HEADER PROTEIN BINDING 06-SEP-19 6SS5 TITLE STRUCTURE OF THE ARGINASE-2-INHIBITORY HUMAN ANTIGEN-BINDING FRAGMENT TITLE 2 FAB C0020187 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB C0020187 HEAVY CHAIN (IGG1); COMPND 3 CHAIN: HHH; 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 C0020187 LIGHT CHAIN (IGG1); COMPND 9 CHAIN: LLL; 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_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETINAE GEN. SP.CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 7 EXPRESSION_SYSTEM_VARIANT: EXPICHO; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 16 EXPRESSION_SYSTEM_VARIANT: EXPICHO; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 18 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 D.T.Y.CHAN,L.JENKINSON,S.W.HAYNES,M.AUSTIN,A.DIAMANDAKIS, JRNL AUTH 2 D.BURSCHOWSKY,C.SEEWOORUTHUN,A.ADDYMAN,S.FIEDLER,S.RYMAN, JRNL AUTH 3 J.WHITEHOUSE,L.H.SLATER,E.GOWANS,Y.SHIBATA,M.BARNARD, JRNL AUTH 4 R.W.WILKINSON,T.J.VAUGHAN,S.V.HOLT,V.CERUNDOLO,M.D.CARR, JRNL AUTH 5 M.A.T.GROVES JRNL TITL EXTENSIVE SEQUENCE AND STRUCTURAL EVOLUTION OF ARGINASE 2 JRNL TITL 2 INHIBITORY ANTIBODIES ENABLED BY AN UNBIASED APPROACH TO JRNL TITL 3 AFFINITY MATURATION. JRNL REF PROC.NATL.ACAD.SCI.USA V. 117 16949 2020 JRNL REFN ESSN 1091-6490 JRNL PMID 32616569 JRNL DOI 10.1073/PNAS.1919565117 REMARK 2 REMARK 2 RESOLUTION. 1.78 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) : 1.78 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.35 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 58262 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) : 0.178 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.017 REMARK 3 FREE R VALUE TEST SET COUNT : 2923 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) : 1.78 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4027 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.13 REMARK 3 BIN R VALUE (WORKING SET) : 0.3780 REMARK 3 BIN FREE R VALUE SET COUNT : 213 REMARK 3 BIN FREE R VALUE : 0.3700 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3278 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 64 REMARK 3 SOLVENT ATOMS : 318 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.21 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.39000 REMARK 3 B22 (A**2) : 3.81100 REMARK 3 B33 (A**2) : -1.42100 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): 0.098 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.725 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3514 ; 0.013 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3149 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4810 ; 1.781 ; 1.656 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7374 ; 1.451 ; 1.585 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 483 ;21.151 ; 5.445 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 128 ;33.662 ;23.047 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 524 ;14.262 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;23.295 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 471 ; 0.082 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4453 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 683 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 578 ; 0.194 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 38 ; 0.252 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1651 ; 0.167 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 309 ; 0.296 ; 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): 1829 ; 2.902 ; 3.233 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1828 ; 2.899 ; 3.233 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2302 ; 3.967 ; 4.831 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2303 ; 3.967 ; 4.832 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1685 ; 4.296 ; 3.734 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1682 ; 4.283 ; 3.734 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2508 ; 6.351 ; 5.391 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2503 ; 6.336 ; 5.390 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 : 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 : 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 6SS5 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_1292104127. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-DEC-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587 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 : 58306 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780 REMARK 200 RESOLUTION RANGE LOW (A) : 49.355 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 10.40 REMARK 200 R MERGE (I) : 0.16000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1 REMARK 200 DATA REDUNDANCY IN SHELL : 8.50 REMARK 200 R MERGE FOR SHELL (I) : 4.11000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.500 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 (%): 61.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5 70% MPD, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 82.19000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.19000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.66000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.68500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.66000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.68500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.19000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.66000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.68500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.19000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.66000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.68500 REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6760 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH L 572 LIES ON A SPECIAL POSITION. 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 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 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 HE22 GLNLL 195 OE2 GLULL 204 1.47 REMARK 500 HE22 GLNLL 195 O HOHLL 403 1.48 REMARK 500 H SERHH 113 O HOHHH 410 1.59 REMARK 500 OE1 GLNLL 17 O HOHLL 401 1.77 REMARK 500 O HOHLL 505 O HOHLL 560 1.79 REMARK 500 OG SERLL 10 O HOHLL 402 1.80 REMARK 500 NE2 GLNLL 195 O HOHLL 403 1.82 REMARK 500 O HOHLL 456 O HOHLL 476 1.83 REMARK 500 O HOHLL 539 O HOHLL 567 1.89 REMARK 500 O HOHLL 537 O HOHLL 548 1.93 REMARK 500 O HOHLL 464 O HOHLL 558 1.93 REMARK 500 O HOHHH 528 O HOHLL 543 1.99 REMARK 500 O HOHLL 501 O HOHLL 575 2.00 REMARK 500 O HOHLL 549 O HOHLL 565 2.00 REMARK 500 O HOHHH 473 O HOHLL 409 2.03 REMARK 500 O HOHHH 512 O HOHLL 561 2.04 REMARK 500 O HOHLL 555 O HOHLL 563 2.05 REMARK 500 OE1 GLULL 199 O HOHLL 404 2.08 REMARK 500 O HOHHH 517 O HOHLL 551 2.09 REMARK 500 OG SERLL 27A O HOHLL 405 2.16 REMARK 500 OE1 GLULL 83 O HOHLL 406 2.18 REMARK 500 O HOHLL 552 O HOHLL 556 2.19 REMARK 500 O HOHLL 559 O HOHLL 579 2.19 REMARK 500 O HOHHH 460 O HOHHH 530 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 O HOHLL 559 O HOHLL 568 4555 1.74 REMARK 500 O HOHLL 575 O HOHLL 580 8455 2.00 REMARK 500 O HOHHH 532 O HOHLL 452 8555 2.07 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 PROHH 149 N - CA - CB ANGL. DEV. = -7.2 DEGREES REMARK 500 ARGLL 61 CB - CA - C ANGL. DEV. = -12.5 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 ALAHH 97 11.05 -143.53 REMARK 500 LEUHH 99 -87.78 -116.88 REMARK 500 THRHH 116 124.23 -37.56 REMARK 500 ASPHH 144 42.50 73.82 REMARK 500 ASNLL 27B -96.48 -107.78 REMARK 500 ASNLL 51 -42.08 75.19 REMARK 500 ASPLL 152 -106.46 52.99 REMARK 500 ASNLL 171 -2.84 83.68 REMARK 500 GLULL 199 -119.11 48.43 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: 6SS0 RELATED DB: PDB REMARK 900 RELATED ID: 6SS2 RELATED DB: PDB REMARK 900 RELATED ID: 6SS4 RELATED DB: PDB REMARK 900 RELATED ID: 6SS6 RELATED DB: PDB REMARK 900 RELATED ID: 6TUL RELATED DB: PDB DBREF 6SS5HH -3 222 PDB 6SS5 6SS5 -3 222 DBREF 6SS5LL -2 213 PDB 6SS5 6SS5 -2 213 SEQRES 1HH 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2HH 233 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3HH 233 ALA ALA SER GLY PHE THR PHE SER SER TYR ALA MET SER 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 GLY 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 THR ILE SER CYS SEQRES 3LL 220 SER GLY SER SER SER ASN ILE GLY ASN 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 PRO 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 SER SER LEU SER ALA LEU VAL SEQRES 9LL 220 PHE GLY GLY GLY THR LYS 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 HET CL HH 301 1 HET CL HH 302 1 HET CL HH 303 1 HET MPD HH 304 22 HET EPE LL 301 32 HET EPE LL 302 32 HET CL LL 303 1 HET CL LL 304 1 HET MPD LL 305 22 HET MPD LL 306 22 HET SO4 LL 307 5 HETNAM CL CHLORIDE ION HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETNAM SO4 SULFATE ION HETSYN EPE HEPES FORMUL 3 CL 5(CL 1-) FORMUL 6 MPD 3(C6 H14 O2) FORMUL 7 EPE 2(C8 H18 N2 O4 S) FORMUL 13 SO4 O4 S 2- FORMUL 14 HOH *318(H2 O) HELIX 1 AA1 THRHH 28 TYRHH 32 5 5 HELIX 2 AA2 ASPHH 61 LYSHH 64 5 4 HELIX 3 AA3 ARGHH 83 THRHH 87 5 5 HELIX 4 AA4 SERHH 156 ALAHH 158 5 3 HELIX 5 AA5 SERHH 187 THRHH 191 5 5 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 SERLL 188 1 7 SHEET 1 AA1 4 GLNHH 3 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O SERHH 21 N SERHH 7 SHEET 3 AA1 4 THRHH 77 METHH 82 -1 O LEUHH 80 N LEUHH 20 SHEET 4 AA1 4 PHEHH 67 ASPHH 72 -1 N SERHH 70 O TYRHH 79 SHEET 1 AA2 6 LEUHH 11 VALHH 12 0 SHEET 2 AA2 6 THRHH 107 VALHH 111 1 O THRHH 110 N VALHH 12 SHEET 3 AA2 6 ALAHH 88 ARGHH 96 -1 N ALAHH 88 O VALHH 109 SHEET 4 AA2 6 ALAHH 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 LEUHH 11 VALHH 12 0 SHEET 2 AA3 4 THRHH 107 VALHH 111 1 O THRHH 110 N VALHH 12 SHEET 3 AA3 4 ALAHH 88 ARGHH 96 -1 N ALAHH 88 O VALHH 109 SHEET 4 AA3 4 TYRHH 100B 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 VALHH 182 N LEUHH 138 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 VALHH 182 N LEUHH 138 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 ILEHH 195 HISHH 200 -1 O ASNHH 197 N SERHH 153 SHEET 3 AA6 3 THRHH 205 ARGHH 210 -1 O VALHH 207 N VALHH 198 SHEET 1 AA7 5 SERLL 10 ALALL 13 0 SHEET 2 AA7 5 THRLL 102 VALLL 106 1 O THRLL 105 N VALLL 11 SHEET 3 AA7 5 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 SHEET 4 AA7 5 SERLL 34 GLNLL 38 -1 N GLNLL 38 O ASPLL 85 SHEET 5 AA7 5 LYSLL 45 ILELL 48 -1 O LEULL 47 N TRPLL 35 SHEET 1 AA8 4 SERLL 10 ALALL 13 0 SHEET 2 AA8 4 THRLL 102 VALLL 106 1 O THRLL 105 N VALLL 11 SHEET 3 AA8 4 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 SHEET 4 AA8 4 ALALL 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 ILELL 75 N VALLL 19 SHEET 3 AA9 3 PHELL 62 SERLL 67 -1 N SERLL 65 O THRLL 72 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 LEULL 181 N ALALL 131 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 LEULL 181 N ALALL 131 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 GLNLL 195 N ALALL 148 SHEET 4 AB3 4 SERLL 201 VALLL 207 -1 O SERLL 201 N HISLL 198 SSBOND 1 CYSHH 22 CYSHH 92 1555 1555 2.10 SSBOND 2 CYSHH 140 CYSHH 196 1555 1555 2.01 SSBOND 3 CYSHH 216 CYSLL 212 1555 1555 2.15 SSBOND 4 CYSLL 23 CYSLL 88 1555 1555 2.02 SSBOND 5 CYSLL 135 CYSLL 194 1555 1555 2.05 CISPEP 1 PHEHH 146 PROHH 147 0 -10.59 CISPEP 2 GLUHH 148 PROHH 149 0 -8.93 CISPEP 3 TYRLL 141 PROLL 142 0 -6.18 CRYST1 71.320 103.370 164.380 90.00 90.00 90.00 C 2 2 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 0.014021 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009674 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006083 0.00000