HEADER PROTEIN BINDING 06-SEP-19 6SS0 TITLE STRUCTURE OF THE ARGINASE-2-INHIBITORY HUMAN ANTIGEN-BINDING FRAGMENT TITLE 2 FAB C0021181 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB C0021181 HEAVY CHAIN (IGG1); COMPND 3 CHAIN: HHH, III; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 6 NUMBERING SCHEME.; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB C0021181 LIGHT CHAIN (IGG1); COMPND 9 CHAIN: LLL, MMM; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 12 NUMBERING SCHEME. RESIDUE 10 WOULD NOT BE PRESENT IN THE KABAT COMPND 13 SCHEME, BUT DUE TO PROBLEMS WITH NON-CONTINUOUS NUMBERING IN L- COMPND 14 PEPTIDES, WE INCLUDED IT. THEREFORE, RESIDUES 2-10 SHOULD BE READ AS COMPND 15 1-9, PER KABAT. 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 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB KEYWDS ARGINASE-2 INHIBITOR, IGG, ANTIGEN-BINDING FRAGMENT, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR D.BURSCHOWSKY,A.ADDYMAN,S.FIEDLER,M.GROVES,S.HAYNES,C.SEEWOORUTHUN, AUTHOR 2 M.CARR JRNL AUTH M.AUSTIN,D.BURSCHOWSKY,D.T.Y.CHAN,L.JENKINSON,S.HAYNES, JRNL AUTH 2 A.DIAMANDAKIS,C.SEEWOORUTHUN,A.ADDYMAN,S.FIEDLER,S.RYMAN, JRNL AUTH 3 J.WHITEHOUSE,L.H.SLATER,A.V.HADJINICOLAOU,U.GILEADI, JRNL AUTH 4 E.GOWANS,Y.SHIBATA,M.BARNARD,T.KASERER,P.SHARMA,N.M.LUHESHI, JRNL AUTH 5 R.W.WILKINSON,T.J.VAUGHAN,S.V.HOLT,V.CERUNDOLO,M.D.CARR, JRNL AUTH 6 M.A.T.GROVES JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF C0021158, A JRNL TITL 2 HIGH-AFFINITY MONOCLONAL ANTIBODY THAT INHIBITS ARGINASE 2 JRNL TITL 3 FUNCTION VIA A NOVEL NON-COMPETITIVE MECHANISM OF ACTION. JRNL REF MABS V. 12 01230 JRNL REFN ESSN 1942-0870 JRNL PMID 32880207 JRNL DOI 10.1080/19420862.2020.1801230 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0253 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) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.54 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 88772 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) : 0.189 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.062 REMARK 3 FREE R VALUE TEST SET COUNT : 4494 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) : 1.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74 REMARK 3 REFLECTION IN BIN (WORKING SET) : 6197 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88 REMARK 3 BIN R VALUE (WORKING SET) : 0.3410 REMARK 3 BIN FREE R VALUE SET COUNT : 315 REMARK 3 BIN FREE R VALUE : 0.3370 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6415 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 51 REMARK 3 SOLVENT ATOMS : 576 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.24 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.39700 REMARK 3 B22 (A**2) : -0.23400 REMARK 3 B33 (A**2) : 1.66200 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.38900 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.117 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.339 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6721 ; 0.005 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6037 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9174 ; 1.313 ; 1.643 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14095 ; 1.222 ; 1.568 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 881 ; 7.601 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 267 ;30.280 ;22.060 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1028 ;13.464 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;20.401 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 887 ; 0.052 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7582 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1363 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 927 ; 0.178 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 145 ; 0.211 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3120 ; 0.153 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 437 ; 0.160 ; 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): 3500 ; 1.375 ; 2.690 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3499 ; 1.374 ; 2.690 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4389 ; 2.238 ; 4.022 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4390 ; 2.237 ; 4.022 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3221 ; 1.657 ; 2.876 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3222 ; 1.657 ; 2.877 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4785 ; 2.663 ; 4.207 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4786 ; 2.663 ; 4.208 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 : Chains H I REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : Chains L M REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE 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 : NULL 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 6SS0 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_1292104089. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-NOV-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97242 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88773 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 46.548 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : 0.15000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 5.40 REMARK 200 R MERGE FOR SHELL (I) : 2.59000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.900 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: 6SRV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SPG PH 7.0 25% PEG1500 PACT A4 REMARK 280 SPG: SUCCINIC ACID, PHOSPHATE, GLYCINE, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 291K 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 33.68500 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19420 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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: 4460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: III, 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 GLY H -3 REMARK 465 ALA H -2 REMARK 465 HIS H -1 REMARK 465 SER H 0 REMARK 465 GLU H 1 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 ALA H 221 REMARK 465 ALA H 222 REMARK 465 GLY L -2 REMARK 465 VAL L -1 REMARK 465 HIS L 0 REMARK 465 SER L 1 REMARK 465 GLN L 2 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 GLY I -3 REMARK 465 ALA I -2 REMARK 465 HIS I -1 REMARK 465 SER I 0 REMARK 465 GLU I 1 REMARK 465 CYS I 216 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 THR I 219 REMARK 465 HIS I 220 REMARK 465 ALA I 221 REMARK 465 ALA I 222 REMARK 465 GLY M -2 REMARK 465 VAL M -1 REMARK 465 HIS M 0 REMARK 465 SER M 1 REMARK 465 GLN M 2 REMARK 465 THR M 210 REMARK 465 GLU M 211 REMARK 465 CYS M 212 REMARK 465 SER M 213 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 HOHII 317 O HOHII 412 1.60 REMARK 500 O HOHII 412 O HOHII 415 1.89 REMARK 500 O GLYLL 29 O HOHLL 401 2.19 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 HG SERHH 21 H GLYII 133 2656 1.33 REMARK 500 HE21 GLNHH 81 HG2 LYSII 129 2656 1.34 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 SERHH 65 -10.87 77.95 REMARK 500 ASPHH 98 -100.86 -117.43 REMARK 500 ASPHH 144 68.09 65.23 REMARK 500 ASNLL 27B -95.18 -116.21 REMARK 500 ASNLL 51 -46.34 76.72 REMARK 500 ASNLL 51 -46.46 76.72 REMARK 500 ASPLL 152 -112.25 53.82 REMARK 500 SERII 65 -9.29 75.52 REMARK 500 ASPII 98 -101.23 -116.74 REMARK 500 SERII 128 -37.42 -32.82 REMARK 500 LYSII 129 -17.07 -150.41 REMARK 500 SERII 130 70.62 -62.83 REMARK 500 ASPII 144 67.96 65.05 REMARK 500 THRII 160 -57.75 -123.32 REMARK 500 ASNMM 27B -96.01 -116.58 REMARK 500 ASNMM 51 -46.83 76.66 REMARK 500 ASPMM 152 -112.70 56.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6SRV RELATED DB: PDB REMARK 900 RELATED ID: 6SRX RELATED DB: PDB REMARK 900 RELATED ID: 6SS2 RELATED DB: PDB REMARK 900 RELATED ID: 6SS4 RELATED DB: PDB REMARK 900 RELATED ID: 6SS5 RELATED DB: PDB REMARK 900 RELATED ID: 6SS6 RELATED DB: PDB REMARK 900 RELATED ID: 6TUL RELATED DB: PDB DBREF 6SS0HH -3 222 PDB 6SS0 6SS0 -3 222 DBREF 6SS0LL -2 213 PDB 6SS0 6SS0 -2 213 DBREF 6SS0II -3 222 PDB 6SS0 6SS0 -3 222 DBREF 6SS0MM -2 213 PDB 6SS0 6SS0 -2 213 SEQRES 1HH 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2HH 233 GLY LEU VAL ARG PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3HH 233 ALA ALA SER GLU PHE THR PHE ARG TYR ASP TYR HIS VAL SEQRES 4HH 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5HH 233 SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA SEQRES 6HH 233 ASP SER VAL LYS SER ARG PHE THR ILE SER ARG ASP ASN SEQRES 7HH 233 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG SEQRES 8HH 233 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LEU ARG SEQRES 9HH 233 ALA ASP LEU GLY LEU TYR MET ASP LEU TRP GLY ARG GLY SEQRES 10HH 233 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11HH 233 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12HH 233 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13HH 233 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14HH 233 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15HH 233 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16HH 233 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17HH 233 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18HH 233 VAL GLU PRO LYS SER CYS ASP LYS THR HIS ALA ALA SEQRES 1LL 220 GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO PRO SER SEQRES 2LL 220 VAL SER ALA ALA PRO GLY GLN LYS VAL ALA VAL SER CYS SEQRES 3LL 220 SER GLY SER SER SER ASN ILE GLY SER HIS TYR VAL SER SEQRES 4LL 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5LL 220 ILE TYR ASP ASN SER GLU ARG THR SER GLY ILE PRO ASP SEQRES 6LL 220 ARG PHE SER GLY SER LYS SER GLY THR SER ALA THR LEU SEQRES 7LL 220 GLY ILE THR GLY LEU GLN THR GLY ASP GLU ALA ASP TYR SEQRES 8LL 220 TYR CYS GLY THR TRP ASP GLU LEU THR SER ASN LEU VAL SEQRES 9LL 220 PHE GLY GLY GLY THR ARG LEU THR VAL LEU GLY GLN PRO SEQRES 10LL 220 LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11LL 220 GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU SEQRES 12LL 220 ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP SEQRES 13LL 220 LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR SEQRES 14LL 220 THR THR PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SEQRES 15LL 220 SER SER TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER SEQRES 16LL 220 HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU GLY SER SEQRES 17LL 220 THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1II 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2II 233 GLY LEU VAL ARG PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3II 233 ALA ALA SER GLU PHE THR PHE ARG TYR ASP TYR HIS VAL SEQRES 4II 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5II 233 SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA SEQRES 6II 233 ASP SER VAL LYS SER ARG PHE THR ILE SER ARG ASP ASN SEQRES 7II 233 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG SEQRES 8II 233 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LEU ARG SEQRES 9II 233 ALA ASP LEU GLY LEU TYR MET ASP LEU TRP GLY ARG GLY SEQRES 10II 233 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11II 233 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12II 233 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13II 233 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14II 233 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15II 233 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16II 233 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17II 233 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18II 233 VAL GLU PRO LYS SER CYS ASP LYS THR HIS ALA ALA SEQRES 1MM 220 GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO PRO SER SEQRES 2MM 220 VAL SER ALA ALA PRO GLY GLN LYS VAL ALA VAL SER CYS SEQRES 3MM 220 SER GLY SER SER SER ASN ILE GLY SER HIS TYR VAL SER SEQRES 4MM 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5MM 220 ILE TYR ASP ASN SER GLU ARG THR SER GLY ILE PRO ASP SEQRES 6MM 220 ARG PHE SER GLY SER LYS SER GLY THR SER ALA THR LEU SEQRES 7MM 220 GLY ILE THR GLY LEU GLN THR GLY ASP GLU ALA ASP TYR SEQRES 8MM 220 TYR CYS GLY THR TRP ASP GLU LEU THR SER ASN LEU VAL SEQRES 9MM 220 PHE GLY GLY GLY THR ARG LEU THR VAL LEU GLY GLN PRO SEQRES 10MM 220 LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11MM 220 GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU SEQRES 12MM 220 ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP SEQRES 13MM 220 LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR SEQRES 14MM 220 THR THR PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SEQRES 15MM 220 SER SER TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER SEQRES 16MM 220 HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU GLY SER SEQRES 17MM 220 THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SER HET CL HH 301 1 HET CL HH 302 1 HET CL HH 303 1 HET SIN LL 301 12 HET PEG LL 302 17 HET SIN MM 301 12 HET PEG MM 302 17 HET PEG MM 303 17 HET CL MM 304 1 HET PGE MM 305 24 HETNAM CL CHLORIDE ION HETNAM SIN SUCCINIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM PGE TRIETHYLENE GLYCOL FORMUL 5 CL 4(CL 1-) FORMUL 8 SIN 2(C4 H6 O4) FORMUL 9 PEG 3(C4 H10 O3) FORMUL 14 PGE C6 H14 O4 FORMUL 15 HOH *576(H2 O) HELIX 1 AA1 GLUHH 26 ASPHH 32 5 7 HELIX 2 AA2 ASNHH 73 LYSHH 75 5 3 HELIX 3 AA3 ARGHH 83 THRHH 87 5 5 HELIX 4 AA4 SERHH 156 ALAHH 158 5 3 HELIX 5 AA5 SERHH 187 LEUHH 189 5 3 HELIX 6 AA6 LYSHH 201 ASNHH 204 5 4 HELIX 7 AA7 GLNLL 79 GLULL 83 5 5 HELIX 8 AA8 SERLL 122 ALALL 128 1 7 HELIX 9 AA9 THRLL 182 HISLL 189 1 8 HELIX 10 AB1 GLUII 26 ASPII 32 5 7 HELIX 11 AB2 ASPII 61 LYSII 64 5 4 HELIX 12 AB3 ASNII 73 LYSII 75 5 3 HELIX 13 AB4 ARGII 83 THRII 87 5 5 HELIX 14 AB5 SERII 156 ALAII 158 5 3 HELIX 15 AB6 LYSII 201 ASNII 204 5 4 HELIX 16 AB7 GLNMM 79 GLUMM 83 5 5 HELIX 17 AB8 SERMM 122 ALAMM 128 1 7 HELIX 18 AB9 THRMM 182 HISMM 189 1 8 SHEET 1 AA1 4 LEUHH 4 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 ALAHH 24 -1 O ALAHH 23 N LEUHH 5 SHEET 3 AA1 4 THRHH 77 METHH 82 -1 O METHH 82 N LEUHH 18 SHEET 4 AA1 4 PHEHH 67 ASPHH 72 -1 N SERHH 70 O TYRHH 79 SHEET 1 AA2 6 GLYHH 10 VALHH 12 0 SHEET 2 AA2 6 THRHH 107 VALHH 111 1 O THRHH 110 N GLYHH 10 SHEET 3 AA2 6 ALAHH 88 ALAHH 97 -1 N TYRHH 90 O THRHH 107 SHEET 4 AA2 6 TYRHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 91 SHEET 5 AA2 6 LEUHH 45 ILEHH 51 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AA2 6 THRHH 57 TYRHH 59 -1 O TYRHH 58 N ALAHH 50 SHEET 1 AA3 4 GLYHH 10 VALHH 12 0 SHEET 2 AA3 4 THRHH 107 VALHH 111 1 O THRHH 110 N GLYHH 10 SHEET 3 AA3 4 ALAHH 88 ALAHH 97 -1 N TYRHH 90 O THRHH 107 SHEET 4 AA3 4 LEUHH 100A TRPHH 103 -1 O TYRHH 100B N ARGHH 96 SHEET 1 AA4 4 SERHH 120 LEUHH 124 0 SHEET 2 AA4 4 THRHH 135 TYRHH 145 -1 O GLYHH 139 N LEUHH 124 SHEET 3 AA4 4 TYRHH 176 PROHH 185 -1 O LEUHH 178 N VALHH 142 SHEET 4 AA4 4 VALHH 163 THRHH 165 -1 N HISHH 164 O VALHH 181 SHEET 1 AA5 4 SERHH 120 LEUHH 124 0 SHEET 2 AA5 4 THRHH 135 TYRHH 145 -1 O GLYHH 139 N LEUHH 124 SHEET 3 AA5 4 TYRHH 176 PROHH 185 -1 O LEUHH 178 N VALHH 142 SHEET 4 AA5 4 VALHH 169 LEUHH 170 -1 N VALHH 169 O SERHH 177 SHEET 1 AA6 3 THRHH 151 TRPHH 154 0 SHEET 2 AA6 3 TYRHH 194 HISHH 200 -1 O ASNHH 197 N SERHH 153 SHEET 3 AA6 3 THRHH 205 VALHH 211 -1 O THRHH 205 N HISHH 200 SHEET 1 AA7 6 SERLL 10 ALALL 13 0 SHEET 2 AA7 6 THRLL 102 VALLL 106 1 O ARGLL 103 N VALLL 11 SHEET 3 AA7 6 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 SHEET 4 AA7 6 SERLL 34 GLNLL 38 -1 N TYRLL 36 O TYRLL 87 SHEET 5 AA7 6 LYSLL 45 TYRLL 49 -1 O LEULL 47 N TRPLL 35 SHEET 6 AA7 6 GLULL 53 ARGLL 54 -1 O GLULL 53 N TYRLL 49 SHEET 1 AA8 4 SERLL 10 ALALL 13 0 SHEET 2 AA8 4 THRLL 102 VALLL 106 1 O ARGLL 103 N VALLL 11 SHEET 3 AA8 4 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 SHEET 4 AA8 4 ASNLL 95B PHELL 98 -1 O VALLL 97 N THRLL 90 SHEET 1 AA9 3 VALLL 19 SERLL 24 0 SHEET 2 AA9 3 SERLL 70 ILELL 75 -1 O LEULL 73 N VALLL 21 SHEET 3 AA9 3 PHELL 62 SERLL 67 -1 N SERLL 63 O GLYLL 74 SHEET 1 AB1 4 SERLL 115 PHELL 119 0 SHEET 2 AB1 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB1 4 TYRLL 173 LEULL 181 -1 O ALALL 175 N ILELL 137 SHEET 4 AB1 4 VALLL 160 THRLL 162 -1 N GLULL 161 O TYRLL 178 SHEET 1 AB2 4 SERLL 115 PHELL 119 0 SHEET 2 AB2 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB2 4 TYRLL 173 LEULL 181 -1 O ALALL 175 N ILELL 137 SHEET 4 AB2 4 SERLL 166 LYSLL 167 -1 N SERLL 166 O ALALL 174 SHEET 1 AB3 4 SERLL 154 VALLL 156 0 SHEET 2 AB3 4 THRLL 146 ALALL 151 -1 N ALALL 151 O SERLL 154 SHEET 3 AB3 4 TYRLL 192 HISLL 198 -1 O THRLL 197 N THRLL 146 SHEET 4 AB3 4 SERLL 201 VALLL 207 -1 O VALLL 203 N VALLL 196 SHEET 1 AB4 4 LEUII 4 SERII 7 0 SHEET 2 AB4 4 LEUII 18 ALAII 24 -1 O ALAII 23 N LEUII 5 SHEET 3 AB4 4 THRII 77 METII 82 -1 O METII 82 N LEUII 18 SHEET 4 AB4 4 PHEII 67 ASPII 72 -1 N SERII 70 O TYRII 79 SHEET 1 AB5 6 GLYII 10 VALII 12 0 SHEET 2 AB5 6 THRII 107 VALII 111 1 O THRII 110 N GLYII 10 SHEET 3 AB5 6 ALAII 88 ALAII 97 -1 N ALAII 88 O VALII 109 SHEET 4 AB5 6 TYRII 33 GLNII 39 -1 N VALII 37 O TYRII 91 SHEET 5 AB5 6 LEUII 45 ILEII 51 -1 O GLUII 46 N ARGII 38 SHEET 6 AB5 6 THRII 57 TYRII 59 -1 O TYRII 58 N ALAII 50 SHEET 1 AB6 4 GLYII 10 VALII 12 0 SHEET 2 AB6 4 THRII 107 VALII 111 1 O THRII 110 N GLYII 10 SHEET 3 AB6 4 ALAII 88 ALAII 97 -1 N ALAII 88 O VALII 109 SHEET 4 AB6 4 LEUII 100A TRPII 103 -1 O TYRII 100B N ARGII 96 SHEET 1 AB7 4 SERII 120 LEUII 124 0 SHEET 2 AB7 4 THRII 135 TYRII 145 -1 O GLYII 139 N LEUII 124 SHEET 3 AB7 4 TYRII 176 PROII 185 -1 O LEUII 178 N VALII 142 SHEET 4 AB7 4 VALII 163 THRII 165 -1 N HISII 164 O VALII 181 SHEET 1 AB8 4 SERII 120 LEUII 124 0 SHEET 2 AB8 4 THRII 135 TYRII 145 -1 O GLYII 139 N LEUII 124 SHEET 3 AB8 4 TYRII 176 PROII 185 -1 O LEUII 178 N VALII 142 SHEET 4 AB8 4 VALII 169 LEUII 170 -1 N VALII 169 O SERII 177 SHEET 1 AB9 3 THRII 151 TRPII 154 0 SHEET 2 AB9 3 TYRII 194 HISII 200 -1 O ASNII 197 N SERII 153 SHEET 3 AB9 3 THRII 205 VALII 211 -1 O THRII 205 N HISII 200 SHEET 1 AC1 6 SERMM 10 ALAMM 13 0 SHEET 2 AC1 6 THRMM 102 VALMM 106 1 O ARGMM 103 N VALMM 11 SHEET 3 AC1 6 ALAMM 84 ASPMM 92 -1 N ALAMM 84 O LEUMM 104 SHEET 4 AC1 6 SERMM 34 GLNMM 38 -1 N TYRMM 36 O TYRMM 87 SHEET 5 AC1 6 LYSMM 45 TYRMM 49 -1 O LEUMM 47 N TRPMM 35 SHEET 6 AC1 6 GLUMM 53 ARGMM 54 -1 O GLUMM 53 N TYRMM 49 SHEET 1 AC2 4 SERMM 10 ALAMM 13 0 SHEET 2 AC2 4 THRMM 102 VALMM 106 1 O ARGMM 103 N VALMM 11 SHEET 3 AC2 4 ALAMM 84 ASPMM 92 -1 N ALAMM 84 O LEUMM 104 SHEET 4 AC2 4 ASNMM 95B PHEMM 98 -1 O VALMM 97 N THRMM 90 SHEET 1 AC3 3 VALMM 19 SERMM 24 0 SHEET 2 AC3 3 SERMM 70 ILEMM 75 -1 O LEUMM 73 N VALMM 21 SHEET 3 AC3 3 PHEMM 62 SERMM 67 -1 N SERMM 63 O GLYMM 74 SHEET 1 AC4 4 SERMM 115 PHEMM 119 0 SHEET 2 AC4 4 ALAMM 131 PHEMM 140 -1 O LEUMM 136 N THRMM 117 SHEET 3 AC4 4 TYRMM 173 LEUMM 181 -1 O ALAMM 175 N ILEMM 137 SHEET 4 AC4 4 VALMM 160 THRMM 162 -1 N GLUMM 161 O TYRMM 178 SHEET 1 AC5 4 SERMM 115 PHEMM 119 0 SHEET 2 AC5 4 ALAMM 131 PHEMM 140 -1 O LEUMM 136 N THRMM 117 SHEET 3 AC5 4 TYRMM 173 LEUMM 181 -1 O ALAMM 175 N ILEMM 137 SHEET 4 AC5 4 SERMM 166 LYSMM 167 -1 N SERMM 166 O ALAMM 174 SHEET 1 AC6 4 SERMM 154 VALMM 156 0 SHEET 2 AC6 4 THRMM 146 ALAMM 151 -1 N ALAMM 151 O SERMM 154 SHEET 3 AC6 4 TYRMM 192 HISMM 198 -1 O THRMM 197 N THRMM 146 SHEET 4 AC6 4 SERMM 201 VALMM 207 -1 O VALMM 203 N VALMM 196 SSBOND 1 CYSHH 22 CYSHH 92 1555 1555 2.06 SSBOND 2 CYSHH 140 CYSHH 196 1555 1555 2.02 SSBOND 3 CYSLL 23 CYSLL 88 1555 1555 2.05 SSBOND 4 CYSLL 135 CYSLL 194 1555 1555 2.03 SSBOND 5 CYSII 22 CYSII 92 1555 1555 2.04 SSBOND 6 CYSII 140 CYSII 196 1555 1555 2.01 SSBOND 7 CYSMM 23 CYSMM 88 1555 1555 2.05 SSBOND 8 CYSMM 135 CYSMM 194 1555 1555 2.03 CISPEP 1 PHEHH 146 PROHH 147 0 -8.13 CISPEP 2 GLUHH 148 PROHH 149 0 -3.48 CISPEP 3 TYRLL 141 PROLL 142 0 -4.61 CISPEP 4 PHEII 146 PROII 147 0 -8.48 CISPEP 5 GLUII 148 PROII 149 0 -5.32 CISPEP 6 TYRMM 141 PROMM 142 0 -4.14 CRYST1 65.400 67.370 94.330 90.00 100.24 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 0.015291 0.000000 0.002762 0.00000 SCALE2 0.000000 0.014843 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010773 0.00000