HEADER VIRAL PROTEIN 05-NOV-24 9KEP TITLE RABV-G-PHD-FD/NM57-SCFV COMPND MOL_ID: 1; COMPND 2 MOLECULE: NM57-SCFV LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RABV-G-PHD-FD; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NM57-SCFV HEAVY CHAIN; COMPND 11 CHAIN: D; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: RABIES VIRUS CVS-11; SOURCE 8 ORGANISM_TAXID: 11294; SOURCE 9 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS RABIES VIRUS, GLYCOPROTEIN, NEUTRALIZING ANTIBODY, SO57, VIRAL KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.LU,F.YANG,Y.KEQING,S.LIN REVDAT 1 23-APR-25 9KEP 0 JRNL AUTH F.YANG,L.ZHAI,K.YIN,S.LIN,J.YANG,F.YE,Z.CHEN,S.SHU,Y.YU, JRNL AUTH 2 L.GUO,B.HE,W.WANG,H.YE,Y.CAO,J.GAO,G.LU JRNL TITL MOLECULAR BASIS OF TWO BROAD-SPECTRUM ANTIBODIES JRNL TITL 2 NEUTRALIZING RABIES VIRUS AND OTHER PHYLOGROUP-I JRNL TITL 3 LYSSAVIRUSES BY BLOCKING STRUCTURAL TRANSITION BETWEEN THE JRNL TITL 4 PLECKSTRIN-HOMOLOGY AND FUSION DOMAINS IN THE GLYCOPROTEIN. JRNL REF INT.J.BIOL.MACROMOL. V. 308 42570 2025 JRNL REFN ISSN 0141-8130 JRNL PMID 40154685 JRNL DOI 10.1016/J.IJBIOMAC.2025.142570 REMARK 2 REMARK 2 RESOLUTION. 2.89 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.79 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 11423 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.236 REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.281 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.530 REMARK 3 FREE R VALUE TEST SET COUNT : 517 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 29.7900 - 4.5800 1.00 2804 121 0.2178 0.2822 REMARK 3 2 4.5800 - 3.6400 1.00 2718 129 0.2131 0.2644 REMARK 3 3 3.6400 - 3.1800 1.00 2715 122 0.2599 0.2658 REMARK 3 4 3.1800 - 2.8900 1.00 2669 145 0.3154 0.3461 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) : 0.440 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.660 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 : 0.004 NULL REMARK 3 ANGLE : 0.814 NULL REMARK 3 CHIRALITY : 0.048 444 REMARK 3 PLANARITY : 0.007 529 REMARK 3 DIHEDRAL : 6.476 420 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 10.3121 -3.2511 23.3193 REMARK 3 T TENSOR REMARK 3 T11: 0.5120 T22: 0.4944 REMARK 3 T33: 0.4405 T12: -0.0414 REMARK 3 T13: 0.0138 T23: -0.0184 REMARK 3 L TENSOR REMARK 3 L11: 1.2932 L22: 1.2643 REMARK 3 L33: 1.8947 L12: 0.3266 REMARK 3 L13: 0.4383 L23: 0.6603 REMARK 3 S TENSOR REMARK 3 S11: -0.1131 S12: 0.3645 S13: 0.1066 REMARK 3 S21: -0.4253 S22: -0.0223 S23: 0.0527 REMARK 3 S31: -0.1835 S32: -0.0132 S33: 0.1149 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 9KEP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300053394. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-23 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 : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11423 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890 REMARK 200 RESOLUTION RANGE LOW (A) : 29.790 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : 0.14200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.37300 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.29 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 180 MM CALCIUM CHLORIDE, 24% PEG3350, REMARK 280 4% V/V POLYPROPYLENE GLYCOL P 400, AND 20% V/V GLYCEROL, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 57.16500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.74000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.16500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.74000 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D 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 GLN A 114 REMARK 465 PRO A 115 REMARK 465 LYS A 116 REMARK 465 LEU B 28 REMARK 465 VAL B 29 REMARK 465 LEU B 38 REMARK 465 SER B 39 REMARK 465 GLU B 40 REMARK 465 LYS B 47 REMARK 465 VAL B 48 REMARK 465 GLY B 49 REMARK 465 TYR B 50 REMARK 465 ILE B 51 REMARK 465 VAL B 66 REMARK 465 VAL B 67 REMARK 465 THR B 68 REMARK 465 GLU B 69 REMARK 465 ALA B 70 REMARK 465 GLU B 71 REMARK 465 THR B 72 REMARK 465 TYR B 73 REMARK 465 THR B 74 REMARK 465 GLY B 75 REMARK 465 GLY B 76 REMARK 465 SER B 77 REMARK 465 GLY B 78 REMARK 465 GLY B 79 REMARK 465 THR B 80 REMARK 465 THR B 81 REMARK 465 PHE B 82 REMARK 465 LYS B 83 REMARK 465 ARG B 84 REMARK 465 LYS B 85 REMARK 465 MET B 106 REMARK 465 ALA B 107 REMARK 465 GLY B 108 REMARK 465 ASP B 109 REMARK 465 PRO B 110 REMARK 465 ARG B 111 REMARK 465 TYR B 112 REMARK 465 GLU B 113 REMARK 465 GLU B 114 REMARK 465 SER B 115 REMARK 465 LEU B 116 REMARK 465 HIS B 117 REMARK 465 ASN B 118 REMARK 465 PRO B 119 REMARK 465 TYR B 120 REMARK 465 GLY B 121 REMARK 465 GLY B 122 REMARK 465 SER B 123 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 ARG B 126 REMARK 465 THR B 127 REMARK 465 THR B 128 REMARK 465 LYS B 129 REMARK 465 GLU B 130 REMARK 465 SER B 131 REMARK 465 LEU B 132 REMARK 465 ILE B 162 REMARK 465 THR B 163 REMARK 465 VAL B 164 REMARK 465 ARG B 184 REMARK 465 PRO B 185 REMARK 465 SER B 246 REMARK 465 ASP B 247 REMARK 465 GLU B 248 REMARK 465 PRO B 253 REMARK 465 PRO B 254 REMARK 465 ASP B 255 REMARK 465 GLN B 256 REMARK 465 LEU B 257 REMARK 465 VAL B 258 REMARK 465 ASN B 259 REMARK 465 LEU B 260 REMARK 465 HIS B 261 REMARK 465 ASP B 262 REMARK 465 PHE B 263 REMARK 465 ARG B 264 REMARK 465 SER B 265 REMARK 465 ASP B 266 REMARK 465 GLU B 267 REMARK 465 ILE B 268 REMARK 465 GLU B 269 REMARK 465 HIS B 270 REMARK 465 HIS B 271 REMARK 465 HIS B 272 REMARK 465 HIS B 273 REMARK 465 HIS B 274 REMARK 465 HIS B 275 REMARK 465 HIS B 276 REMARK 465 GLN D 1 REMARK 465 SER D 127 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 OG1 THR B 171 OG1 THR B 176 2.13 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 B 89 CD PRO B 89 N 0.175 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 ARG B 88 N - CA - C ANGL. DEV. = 16.6 DEGREES REMARK 500 PRO B 89 CA - N - CD ANGL. DEV. = -12.3 DEGREES REMARK 500 PRO B 89 N - CA - CB ANGL. DEV. = 7.9 DEGREES REMARK 500 ALA B 200 CB - CA - C ANGL. DEV. = -22.6 DEGREES REMARK 500 SER B 201 CB - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 SER B 201 N - CA - CB ANGL. DEV. = -15.1 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 CYS A 22 119.02 -164.35 REMARK 500 PHE A 34 100.68 -162.30 REMARK 500 CYS B 159 -178.27 -171.47 REMARK 500 THR B 171 -161.03 -106.85 REMARK 500 ARG B 196 12.68 -143.07 REMARK 500 MET B 243 -166.90 -118.85 REMARK 500 LYS D 12 -157.89 -135.45 REMARK 500 CYS D 22 114.51 -163.94 REMARK 500 SER D 25 -65.03 -91.56 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 LYS B 198 ARG B 199 -146.82 REMARK 500 LYS D 12 LYS D 13 -147.10 REMARK 500 REMARK 500 REMARK: NULL DBREF 9KEP A 1 116 PDB 9KEP 9KEP 1 116 DBREF 9KEP B 28 276 PDB 9KEP 9KEP 28 276 DBREF 9KEP D 1 127 PDB 9KEP 9KEP 1 127 SEQRES 1 A 116 GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SER SEQRES 2 A 116 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 A 116 SER ASP ILE GLY GLY TYR ASN PHE VAL SER TRP TYR GLN SEQRES 4 A 116 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 A 116 ALA THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 A 116 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 A 116 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS CYS SEQRES 8 A 116 SER TYR ALA GLY ASP TYR THR PRO GLY VAL VAL PHE GLY SEQRES 9 A 116 GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS SEQRES 1 B 243 LEU VAL VAL GLU ASP GLU GLY CYS THR ASN LEU SER GLU SEQRES 2 B 243 PHE SER TYR MET GLU LEU LYS VAL GLY TYR ILE SER ALA SEQRES 3 B 243 ILE LYS VAL ASN GLY PHE THR CYS THR GLY VAL VAL THR SEQRES 4 B 243 GLU ALA GLU THR TYR THR GLY GLY SER GLY GLY THR THR SEQRES 5 B 243 PHE LYS ARG LYS HIS PHE ARG PRO THR PRO ASP ALA CYS SEQRES 6 B 243 ARG ALA ALA TYR ASN TRP LEU MET ALA GLY ASP PRO ARG SEQRES 7 B 243 TYR GLU GLU SER LEU HIS ASN PRO TYR GLY GLY SER GLY SEQRES 8 B 243 GLY ARG THR THR LYS GLU SER LEU ILE ILE ILE SER PRO SEQRES 9 B 243 SER VAL THR ASP LEU ASP PRO TYR ASP LYS SER LEU HIS SEQRES 10 B 243 SER ARG VAL PHE PRO GLY GLY LYS CYS SER GLY ILE THR SEQRES 11 B 243 VAL SER SER THR TYR CYS SER THR ASN HIS ASP TYR THR SEQRES 12 B 243 ILE TRP MET PRO GLU ASN PRO ARG PRO ARG THR PRO CYS SEQRES 13 B 243 ASP ILE PHE THR ASN SER ARG GLY LYS ARG ALA SER ASN SEQRES 14 B 243 GLY ASN LYS THR CYS GLY PHE VAL ASP GLU ARG GLY LEU SEQRES 15 B 243 TYR LYS SER LEU LYS GLY ALA CYS ARG LEU LYS LEU CYS SEQRES 16 B 243 GLY VAL LEU GLY LEU ARG LEU MET ASP GLY THR TRP VAL SEQRES 17 B 243 ALA MET GLN THR SER ASP GLU THR LYS TRP CYS PRO PRO SEQRES 18 B 243 ASP GLN LEU VAL ASN LEU HIS ASP PHE ARG SER ASP GLU SEQRES 19 B 243 ILE GLU HIS HIS HIS HIS HIS HIS HIS SEQRES 1 D 127 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 D 127 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 D 127 GLY THR PHE ASN ARG TYR THR VAL ASN TRP VAL ARG GLN SEQRES 4 D 127 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 D 127 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN ARG PHE GLN SEQRES 6 D 127 GLY ARG LEU THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 D 127 ALA TYR MET GLU LEU SER SER LEU ARG SER ASP ASP THR SEQRES 8 D 127 ALA VAL TYR PHE CYS ALA ARG GLU ASN LEU ASP ASN SER SEQRES 9 D 127 GLY THR TYR TYR TYR PHE SER GLY TRP PHE ASP PRO TRP SEQRES 10 D 127 GLY GLN GLY THR LEU VAL THR VAL SER SER HELIX 1 AA1 GLN A 81 GLU A 85 5 5 HELIX 2 AA2 THR B 90 TRP B 100 1 11 HELIX 3 AA3 ARG D 87 THR D 91 5 5 SHEET 1 AA1 5 SER A 9 GLY A 12 0 SHEET 2 AA1 5 THR A 107 VAL A 111 1 O LYS A 108 N VAL A 10 SHEET 3 AA1 5 ALA A 86 TYR A 93 -1 N TYR A 88 O THR A 107 SHEET 4 AA1 5 VAL A 35 GLN A 40 -1 N GLN A 40 O ASP A 87 SHEET 5 AA1 5 LYS A 47 ILE A 50 -1 O LYS A 47 N GLN A 39 SHEET 1 AA2 4 SER A 9 GLY A 12 0 SHEET 2 AA2 4 THR A 107 VAL A 111 1 O LYS A 108 N VAL A 10 SHEET 3 AA2 4 ALA A 86 TYR A 93 -1 N TYR A 88 O THR A 107 SHEET 4 AA2 4 VAL A 101 PHE A 103 -1 O VAL A 102 N SER A 92 SHEET 1 AA3 3 VAL A 18 ILE A 20 0 SHEET 2 AA3 3 THR A 72 ILE A 77 -1 O LEU A 75 N ILE A 20 SHEET 3 AA3 3 PHE A 64 SER A 69 -1 N SER A 65 O THR A 76 SHEET 1 AA4 5 THR B 193 SER B 195 0 SHEET 2 AA4 5 TYR B 43 GLU B 45 -1 N TYR B 43 O SER B 195 SHEET 3 AA4 5 TRP B 240 ALA B 242 -1 O ALA B 242 N MET B 44 SHEET 4 AA4 5 VAL B 230 ARG B 234 -1 N LEU B 233 O VAL B 241 SHEET 5 AA4 5 CYS B 223 LEU B 227 -1 N CYS B 223 O ARG B 234 SHEET 1 AA5 3 LYS B 55 VAL B 56 0 SHEET 2 AA5 3 THR B 140 ASP B 143 -1 O THR B 140 N VAL B 56 SHEET 3 AA5 3 SER B 148 HIS B 150 -1 O HIS B 150 N ASP B 141 SHEET 1 AA6 3 ILE B 134 PRO B 137 0 SHEET 2 AA6 3 GLY B 58 THR B 62 -1 N THR B 62 O ILE B 134 SHEET 3 AA6 3 ILE B 177 PRO B 180 -1 O ILE B 177 N CYS B 61 SHEET 1 AA7 4 LEU D 4 GLN D 6 0 SHEET 2 AA7 4 VAL D 18 ALA D 24 -1 O LYS D 23 N VAL D 5 SHEET 3 AA7 4 THR D 78 LEU D 83 -1 O LEU D 83 N VAL D 18 SHEET 4 AA7 4 LEU D 68 ASP D 73 -1 N ASP D 73 O THR D 78 SHEET 1 AA8 6 GLU D 10 LYS D 12 0 SHEET 2 AA8 6 LEU D 122 VAL D 125 1 O THR D 124 N LYS D 12 SHEET 3 AA8 6 ALA D 92 ARG D 98 -1 N ALA D 92 O VAL D 123 SHEET 4 AA8 6 VAL D 34 GLN D 39 -1 N ASN D 35 O ALA D 97 SHEET 5 AA8 6 LEU D 45 ILE D 51 -1 O ILE D 51 N VAL D 34 SHEET 6 AA8 6 ALA D 58 TYR D 60 -1 O ASN D 59 N GLY D 50 SSBOND 1 CYS A 22 CYS A 90 1555 1555 2.04 SSBOND 2 CYS B 35 CYS B 207 1555 1555 2.03 SSBOND 3 CYS B 61 CYS B 94 1555 1555 2.03 SSBOND 4 CYS B 159 CYS B 169 1555 1555 2.03 SSBOND 5 CYS B 189 CYS B 228 1555 1555 2.03 SSBOND 6 CYS B 223 CYS B 252 1555 1555 2.03 SSBOND 7 CYS D 22 CYS D 96 1555 1555 2.03 CRYST1 114.330 49.480 100.860 90.00 117.62 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008747 0.000000 0.004577 0.00000 SCALE2 0.000000 0.020210 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011190 0.00000