HEADER VIRAL PROTEIN/IMMUNE SYSTEM 16-OCT-23 8ULH TITLE FAB OF RSV NEUTRALIZING ANTIBODY 1G12 CAVEAT 8ULH RESIDUES PRO H 134 AND GLY H 142 THAT ARE NEXT TO EACH OTHER CAVEAT 2 8ULH IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 3 8ULH BETWEEN C AND N IS 12.23. COMPND MOL_ID: 1; COMPND 2 MOLECULE: 1G12 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 1G12 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEUTRALIZING, ANTIBODY, RSV, ANTIVIRAL, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.D.HARSHBARGER,E.ANDREANO,E.MALITO REVDAT 1 06-NOV-24 8ULH 0 JRNL AUTH Y.XIAN,E.ANDREANO,S.TIAN,E.PHUNG,L.GARBINSKI,M.BIANCUCCI, JRNL AUTH 2 G.LOFANO,C.P.MALLETT,A.BALSARAF,Y.HUANG,F.BURICCHI,O.FINCO, JRNL AUTH 3 R.RAPPUOLI,M.J.BOTTOMLEY,S.CHANDRAMOULI,L.WARTER,J.WILLIAMS, JRNL AUTH 4 E.MALITO,W.D.HARSHBARGER JRNL TITL STRUCTURAL AND FUNCTIONAL PROPERTIES OF MONOCLONAL AND JRNL TITL 2 VACCINE-INDUCED ANTIBODIES TARGETING EPITOPES OF EMERGING JRNL TITL 3 RSV VARIANTS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.69 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) : 1.69 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 77.7 REMARK 3 NUMBER OF REFLECTIONS : 63223 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.180 REMARK 3 FREE R VALUE TEST SET COUNT : 3138 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 34.0800 - 4.7400 0.99 5551 174 0.1969 0.2102 REMARK 3 2 4.7400 - 3.7600 0.99 5515 183 0.1623 0.1896 REMARK 3 3 3.7600 - 3.2900 1.00 5599 186 0.1756 0.2136 REMARK 3 4 3.2900 - 2.9900 1.00 5592 188 0.1924 0.2423 REMARK 3 5 2.9900 - 2.7700 1.00 5579 173 0.2019 0.2772 REMARK 3 6 2.7700 - 2.6100 1.00 5594 182 0.2089 0.2125 REMARK 3 7 2.6100 - 2.4800 0.98 5481 182 0.2042 0.2263 REMARK 3 8 2.4800 - 2.3700 0.99 5552 180 0.2023 0.2713 REMARK 3 9 2.3700 - 2.2800 0.99 5552 183 0.2018 0.1974 REMARK 3 10 2.2800 - 2.2000 0.98 5476 175 0.1909 0.2564 REMARK 3 11 2.2000 - 2.1300 0.93 5211 177 0.1869 0.2349 REMARK 3 12 2.1300 - 2.0700 0.87 4790 162 0.1815 0.2189 REMARK 3 13 2.0700 - 2.0200 0.79 4369 144 0.1837 0.1994 REMARK 3 14 2.0200 - 1.9700 0.73 4088 131 0.1822 0.1919 REMARK 3 15 1.9700 - 1.9200 0.65 3603 121 0.2155 0.2430 REMARK 3 16 1.9200 - 1.8800 0.60 3385 114 0.2216 0.2555 REMARK 3 17 1.8800 - 1.8400 0.56 3124 105 0.2322 0.2652 REMARK 3 18 1.8400 - 1.8100 0.49 2747 88 0.2319 0.3103 REMARK 3 19 1.8100 - 1.7800 0.45 2491 83 0.2424 0.2842 REMARK 3 20 1.7800 - 1.7500 0.43 2386 77 0.2536 0.2968 REMARK 3 21 1.7500 - 1.7200 0.39 2178 72 0.2722 0.2757 REMARK 3 22 1.7200 - 1.6900 0.31 1778 58 0.3071 0.3033 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) : 0.181 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.331 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 12.95 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.84 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 : 0.012 3330 REMARK 3 ANGLE : 1.205 4539 REMARK 3 CHIRALITY : 0.066 511 REMARK 3 PLANARITY : 0.009 579 REMARK 3 DIHEDRAL : 28.338 459 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 8ULH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1000278356. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-JUN-19 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 : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 1.20.1_4487 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66305 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690 REMARK 200 RESOLUTION RANGE LOW (A) : 34.080 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.6700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM HEPES PH 7.5, 150 MM NACL, 5% REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 31.72800 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.11700 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.28150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.11700 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.72800 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.28150 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3150 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 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 LYS H 222 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 GLY H 227 REMARK 465 SER H 228 REMARK 465 GLU H 229 REMARK 465 ASN H 230 REMARK 465 LEU H 231 REMARK 465 TYR H 232 REMARK 465 PHE H 233 REMARK 465 GLN H 234 REMARK 465 GLY H 235 REMARK 465 SER H 236 REMARK 465 TRP H 237 REMARK 465 SER H 238 REMARK 465 HIS H 239 REMARK 465 PRO H 240 REMARK 465 GLN H 241 REMARK 465 PHE H 242 REMARK 465 GLU H 243 REMARK 465 LYS H 244 REMARK 465 GLY H 245 REMARK 465 GLY H 246 REMARK 465 GLY H 247 REMARK 465 SER H 248 REMARK 465 GLY H 249 REMARK 465 GLY H 250 REMARK 465 GLY H 251 REMARK 465 SER H 252 REMARK 465 GLY H 253 REMARK 465 GLY H 254 REMARK 465 GLY H 255 REMARK 465 SER H 256 REMARK 465 TRP H 257 REMARK 465 SER H 258 REMARK 465 HIS H 259 REMARK 465 PRO H 260 REMARK 465 GLN H 261 REMARK 465 PHE H 262 REMARK 465 GLU H 263 REMARK 465 LYS H 264 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 HOH H 404 O HOH H 509 2.03 REMARK 500 O HOH L 308 O HOH L 430 2.07 REMARK 500 O HOH L 541 O HOH L 597 2.08 REMARK 500 O HOH L 357 O HOH L 464 2.08 REMARK 500 O HOH L 461 O HOH L 593 2.09 REMARK 500 OD1 ASN L 175 O HOH L 301 2.10 REMARK 500 O HOH L 516 O HOH L 593 2.12 REMARK 500 O HOH H 574 O HOH H 630 2.13 REMARK 500 O HOH H 509 O HOH L 543 2.13 REMARK 500 OE1 GLN L 172 N ASN L 174 2.14 REMARK 500 O HOH L 313 O HOH L 514 2.14 REMARK 500 O HOH H 479 O HOH H 542 2.14 REMARK 500 O HOH H 496 O HOH H 541 2.15 REMARK 500 O PRO H 221 O HOH H 301 2.16 REMARK 500 O HOH H 515 O HOH H 613 2.16 REMARK 500 O HOH L 376 O HOH L 517 2.16 REMARK 500 O HOH H 374 O HOH H 556 2.17 REMARK 500 O HOH L 455 O HOH L 536 2.17 REMARK 500 O HOH L 568 O HOH L 597 2.18 REMARK 500 O HOH H 654 O HOH H 662 2.18 REMARK 500 O HOH H 385 O HOH H 463 2.18 REMARK 500 NE2 GLN H 1 O HOH H 302 2.18 REMARK 500 OG1 THR L 74 O HOH L 302 2.18 REMARK 500 O HOH L 493 O HOH L 541 2.19 REMARK 500 O HOH H 563 O HOH H 648 2.19 REMARK 500 O HOH L 628 O HOH L 633 2.19 REMARK 500 O HOH H 324 O HOH H 382 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 HOH L 547 O HOH L 561 4445 2.11 REMARK 500 O HOH L 591 O HOH L 603 4545 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO L 169 CG PRO L 169 CD -0.459 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 LEU L 109 CA - CB - CG ANGL. DEV. = -17.6 DEGREES REMARK 500 PRO L 169 CA - CB - CG ANGL. DEV. = -25.8 DEGREES REMARK 500 PRO L 169 N - CD - CG ANGL. DEV. = -23.8 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 LEU H 107 -71.09 -115.61 REMARK 500 VAL L 56 -51.81 71.28 REMARK 500 ASN L 133 32.77 72.30 REMARK 500 ALA L 162 -173.49 63.59 REMARK 500 SER L 205 -79.65 -126.78 REMARK 500 THR L 206 104.95 -173.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER L 173 ASN L 174 144.17 REMARK 500 PRO L 213 THR L 214 -147.71 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 660 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH H 661 DISTANCE = 6.15 ANGSTROMS REMARK 525 HOH H 662 DISTANCE = 6.16 ANGSTROMS REMARK 525 HOH H 663 DISTANCE = 6.52 ANGSTROMS REMARK 525 HOH H 664 DISTANCE = 6.65 ANGSTROMS REMARK 525 HOH H 665 DISTANCE = 7.03 ANGSTROMS REMARK 525 HOH H 666 DISTANCE = 7.40 ANGSTROMS REMARK 525 HOH L 628 DISTANCE = 5.85 ANGSTROMS REMARK 525 HOH L 629 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH L 630 DISTANCE = 6.11 ANGSTROMS REMARK 525 HOH L 631 DISTANCE = 6.25 ANGSTROMS REMARK 525 HOH L 632 DISTANCE = 7.51 ANGSTROMS REMARK 525 HOH L 633 DISTANCE = 7.88 ANGSTROMS DBREF 8ULH H 1 264 PDB 8ULH 8ULH 1 264 DBREF 8ULH L 1 214 PDB 8ULH 8ULH 1 214 SEQRES 1 H 257 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 257 SER GLY ALA SER VAL GLN VAL SER CYS LYS ALA SER GLY SEQRES 3 H 257 TYR PRO PHE GLY ASN TYR GLY ILE THR TRP VAL ARG GLN SEQRES 4 H 257 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE SER SEQRES 5 H 257 ALA TYR ASN GLY GLN THR TYR TYR ALA GLU LYS PHE GLN SEQRES 6 H 257 GLY ARG VAL THR MET THR THR ASP THR SER THR SER THR SEQRES 7 H 257 GLY TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR SEQRES 8 H 257 ALA VAL TYR PHE CYS ALA ARG ASP VAL PRO VAL VAL ALA SEQRES 9 H 257 ALA VAL LEU ARG ASP TYR TRP GLY GLN GLY VAL THR VAL SEQRES 10 H 257 SER SER SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 257 PRO LEU ALA PRO GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 H 257 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 H 257 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 H 257 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 H 257 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 H 257 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 H 257 ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS GLY SER SEQRES 18 H 257 GLU ASN LEU TYR PHE GLN GLY SER TRP SER HIS PRO GLN SEQRES 19 H 257 PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SEQRES 20 H 257 GLY SER TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 L 214 VAL LYS GLY MET THR GLN SER PRO LEU PHE LEU PRO VAL SEQRES 2 L 214 THR LEU GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 214 GLN SER LEU VAL HIS SER ASP GLY ASN ILE TYR LEU SER SEQRES 4 L 214 TRP PHE GLN GLN ARG PRO GLY GLN SER PRO ARG ARG LEU SEQRES 5 L 214 ILE TYR LYS VAL PHE ASP ARG ASP SER GLY VAL PRO ASP SEQRES 6 L 214 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 214 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL ALA HIS TYR SEQRES 8 L 214 TYR CYS MET GLN ALA THR HIS TRP PRO GLY THR PHE GLY SEQRES 9 L 214 GLY GLY THR LYS LEU THR VAL LEU ARG THR VAL ALA ALA SEQRES 10 L 214 PRO SER VAL PHE LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 214 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 214 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 214 SER SER PRO SER LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 214 SER LYS GLN SER ASN ASN LYS TYR SER LEU SER SER VAL SEQRES 15 L 214 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 214 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 214 LYS THR PHE ALA PRO THR FORMUL 3 HOH *699(H2 O) HELIX 1 AA1 PRO H 28 ASN H 31 5 4 HELIX 2 AA2 THR H 74 THR H 76 5 3 HELIX 3 AA3 ARG H 87 THR H 91 5 5 HELIX 4 AA4 SER H 164 ALA H 166 5 3 HELIX 5 AA5 SER H 195 GLY H 198 5 4 HELIX 6 AA6 LYS H 209 ASN H 212 5 4 HELIX 7 AA7 GLU L 84 VAL L 88 5 5 HELIX 8 AA8 SER L 126 ALA L 132 1 7 HELIX 9 AA9 THR L 186 SER L 192 1 7 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20 SHEET 4 AA1 4 VAL H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA2 6 GLU H 10 LYS H 13 0 SHEET 2 AA2 6 VAL H 115 SER H 120 1 O SER H 118 N LYS H 12 SHEET 3 AA2 6 ALA H 92 ASP H 99 -1 N ALA H 92 O VAL H 117 SHEET 4 AA2 6 GLY H 33 GLN H 39 -1 N VAL H 37 O PHE H 95 SHEET 5 AA2 6 GLU H 46 SER H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O TYR H 59 N TRP H 50 SHEET 1 AA3 4 SER H 128 LEU H 132 0 SHEET 2 AA3 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA3 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AA3 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AA4 4 SER H 128 LEU H 132 0 SHEET 2 AA4 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA4 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AA4 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AA5 3 THR H 159 TRP H 162 0 SHEET 2 AA5 3 ILE H 203 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AA5 3 THR H 213 ARG H 218 -1 O VAL H 215 N VAL H 206 SHEET 1 AA6 4 MET L 4 SER L 7 0 SHEET 2 AA6 4 ALA L 19 SER L 25 -1 O SER L 22 N SER L 7 SHEET 3 AA6 4 ASP L 75 ILE L 80 -1 O PHE L 76 N CYS L 23 SHEET 4 AA6 4 PHE L 67 SER L 72 -1 N SER L 68 O LYS L 79 SHEET 1 AA7 6 PHE L 10 VAL L 13 0 SHEET 2 AA7 6 THR L 107 VAL L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AA7 6 HIS L 90 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA7 6 LEU L 38 GLN L 43 -1 N SER L 39 O MET L 94 SHEET 5 AA7 6 ARG L 50 TYR L 54 -1 O LEU L 52 N TRP L 40 SHEET 6 AA7 6 ASP L 58 ARG L 59 -1 O ASP L 58 N TYR L 54 SHEET 1 AA8 4 PHE L 10 VAL L 13 0 SHEET 2 AA8 4 THR L 107 VAL L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AA8 4 HIS L 90 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA8 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AA9 4 SER L 119 PHE L 123 0 SHEET 2 AA9 4 ALA L 135 PHE L 144 -1 O SER L 142 N SER L 119 SHEET 3 AA9 4 TYR L 177 LEU L 185 -1 O LEU L 185 N ALA L 135 SHEET 4 AA9 4 VAL L 164 THR L 167 -1 N THR L 167 O SER L 180 SHEET 1 AB1 4 SER L 158 PRO L 159 0 SHEET 2 AB1 4 THR L 150 ALA L 155 -1 N ALA L 155 O SER L 158 SHEET 3 AB1 4 TYR L 196 THR L 201 -1 O GLN L 199 N ALA L 152 SHEET 4 AB1 4 VAL L 207 PHE L 211 -1 O VAL L 207 N VAL L 200 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.08 SSBOND 2 CYS H 148 CYS H 204 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 93 1555 1555 2.10 SSBOND 4 CYS L 139 CYS L 198 1555 1555 2.03 CISPEP 1 PHE H 154 PRO H 155 0 -3.11 CISPEP 2 GLU H 156 PRO H 157 0 0.87 CISPEP 3 SER L 7 PRO L 8 0 -8.62 CISPEP 4 TRP L 99 PRO L 100 0 -0.58 CISPEP 5 TYR L 145 PRO L 146 0 3.01 CRYST1 63.456 82.563 112.234 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 0.015759 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012112 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008910 0.00000