 LYSLL 194 1 6 HELIX 11 AB2 SERKK 28 PHEKK 32 5 5 HELIX 12 AB3 ASNKK 74 LYSKK 76 5 3 HELIX 13 AB4 ARGKK 87 THRKK 91 5 5 HELIX 14 AB5 SERKK 159 ALAKK 161 5 3 HELIX 15 AB6 SERKK 190 LEUKK 192 5 3 HELIX 16 AB7 LYSKK 204 ASNKK 207 5 4 HELIX 17 AB8 THRMM 32 ASNMM 35 5 4 HELIX 18 AB9 GLNMM 85 VALMM 89 5 5 HELIX 19 AC1 SERMM 127 LYSMM 132 1 6 HELIX 20 AC2 LYSMM 189 LYSMM 194 1 6 SHEET 1 AA1 4 GLNHH 3 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O SERHH 23 N VALHH 5 SHEET 3 AA1 4 THRHH 78 METHH 83 -1 O LEUHH 81 N LEUHH 20 SHEET 4 AA1 4 PHEHH 68 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AA2 6 LEUHH 11 VALHH 12 0 SHEET 2 AA2 6 THRHH 110 VALHH 114 1 O THRHH 113 N VALHH 12 SHEET 3 AA2 6 ALAHH 92 GLYHH 99 -1 N ALAHH 92 O VALHH 112 SHEET 4 AA2 6 METHH 34 GLNHH 39 -1 N VALHH 37 O TYRHH 95 SHEET 5 AA2 6 LEUHH 45 THRHH 51 -1 O VALHH 46 N ARGHH 38 SHEET 6 AA2 6 THRHH 58 TYRHH 60 -1 O ALAHH 59 N PHEHH 50 SHEET 1 AA3 4 LEUHH 11 VALHH 12 0 SHEET 2 AA3 4 THRHH 110 VALHH 114 1 O THRHH 113 N VALHH 12 SHEET 3 AA3 4 ALAHH 92 GLYHH 99 -1 N ALAHH 92 O VALHH 112 SHEET 4 AA3 4 LEUHH 103 ASPHH 104 -1 O ASPHH 104 N ARGHH 98 SHEET 1 AA4 4 SERHH 123 LEUHH 127 0 SHEET 2 AA4 4 THRHH 138 TYRHH 148 -1 O GLYHH 142 N LEUHH 127 SHEET 3 AA4 4 TYRHH 179 PROHH 188 -1 O LEUHH 181 N VALHH 145 SHEET 4 AA4 4 VALHH 166 THRHH 168 -1 N HISHH 167 O VALHH 184 SHEET 1 AA5 4 SERHH 123 LEUHH 127 0 SHEET 2 AA5 4 THRHH 138 TYRHH 148 -1 O GLYHH 142 N LEUHH 127 SHEET 3 AA5 4 TYRHH 179 PROHH 188 -1 O LEUHH 181 N VALHH 145 SHEET 4 AA5 4 VALHH 172 LEUHH 173 -1 N VALHH 172 O SERHH 180 SHEET 1 AA6 3 THRHH 154 TRPHH 157 0 SHEET 2 AA6 3 TYRHH 197 HISHH 203 -1 O ASNHH 200 N SERHH 156 SHEET 3 AA6 3 THRHH 208 VALHH 214 -1 O VALHH 210 N VALHH 201 SHEET 1 AA7 4 LEULL 4 SERLL 7 0 SHEET 2 AA7 4 ALALL 19 SERLL 25 -1 O ASNLL 22 N SERLL 7 SHEET 3 AA7 4 ASPLL 76 ILELL 81 -1 O LEULL 79 N ILELL 21 SHEET 4 AA7 4 PHELL 68 PHELL 73 -1 N SERLL 69 O THRLL 80 SHEET 1 AA8 6 SERLL 10 SERLL 14 0 SHEET 2 AA8 6 THRLL 108 LYSLL 113 1 O GLULL 111 N LEULL 11 SHEET 3 AA8 6 ALALL 90 GLNLL 96 -1 N TYRLL 92 O THRLL 108 SHEET 4 AA8 6 LEULL 39 GLNLL 44 -1 N ASNLL 40 O GLNLL 95 SHEET 5 AA8 6 ARGLL 51 HISLL 55 -1 O LEULL 53 N TRPLL 41 SHEET 6 AA8 6 THRLL 59 ARGLL 60 -1 O THRLL 59 N HISLL 55 SHEET 1 AA9 2 PHELL 30 ARGLL 31 0 SHEET 2 AA9 2 LYSLL 36 ASNLL 37 -1 O LYSLL 36 N ARGLL 31 SHEET 1 AB1 4 SERLL 120 PHELL 124 0 SHEET 2 AB1 4 THRLL 135 PHELL 145 -1 O ASNLL 143 N SERLL 120 SHEET 3 AB1 4 TYRLL 179 SERLL 188 -1 O SERLL 183 N CYSLL 140 SHEET 4 AB1 4 SERLL 165 VALLL 169 -1 N GLNLL 166 O THRLL 184 SHEET 1 AB2 4 ALALL 159 LEULL 160 0 SHEET 2 AB2 4 LYSLL 151 VALLL 156 -1 N VALLL 156 O ALALL 159 SHEET 3 AB2 4 VALLL 197 THRLL 203 -1 O GLULL 201 N GLNLL 153 SHEET 4 AB2 4 VALLL 211 ASNLL 216 -1 O VALLL 211 N VALLL 202 SHEET 1 AB3 4 GLNKK 3 SERKK 7 0 SHEET 2 AB3 4 LEUKK 18 SERKK 25 -1 O SERKK 23 N VALKK 5 SHEET 3 AB3 4 THRKK 78 METKK 83 -1 O LEUKK 81 N LEUKK 20 SHEET 4 AB3 4 PHEKK 68 ASPKK 73 -1 N SERKK 71 O TYRKK 80 SHEET 1 AB4 6 GLYKK 10 VALKK 12 0 SHEET 2 AB4 6 THRKK 110 VALKK 114 1 O THRKK 113 N VALKK 12 SHEET 3 AB4 6 ALAKK 92 GLYKK 99 -1 N TYRKK 94 O THRKK 110 SHEET 4 AB4 6 METKK 34 GLNKK 39 -1 N VALKK 37 O TYRKK 95 SHEET 5 AB4 6 LEUKK 45 THRKK 51 -1 O VALKK 46 N ARGKK 38 SHEET 6 AB4 6 THRKK 58 TYRKK 60 -1 O ALAKK 59 N PHEKK 50 SHEET 1 AB5 4 GLYKK 10 VALKK 12 0 SHEET 2 AB5 4 THRKK 110 VALKK 114 1 O THRKK 113 N VALKK 12 SHEET 3 AB5 4 ALAKK 92 GLYKK 99 -1 N TYRKK 94 O THRKK 110 SHEET 4 AB5 4 LEUKK 103 ASPKK 104 -1 O ASPKK 104 N ARGKK 98 SHEET 1 AB6 4 SERKK 123 LEUKK 127 0 SHEET 2 AB6 4 THRKK 138 TYRKK 148 -1 O GLYKK 142 N LEUKK 127 SHEET 3 AB6 4 TYRKK 179 PROKK 188 -1 O LEUKK 181 N VALKK 145 SHEET 4 AB6 4 VALKK 166 THRKK 168 -1 N HISKK 167 O VALKK 184 SHEET 1 AB7 4 SERKK 123 LEUKK 127 0 SHEET 2 AB7 4 THRKK 138 TYRKK 148 -1 O GLYKK 142 N LEUKK 127 SHEET 3 AB7 4 TYRKK 179 PROKK 188 -1 O LEUKK 181 N VALKK 145 SHEET 4 AB7 4 VALKK 172 LEUKK 173 -1 N VALKK 172 O SERKK 180 SHEET 1 AB8 3 THRKK 154 TRPKK 157 0 SHEET 2 AB8 3 ILEKK 198 HISKK 203 -1 O ASNKK 200 N SERKK 156 SHEET 3 AB8 3 THRKK 208 LYSKK 213 -1 O VALKK 210 N VALKK 201 SHEET 1 AB9 4 LEUMM 4 SERMM 7 0 SHEET 2 AB9 4 ALAMM 19 SERMM 25 -1 O ASNMM 22 N SERMM 7 SHEET 3 AB9 4 ASPMM 76 ILEMM 81 -1 O LEUMM 79 N ILEMM 21 SHEET 4 AB9 4 PHEMM 68 PHEMM 73 -1 N SERMM 69 O THRMM 80 SHEET 1 AC1 6 SERMM 10 SERMM 14 0 SHEET 2 AC1 6 THRMM 108 LYSMM 113 1 O GLUMM 111 N LEUMM 11 SHEET 3 AC1 6 ALAMM 90 GLNMM 96 -1 N ALAMM 90 O LEUMM 110 SHEET 4 AC1 6 LEUMM 39 GLNMM 44 -1 N ASNMM 40 O GLNMM 95 SHEET 5 AC1 6 ARGMM 51 HISMM 55 -1 O LEUMM 53 N TRPMM 41 SHEET 6 AC1 6 THRMM 59 ARGMM 60 -1 O THRMM 59 N HISMM 55 SHEET 1 AC2 2 PHEMM 30 ARGMM 31 0 SHEET 2 AC2 2 LYSMM 36 ASNMM 37 -1 O LYSMM 36 N ARGMM 31 SHEET 1 AC3 4 SERMM 120 PHEMM 124 0 SHEET 2 AC3 4 THRMM 135 PHEMM 145 -1 O ASNMM 143 N SERMM 120 SHEET 3 AC3 4 TYRMM 179 SERMM 188 -1 O LEUMM 185 N VALMM 138 SHEET 4 AC3 4 SERMM 165 VALMM 169 -1 N GLNMM 166 O THRMM 184 SHEET 1 AC4 4 ALAMM 159 GLNMM 161 0 SHEET 2 AC4 4 LYSMM 151 VALMM 156 -1 N TRPMM 154 O GLNMM 161 SHEET 3 AC4 4 VALMM 197 THRMM 203 -1 O GLUMM 201 N GLNMM 153 SHEET 4 AC4 4 VALMM 211 ASNMM 216 -1 O VALMM 211 N VALMM 202 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.14 SSBOND 2 CYSHH 143 CYSHH 199 1555 1555 2.05 SSBOND 3 CYSLL 23 CYSLL 94 1555 1555 2.19 SSBOND 4 CYSLL 140 CYSLL 200 1555 1555 2.03 SSBOND 5 CYSKK 22 CYSKK 96 1555 1555 2.11 SSBOND 6 CYSKK 143 CYSKK 199 1555 1555 2.06 SSBOND 7 CYSMM 23 CYSMM 94 1555 1555 2.17 SSBOND 8 CYSMM 140 CYSMM 200 1555 1555 2.01 CISPEP 1 PHEHH 149 PROHH 150 0 -8.61 CISPEP 2 GLUHH 151 PROHH 152 0 -5.78 CISPEP 3 SERLL 7 PROLL 8 0 0.55 CISPEP 4 PROLL 100 PROLL 101 0 -1.83 CISPEP 5 TYRLL 146 PROLL 147 0 -0.38 CISPEP 6 PHEKK 149 PROKK 150 0 -9.11 CISPEP 7 GLUKK 151 PROKK 152 0 -4.07 CISPEP 8 GLUKK 151 PROKK 152 0 -3.95 CISPEP 9 SERMM 7 PROMM 8 0 -5.36 CISPEP 10 PROMM 100 PROMM 101 0 0.99 CISPEP 11 TYRMM 146 PROMM 147 0 -1.07 CRYST1 64.392 113.371 154.557 90.00 90.00 90.00 P 21 21 21 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 0.015530 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008821 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006470 0.00000