HEADER IMMUNE SYSTEM 31-DEC-24 9L9Z TITLE FAB OF ANTI-HEV MAB 6H8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF MAB 6H8; COMPND 3 CHAIN: H; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: LIGHT CHAIN OF MAB 6H8; COMPND 6 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090 KEYWDS IMMUNE COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.ZIMIN,W.GUIPING,Y.HAI,Z.QING,Z.ZIZHENG,X.NINGSHAO,L.SHAOWEI REVDAT 1 14-JAN-26 9L9Z 0 JRNL AUTH T.ZIMIN,Y.HAI,W.GUIPING,L.CHANG,Y.ZIHAO,L.JUNFEI,W.SILING, JRNL AUTH 2 Y.DONG,F.MUJIN,W.YINGBIN,G.YING,Z.JUN,L.SHAOWEI,Z.QINGBING, JRNL AUTH 3 X.NINGSHAO,Z.ZIZHENG JRNL TITL CRITICAL ROLE OF ASN490 AND MET492 ON CAPSID PROTEIN OF JRNL TITL 2 ZOONOTIC GROUP HEV IN HOST TROPISM FROM SWINE TO HUMAN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.58 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 60717 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.210 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 3066 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 24.5820 - 4.1965 0.93 2658 133 0.1654 0.1700 REMARK 3 2 4.1965 - 3.3335 0.98 2682 155 0.1554 0.1775 REMARK 3 3 3.3335 - 2.9129 1.00 2674 156 0.1730 0.2097 REMARK 3 4 2.9129 - 2.6469 1.00 2722 129 0.1813 0.2040 REMARK 3 5 2.6469 - 2.4574 1.00 2651 138 0.1935 0.2280 REMARK 3 6 2.4574 - 2.3126 1.00 2707 139 0.1931 0.2727 REMARK 3 7 2.3126 - 2.1969 1.00 2658 148 0.1860 0.2271 REMARK 3 8 2.1969 - 2.1013 1.00 2596 168 0.1848 0.1940 REMARK 3 9 2.1013 - 2.0204 1.00 2653 154 0.1924 0.2308 REMARK 3 10 2.0204 - 1.9507 1.00 2687 125 0.1962 0.2134 REMARK 3 11 1.9507 - 1.8898 1.00 2625 141 0.2002 0.2559 REMARK 3 12 1.8898 - 1.8358 1.00 2637 131 0.2135 0.2401 REMARK 3 13 1.8358 - 1.7875 1.00 2624 155 0.2227 0.2581 REMARK 3 14 1.7875 - 1.7439 1.00 2620 144 0.2218 0.2301 REMARK 3 15 1.7439 - 1.7042 1.00 2640 129 0.2218 0.2765 REMARK 3 16 1.7042 - 1.6680 1.00 2628 153 0.2267 0.2739 REMARK 3 17 1.6680 - 1.6346 1.00 2652 120 0.2322 0.2920 REMARK 3 18 1.6346 - 1.6038 0.99 2626 132 0.2380 0.2833 REMARK 3 19 1.6038 - 1.5751 0.98 2600 115 0.2460 0.3094 REMARK 3 20 1.5751 - 1.5484 0.97 2509 145 0.2601 0.3077 REMARK 3 21 1.5484 - 1.5235 0.94 2476 121 0.2652 0.3120 REMARK 3 22 1.5235 - 1.5000 0.88 2326 135 0.2785 0.3332 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.180 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.270 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.003 3376 REMARK 3 ANGLE : 0.674 4618 REMARK 3 CHIRALITY : 0.046 521 REMARK 3 PLANARITY : 0.003 583 REMARK 3 DIHEDRAL : 11.016 2040 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.6035 21.5156 -1.7944 REMARK 3 T TENSOR REMARK 3 T11: 0.2810 T22: 0.2086 REMARK 3 T33: 0.2374 T12: 0.0352 REMARK 3 T13: 0.0515 T23: -0.0097 REMARK 3 L TENSOR REMARK 3 L11: 4.9516 L22: 7.3787 REMARK 3 L33: 3.0524 L12: 2.6109 REMARK 3 L13: -0.5478 L23: 0.3313 REMARK 3 S TENSOR REMARK 3 S11: 0.1975 S12: -0.3586 S13: 0.1705 REMARK 3 S21: 0.6193 S22: -0.2171 S23: 0.2390 REMARK 3 S31: -0.1867 S32: 0.0648 S33: -0.0265 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 44 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.8526 26.8451 -4.7648 REMARK 3 T TENSOR REMARK 3 T11: 0.3728 T22: 0.2362 REMARK 3 T33: 0.3249 T12: 0.0411 REMARK 3 T13: 0.1234 T23: 0.0146 REMARK 3 L TENSOR REMARK 3 L11: 4.9193 L22: 5.8821 REMARK 3 L33: 4.5210 L12: -1.8649 REMARK 3 L13: -1.5826 L23: 1.3286 REMARK 3 S TENSOR REMARK 3 S11: 0.2363 S12: -0.3217 S13: 0.2574 REMARK 3 S21: 0.7166 S22: 0.0498 S23: 0.6467 REMARK 3 S31: -0.5374 S32: -0.3983 S33: -0.0029 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 146 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.8941 1.4058 -4.4367 REMARK 3 T TENSOR REMARK 3 T11: 0.2360 T22: 0.2212 REMARK 3 T33: 0.1522 T12: -0.0162 REMARK 3 T13: 0.0144 T23: 0.0015 REMARK 3 L TENSOR REMARK 3 L11: 1.1640 L22: 3.5374 REMARK 3 L33: 0.5383 L12: 0.1580 REMARK 3 L13: -0.0798 L23: -0.5484 REMARK 3 S TENSOR REMARK 3 S11: 0.0293 S12: -0.0682 S13: -0.1365 REMARK 3 S21: -0.0588 S22: 0.0129 S23: 0.3749 REMARK 3 S31: 0.0012 S32: 0.0280 S33: -0.0416 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 147 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.5434 -10.2096 0.6770 REMARK 3 T TENSOR REMARK 3 T11: 0.1965 T22: 0.1873 REMARK 3 T33: 0.2089 T12: -0.0262 REMARK 3 T13: -0.0014 T23: 0.0306 REMARK 3 L TENSOR REMARK 3 L11: 5.3587 L22: 4.9594 REMARK 3 L33: 3.3755 L12: -2.6792 REMARK 3 L13: -2.5390 L23: 1.0827 REMARK 3 S TENSOR REMARK 3 S11: -0.1409 S12: -0.1846 S13: 0.0399 REMARK 3 S21: 0.2032 S22: 0.1728 S23: 0.0650 REMARK 3 S31: 0.2080 S32: 0.2453 S33: -0.0943 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.6145 15.3798 -24.8664 REMARK 3 T TENSOR REMARK 3 T11: 0.3318 T22: 0.2049 REMARK 3 T33: 0.2370 T12: 0.0122 REMARK 3 T13: 0.0058 T23: 0.0046 REMARK 3 L TENSOR REMARK 3 L11: 2.6640 L22: 4.0605 REMARK 3 L33: 3.4182 L12: -3.0947 REMARK 3 L13: 1.3907 L23: -0.5950 REMARK 3 S TENSOR REMARK 3 S11: 0.1600 S12: 0.4688 S13: -0.1313 REMARK 3 S21: -0.3060 S22: -0.1762 S23: 0.1588 REMARK 3 S31: -0.0455 S32: -0.0881 S33: -0.0189 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 74 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.7102 23.9181 -18.1424 REMARK 3 T TENSOR REMARK 3 T11: 0.1897 T22: 0.1332 REMARK 3 T33: 0.1444 T12: -0.0307 REMARK 3 T13: -0.0111 T23: -0.0298 REMARK 3 L TENSOR REMARK 3 L11: 5.6857 L22: 5.4858 REMARK 3 L33: 4.5010 L12: -1.6499 REMARK 3 L13: -0.3238 L23: -0.2057 REMARK 3 S TENSOR REMARK 3 S11: 0.1195 S12: -0.0569 S13: 0.0925 REMARK 3 S21: -0.1255 S22: -0.0447 S23: -0.0007 REMARK 3 S31: -0.1900 S32: -0.0565 S33: -0.0610 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 75 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.9117 2.8206 -14.6672 REMARK 3 T TENSOR REMARK 3 T11: 0.1559 T22: 0.2241 REMARK 3 T33: 0.1873 T12: -0.0062 REMARK 3 T13: -0.0144 T23: -0.0152 REMARK 3 L TENSOR REMARK 3 L11: 0.1299 L22: 4.6329 REMARK 3 L33: 0.8192 L12: -0.1114 REMARK 3 L13: -0.0021 L23: -0.6583 REMARK 3 S TENSOR REMARK 3 S11: 0.0895 S12: 0.0123 S13: -0.1331 REMARK 3 S21: -0.1065 S22: -0.1065 S23: 0.3037 REMARK 3 S31: -0.0073 S32: -0.0129 S33: -0.0193 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 137 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.1319 -14.6725 -17.2336 REMARK 3 T TENSOR REMARK 3 T11: 0.2107 T22: 0.2275 REMARK 3 T33: 0.3199 T12: 0.0088 REMARK 3 T13: -0.0797 T23: -0.0019 REMARK 3 L TENSOR REMARK 3 L11: 3.0519 L22: 5.6305 REMARK 3 L33: 1.6205 L12: 2.8710 REMARK 3 L13: -1.4434 L23: -0.8451 REMARK 3 S TENSOR REMARK 3 S11: -0.0810 S12: 0.1764 S13: 0.0608 REMARK 3 S21: -0.2198 S22: 0.0561 S23: 0.6511 REMARK 3 S31: 0.1112 S32: -0.2116 S33: 0.0392 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 9L9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 09-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300055287. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-OCT-13 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 : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60969 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 9.600 REMARK 200 R MERGE (I) : 0.06500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.90 REMARK 200 R MERGE FOR SHELL (I) : 0.86900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: 3S62 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG1500, EVAPORATION, TEMPERATURE REMARK 280 293.15K 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 34.79450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.36700 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.73450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.36700 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.79450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.73450 REMARK 290 SMTRY3 4 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: 3720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 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 OE1 GLU L 104 HH TYR L 172 1.49 REMARK 500 HH TYR H 95 O HOH H 306 1.57 REMARK 500 O HOH L 302 O HOH L 308 1.82 REMARK 500 O HOH H 467 O HOH H 475 1.87 REMARK 500 O HOH H 444 O HOH H 477 1.89 REMARK 500 O HOH H 438 O HOH H 471 1.92 REMARK 500 O HOH H 446 O HOH H 464 1.97 REMARK 500 O HOH H 391 O HOH H 467 1.99 REMARK 500 O HOH H 449 O HOH L 450 1.99 REMARK 500 O HOH H 393 O HOH H 417 2.02 REMARK 500 O HOH L 325 O HOH L 370 2.04 REMARK 500 OE1 GLU L 184 O HOH L 301 2.05 REMARK 500 O HOH H 445 O HOH H 463 2.07 REMARK 500 O HOH H 411 O HOH H 441 2.10 REMARK 500 O HOH L 357 O HOH L 472 2.10 REMARK 500 OD1 ASN L 156 O HOH L 302 2.13 REMARK 500 O HOH L 435 O HOH L 456 2.13 REMARK 500 O HOH H 321 O HOH H 400 2.14 REMARK 500 O HOH H 440 O HOH L 484 2.15 REMARK 500 NE2 GLN H 172 O HOH H 301 2.15 REMARK 500 O HOH L 461 O HOH L 491 2.16 REMARK 500 OD2 ASP H 99 O HOH H 302 2.17 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 HOH H 453 O HOH L 439 3454 2.05 REMARK 500 O HOH L 322 O HOH L 408 3554 2.15 REMARK 500 O HOH H 348 O HOH L 304 2455 2.16 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 VAL H 54 -61.23 66.93 REMARK 500 ASP H 66 33.59 -99.47 REMARK 500 LYS H 67 -37.65 -136.94 REMARK 500 ASP H 131 54.61 -93.85 REMARK 500 THR H 133 -115.58 68.17 REMARK 500 ASP H 174 16.39 57.47 REMARK 500 PRO H 216 -172.12 -61.11 REMARK 500 TRP L 46 -55.58 -127.10 REMARK 500 THR L 50 -48.03 77.52 REMARK 500 ALA L 83 174.86 179.84 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 479 DISTANCE = 5.85 ANGSTROMS REMARK 525 HOH H 480 DISTANCE = 6.13 ANGSTROMS DBREF 9L9Z H 1 217 PDB 9L9Z 9L9Z 1 217 DBREF 9L9Z L 1 213 PDB 9L9Z 9L9Z 1 213 SEQRES 1 H 217 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 H 217 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA LEU GLY SEQRES 3 H 217 TYR THR PHE SER ASP TYR GLU ILE HIS TRP MET LYS GLN SEQRES 4 H 217 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE HIS SEQRES 5 H 217 PRO VAL SER ASP THR THR ALA TYR ASN GLN LYS PHE LYS SEQRES 6 H 217 ASP LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 217 ALA TYR MET GLU VAL SER SER LEU THR SER GLU ASP SER SEQRES 8 H 217 ALA VAL TYR TYR CYS THR ARG ASP TYR GLY ALA TYR TRP SEQRES 9 H 217 GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR SEQRES 10 H 217 THR ALA PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY SEQRES 11 H 217 ASP LYS THR GLY ILE SER VAL THR LEU GLY CYS LEU VAL SEQRES 12 H 217 LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SEQRES 13 H 217 SER GLY ALA LEU SER SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 H 217 VAL LEU GLN ALA ASP LEU TYR THR LEU SER SER SER VAL SEQRES 15 H 217 THR VAL THR SER SER THR TRP PRO SER GLN SER ILE THR SEQRES 16 H 217 CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP SEQRES 17 H 217 LYS LYS ILE GLU PRO ARG GLY PRO ALA SEQRES 1 L 213 PCA ILE PHE LEU THR GLN SER PRO ALA SER MET SER ALA SEQRES 2 L 213 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3 L 213 SER SER VAL SER TYR MET SER TRP TYR GLN GLN LYS PRO SEQRES 4 L 213 ARG SER SER PRO LYS PRO TRP ILE TYR LEU THR SER ASN SEQRES 5 L 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 213 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 L 213 PRO GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 L 213 SER ASN PRO PHE THR PHE GLY SER GLY THR LYS LEU GLU SEQRES 9 L 213 ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 L 213 ASN ARG ASN GLU CYS HET PCA H 1 14 HET PCA L 1 14 HETNAM PCA PYROGLUTAMIC ACID FORMUL 1 PCA 2(C5 H7 N O3) FORMUL 3 HOH *376(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 GLN H 62 LYS H 65 5 4 HELIX 3 AA3 THR H 87 SER H 91 5 5 HELIX 4 AA4 ARG H 98 ALA H 102 5 5 HELIX 5 AA5 SER H 157 ALA H 159 5 3 HELIX 6 AA6 PRO H 201 SER H 204 5 4 HELIX 7 AA7 GLU L 78 ALA L 82 5 5 HELIX 8 AA8 GLU L 122 SER L 126 5 5 HELIX 9 AA9 LYS L 182 GLU L 186 1 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 LEU H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 VAL H 83 -1 O MET H 81 N LEU H 20 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 108 VAL H 112 1 O LEU H 109 N GLU H 10 SHEET 3 AA2 6 ALA H 92 THR H 97 -1 N ALA H 92 O VAL H 110 SHEET 4 AA2 6 ILE H 34 THR H 40 -1 N MET H 37 O TYR H 95 SHEET 5 AA2 6 GLY H 44 HIS H 52 -1 O ILE H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 60 -1 O ALA H 59 N ALA H 50 SHEET 1 AA3 4 SER H 121 LEU H 125 0 SHEET 2 AA3 4 SER H 136 TYR H 146 -1 O LYS H 144 N SER H 121 SHEET 3 AA3 4 LEU H 175 THR H 185 -1 O LEU H 178 N VAL H 143 SHEET 4 AA3 4 VAL H 164 THR H 166 -1 N HIS H 165 O SER H 181 SHEET 1 AA4 4 SER H 121 LEU H 125 0 SHEET 2 AA4 4 SER H 136 TYR H 146 -1 O LYS H 144 N SER H 121 SHEET 3 AA4 4 LEU H 175 THR H 185 -1 O LEU H 178 N VAL H 143 SHEET 4 AA4 4 VAL H 170 GLN H 172 -1 N GLN H 172 O LEU H 175 SHEET 1 AA5 3 THR H 152 TRP H 155 0 SHEET 2 AA5 3 THR H 195 HIS H 200 -1 O ASN H 197 N THR H 154 SHEET 3 AA5 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA6 4 LEU L 4 SER L 7 0 SHEET 2 AA6 4 VAL L 19 ALA L 25 -1 O SER L 24 N THR L 5 SHEET 3 AA6 4 SER L 69 ILE L 74 -1 O ILE L 74 N VAL L 19 SHEET 4 AA6 4 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73 SHEET 1 AA7 6 SER L 10 ALA L 13 0 SHEET 2 AA7 6 THR L 101 ILE L 105 1 O GLU L 104 N MET L 11 SHEET 3 AA7 6 ALA L 83 GLN L 89 -1 N ALA L 83 O LEU L 103 SHEET 4 AA7 6 MET L 32 GLN L 37 -1 N SER L 33 O GLN L 88 SHEET 5 AA7 6 LYS L 44 TYR L 48 -1 O ILE L 47 N TRP L 34 SHEET 6 AA7 6 ASN L 52 LEU L 53 -1 O ASN L 52 N TYR L 48 SHEET 1 AA8 4 THR L 113 PHE L 117 0 SHEET 2 AA8 4 GLY L 128 PHE L 138 -1 O VAL L 132 N PHE L 117 SHEET 3 AA8 4 TYR L 172 THR L 181 -1 O LEU L 180 N ALA L 129 SHEET 4 AA8 4 VAL L 158 TRP L 162 -1 N SER L 161 O SER L 175 SHEET 1 AA9 4 SER L 152 ARG L 154 0 SHEET 2 AA9 4 ASN L 144 ILE L 149 -1 N ILE L 149 O SER L 152 SHEET 3 AA9 4 SER L 190 THR L 196 -1 O GLU L 194 N LYS L 146 SHEET 4 AA9 4 ILE L 204 ASN L 209 -1 O ILE L 204 N ALA L 195 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 129 CYS L 213 1555 1555 2.03 SSBOND 3 CYS H 141 CYS H 196 1555 1555 2.04 SSBOND 4 CYS L 23 CYS L 87 1555 1555 2.04 SSBOND 5 CYS L 133 CYS L 193 1555 1555 2.04 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 LINK C PCA L 1 N ILE L 2 1555 1555 1.33 CISPEP 1 PHE H 147 PRO H 148 0 -3.02 CISPEP 2 GLU H 149 PRO H 150 0 -0.02 CISPEP 3 TRP H 189 PRO H 190 0 6.42 CISPEP 4 SER L 7 PRO L 8 0 -4.09 CISPEP 5 ASN L 93 PRO L 94 0 -1.54 CISPEP 6 TYR L 139 PRO L 140 0 3.94 CRYST1 69.589 69.469 78.734 90.00 90.00 90.00 P 21 21 21 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 0.014370 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014395 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012701 0.00000