HEADER IMMUNE SYSTEM 09-FEB-25 9N8Q TITLE CRYSTAL STRUCTURE OF TRASTUZUMAB FAB WITH P151A COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRASTUZUMAB FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: TRASTUZUMAB FAB LIGHT CHAIN; COMPND 8 CHAIN: L; COMPND 9 ENGINEERED: YES 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 HUMAN FAB FRAGMENT, IMMUNE RESPONSE, IMMUNE SYSTEM, PROALA, PROLINE- KEYWDS 2 TO-ALANINE, BISPECIFIC ANTIBODY, BSAB, BSIGG, CIS-PEPTIDE, KEYWDS 3 TRASTUZUMAB, FAB EXPDTA X-RAY DIFFRACTION AUTHOR W.S.CHOI,C.TILEGENOVA,M.ARE,A.ZWOLAK,P.SHAFFER,S.SHARMA REVDAT 1 22-OCT-25 9N8Q 0 JRNL AUTH C.TILEGENOVA,T.LIU,Q.ZHAO,M.ARE,Y.ZHAO,W.S.CHOI,A.BHAUMIK, JRNL AUTH 2 R.STEELE,N.MANIERI,B.TUREGUN,P.SHAFFER,R.ERNST,S.SHARMA, JRNL AUTH 3 W.CHEUNG,A.ZWOLAK JRNL TITL FOLDING-MEDIATED SECRETION OF PURE BISPECIFIC ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 19549 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.213 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930 REMARK 3 FREE R VALUE TEST SET COUNT : 964 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 45.0000 - 4.9800 1.00 2857 160 0.1937 0.2468 REMARK 3 2 4.9800 - 3.9500 1.00 2686 141 0.1644 0.2206 REMARK 3 3 3.9500 - 3.4500 1.00 2655 128 0.2212 0.2802 REMARK 3 4 3.4500 - 3.1400 1.00 2640 132 0.2387 0.3272 REMARK 3 5 3.1400 - 2.9100 1.00 2578 141 0.2913 0.3901 REMARK 3 6 2.9100 - 2.7400 1.00 2613 125 0.2738 0.3539 REMARK 3 7 2.7400 - 2.6000 0.99 2556 137 0.3171 0.4042 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.413 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.483 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 58.45 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.02 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 3329 REMARK 3 ANGLE : 0.957 4531 REMARK 3 CHIRALITY : 0.053 512 REMARK 3 PLANARITY : 0.008 582 REMARK 3 DIHEDRAL : 9.155 477 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.8585 -23.7430 -16.8694 REMARK 3 T TENSOR REMARK 3 T11: 0.6476 T22: 0.3497 REMARK 3 T33: 0.5535 T12: -0.0173 REMARK 3 T13: -0.0960 T23: 0.0332 REMARK 3 L TENSOR REMARK 3 L11: 0.6891 L22: 0.3102 REMARK 3 L33: 0.5903 L12: 0.0943 REMARK 3 L13: 0.0797 L23: 0.3668 REMARK 3 S TENSOR REMARK 3 S11: -0.1745 S12: 0.1414 S13: 0.1228 REMARK 3 S21: 0.0163 S22: -0.0033 S23: -0.0605 REMARK 3 S31: -0.0438 S32: 0.2919 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 95 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.1975 -34.6863 -24.0508 REMARK 3 T TENSOR REMARK 3 T11: 0.7939 T22: 0.5304 REMARK 3 T33: 0.6326 T12: 0.0909 REMARK 3 T13: -0.1010 T23: 0.0678 REMARK 3 L TENSOR REMARK 3 L11: 0.0503 L22: 0.0405 REMARK 3 L33: 0.0357 L12: -0.0345 REMARK 3 L13: 0.0037 L23: 0.0198 REMARK 3 S TENSOR REMARK 3 S11: 0.1917 S12: 0.0698 S13: -0.3769 REMARK 3 S21: 0.4398 S22: -0.0594 S23: -0.1255 REMARK 3 S31: 0.3079 S32: 0.0712 S33: -0.0004 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 107 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9455 -32.6954 5.9851 REMARK 3 T TENSOR REMARK 3 T11: 1.1863 T22: 0.4243 REMARK 3 T33: 0.4595 T12: -0.2061 REMARK 3 T13: 0.0367 T23: 0.0360 REMARK 3 L TENSOR REMARK 3 L11: 2.0856 L22: 0.2320 REMARK 3 L33: 0.1663 L12: 0.7657 REMARK 3 L13: -0.6024 L23: -0.2438 REMARK 3 S TENSOR REMARK 3 S11: -0.2476 S12: -0.9610 S13: 0.3240 REMARK 3 S21: 0.2840 S22: -0.1284 S23: -0.1163 REMARK 3 S31: 0.8164 S32: 0.2415 S33: -0.2298 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.6217 -33.2765 -29.0559 REMARK 3 T TENSOR REMARK 3 T11: 0.6509 T22: 0.3608 REMARK 3 T33: 0.5047 T12: -0.1692 REMARK 3 T13: 0.0101 T23: 0.0090 REMARK 3 L TENSOR REMARK 3 L11: 1.3528 L22: 0.2451 REMARK 3 L33: 0.3976 L12: -0.0555 REMARK 3 L13: 0.2650 L23: 0.1734 REMARK 3 S TENSOR REMARK 3 S11: -0.2568 S12: 0.2849 S13: 0.1439 REMARK 3 S21: 0.0199 S22: 0.1666 S23: 0.0455 REMARK 3 S31: 0.5603 S32: -0.2329 S33: 0.0003 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.2169 -30.0454 -22.6819 REMARK 3 T TENSOR REMARK 3 T11: 0.5766 T22: 0.2941 REMARK 3 T33: 0.5609 T12: -0.1626 REMARK 3 T13: 0.0108 T23: 0.0324 REMARK 3 L TENSOR REMARK 3 L11: 0.1307 L22: 0.1508 REMARK 3 L33: 0.2016 L12: -0.0928 REMARK 3 L13: 0.1952 L23: -0.1846 REMARK 3 S TENSOR REMARK 3 S11: -0.0714 S12: 0.2318 S13: -0.0441 REMARK 3 S21: 0.3622 S22: -0.1056 S23: -0.1282 REMARK 3 S31: -0.1571 S32: -0.0380 S33: -0.0001 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.9383 -27.0328 5.5114 REMARK 3 T TENSOR REMARK 3 T11: 1.0386 T22: 0.8520 REMARK 3 T33: 0.6496 T12: -0.4041 REMARK 3 T13: 0.1866 T23: -0.2601 REMARK 3 L TENSOR REMARK 3 L11: 0.5266 L22: 0.2019 REMARK 3 L33: 0.2356 L12: -0.2033 REMARK 3 L13: 0.1910 L23: -0.0123 REMARK 3 S TENSOR REMARK 3 S11: -0.1136 S12: -0.9335 S13: 0.2484 REMARK 3 S21: 0.1914 S22: 0.0140 S23: 0.3970 REMARK 3 S31: 0.2412 S32: -0.6805 S33: 0.0287 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 164 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.3661 -29.1968 5.1623 REMARK 3 T TENSOR REMARK 3 T11: 0.6724 T22: 0.8665 REMARK 3 T33: 0.3966 T12: -0.4257 REMARK 3 T13: 0.1372 T23: -0.2665 REMARK 3 L TENSOR REMARK 3 L11: 0.2981 L22: 1.4360 REMARK 3 L33: 0.9844 L12: 0.6026 REMARK 3 L13: -0.0574 L23: 0.3673 REMARK 3 S TENSOR REMARK 3 S11: 0.1925 S12: -0.8880 S13: -0.4070 REMARK 3 S21: 0.4063 S22: -0.7356 S23: 0.1762 REMARK 3 S31: 0.3793 S32: -0.0985 S33: -0.5509 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9N8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000292764. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JAN-25 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976254 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35686 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120 REMARK 200 RESOLUTION RANGE LOW (A) : 85.890 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 39.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 40.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.200 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.019M DISODIUM ATP, 0.1M SODIUM REMARK 280 CACODYLATE PH 6.5, 18.6% W/V PEG 10,000, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+5/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+1/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.44600 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 140.89200 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 105.66900 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 176.11500 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 35.22300 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.44600 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 140.89200 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 176.11500 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 105.66900 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 35.22300 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: 3620 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19420 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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 C1 PEG L 301 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 SER H 132 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 LYS H 218 REMARK 465 SER H 219 REMARK 465 CYS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 CYS L 214 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 LYS H 30 CG CD CE NZ REMARK 470 ASP H 98 CG OD1 OD2 REMARK 470 TYR H 100A CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 141 CG CD CE NZ REMARK 470 LYS H 205 CG CD CE NZ REMARK 470 LYS H 210 CG CD CE NZ REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 GLN L 100 CG CD OE1 NE2 REMARK 470 GLU L 165 CG CD OE1 OE2 REMARK 470 LYS L 190 CG CD CE NZ 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 GLU H 152 O HOH H 401 2.17 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 PHE H 27 -178.38 -174.07 REMARK 500 ASP H 148 68.77 60.32 REMARK 500 PHE H 150 139.38 -173.02 REMARK 500 ASN L 30 -131.85 58.16 REMARK 500 ALA L 51 -23.05 71.09 REMARK 500 ALA L 84 175.73 179.39 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9MVX RELATED DB: PDB DBREF 9N8Q H 1 226 PDB 9N8Q 9N8Q 1 226 DBREF 9N8Q L 1 214 PDB 9N8Q 9N8Q 1 214 SEQRES 1 H 229 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 229 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 229 PHE ASN ILE LYS ASP THR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 H 229 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE TYR SEQRES 5 H 229 PRO THR ASN GLY TYR THR ARG TYR ALA ASP SER VAL LYS SEQRES 6 H 229 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 H 229 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 229 ALA VAL TYR TYR CYS SER ARG TRP GLY GLY ASP GLY PHE SEQRES 9 H 229 TYR ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 229 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 229 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 229 LYS LEU GLY CYS LEU VAL LYS ASP TYR PHE ALA GLU PRO SEQRES 13 H 229 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 229 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 229 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 229 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 229 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 H 229 SER CYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN ASP VAL ASN THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 214 PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN HIS SEQRES 8 L 214 TYR THR THR PRO PRO THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL ASP ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET PEG H 301 7 HET PEG H 302 7 HET PEG H 303 7 HET PEG L 301 7 HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 3 PEG 4(C4 H10 O3) FORMUL 7 HOH *74(H2 O) HELIX 1 AA1 ASN H 28 THR H 32 5 5 HELIX 2 AA2 ARG H 83 THR H 87 5 5 HELIX 3 AA3 SER H 160 ALA H 162 5 3 HELIX 4 AA4 SER H 191 LEU H 193 5 3 HELIX 5 AA5 LYS H 205 ASN H 208 5 4 HELIX 6 AA6 GLN L 79 PHE L 83 5 5 HELIX 7 AA7 SER L 121 SER L 127 1 7 HELIX 8 AA8 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 TRP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ARG H 58 N ARG H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 TRP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 MET H 100C TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA4 4 SER H 124 LEU H 128 0 SHEET 2 AA4 4 THR H 139 TYR H 149 -1 O GLY H 143 N LEU H 128 SHEET 3 AA4 4 TYR H 180 PRO H 189 -1 O VAL H 188 N ALA H 140 SHEET 4 AA4 4 HIS H 168 THR H 169 -1 N HIS H 168 O VAL H 185 SHEET 1 AA5 4 SER H 124 LEU H 128 0 SHEET 2 AA5 4 THR H 139 TYR H 149 -1 O GLY H 143 N LEU H 128 SHEET 3 AA5 4 TYR H 180 PRO H 189 -1 O VAL H 188 N ALA H 140 SHEET 4 AA5 4 VAL H 173 LEU H 174 -1 N VAL H 173 O SER H 181 SHEET 1 AA6 3 THR H 155 TRP H 158 0 SHEET 2 AA6 3 TYR H 198 HIS H 204 -1 O ASN H 201 N SER H 157 SHEET 3 AA6 3 THR H 209 VAL H 215 -1 O VAL H 215 N TYR H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 SER L 14 0 SHEET 2 AA8 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 VAL L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA8 6 PHE L 53 LEU L 54 -1 O PHE L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 SER L 14 0 SHEET 2 AA9 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N ASP L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 144 CYS H 200 1555 1555 2.02 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 PHE H 150 ALA H 151 0 -5.81 CISPEP 2 GLU H 152 PRO H 153 0 2.18 CISPEP 3 SER L 7 PRO L 8 0 -12.16 CISPEP 4 THR L 94 PRO L 95 0 8.00 CISPEP 5 TYR L 140 PRO L 141 0 1.36 CRYST1 99.191 99.191 211.338 90.00 90.00 120.00 P 61 2 2 12 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 0.010082 0.005821 0.000000 0.00000 SCALE2 0.000000 0.011641 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004732 0.00000