HEADER IMMUNE SYSTEM 21-MAY-25 9ORE TITLE CRYOEM STRUCTURE OF 4F11 FAB BOUND TO STABILIZED MPV-2C HMPV PREF COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 4F11 HEAVY CHAIN; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: 4F11 LIGHT CHAIN; COMPND 19 CHAIN: L; COMPND 20 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN METAPNEUMOVIRUS; SOURCE 3 ORGANISM_TAXID: 162145; SOURCE 4 GENE: F, KMM_36597GPF; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN METAPNEUMOVIRUS; SOURCE 10 ORGANISM_TAXID: 162145; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HUMAN METAPNEUMOVIRUS; SOURCE 16 ORGANISM_TAXID: 162145; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IMMUNE SYSTEM, HMPV, PREFUSION F, ANTIBODY, SITE 0, GLYCAN DEPENDENT EXPDTA ELECTRON MICROSCOPY AUTHOR M.R.MCGOVERN,M.PANCERA REVDAT 1 30-JUL-25 9ORE 0 JRNL AUTH E.D.HARRIS,M.MCGOVERN,S.PERNIKOFF,R.IKEDA,L.KIPNIS,W.HANNON, JRNL AUTH 2 E.B.SOBOLIK,M.GRAY,A.L.GRENINGER,S.HE,C.N.CHIN,T.M.FU, JRNL AUTH 3 M.PANCERA,J.BOONYARATANAKORNKIT JRNL TITL DEVELOPMENT OF A POTENT MONOCLONAL ANTIBODY FOR TREATMENT OF JRNL TITL 2 HUMAN METAPNEUMOVIRUS INFECTIONS. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 40666860 JRNL DOI 10.1101/2025.06.09.657676 REMARK 2 REMARK 2 RESOLUTION. 4.13 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.130 REMARK 3 NUMBER OF PARTICLES : 276088 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9ORE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-25. REMARK 100 THE DEPOSITION ID IS D_1000293897. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : 4F11 FAB BOUND TO MPV-2C; MPV REMARK 245 -2C; 4F11 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, H, L, D, E 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 GLU H 1 REMARK 465 SER H 112 REMARK 465 SER H 113 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 H CYS A 292 HH TYR A 385 1.12 REMARK 500 HB2 CYS A 350 HA ILE A 354 1.20 REMARK 500 O THR B 337 H GLY B 340 1.23 REMARK 500 HD21 ASN C 172 HH11 ARG C 175 1.24 REMARK 500 HG SER A 371 HA CYS A 384 1.29 REMARK 500 O CYS C 350 H ILE C 352 1.36 REMARK 500 O LYS C 386 H VAL C 388 1.37 REMARK 500 HG SER B 291 OG SER B 443 1.43 REMARK 500 OE2 GLU A 294 H GLY A 297 1.48 REMARK 500 O SER C 347 H CYS C 350 1.49 REMARK 500 HE ARG C 40 OD1 ASP C 336 1.49 REMARK 500 O LYS A 348 HD21 ASN A 351 1.50 REMARK 500 HD22 ASN C 353 OG1 THR C 356 1.52 REMARK 500 O THR B 59 HD21 ASN B 180 1.52 REMARK 500 SG CYS A 350 HG13 ILE A 354 1.52 REMARK 500 O SER C 61 H GLY C 63 1.53 REMARK 500 H THR B 30 O LYS B 287 1.56 REMARK 500 O ASN A 466 OD1 ASN A 468 1.59 REMARK 500 SG CYS C 350 HG13 ILE C 354 1.59 REMARK 500 O THR B 337 N GLY B 340 2.19 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 SER A 29 CA SER A 29 CB -0.112 REMARK 500 SER B 29 CA SER B 29 CB -0.108 REMARK 500 SER C 29 CA SER C 29 CB -0.110 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 GLU A 25 CB - CA - C ANGL. DEV. = -32.6 DEGREES REMARK 500 GLU A 25 N - CA - CB ANGL. DEV. = -11.7 DEGREES REMARK 500 CYS A 28 CB - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 PRO A 282 N - CA - CB ANGL. DEV. = -18.3 DEGREES REMARK 500 PRO A 282 N - CA - C ANGL. DEV. = 21.8 DEGREES REMARK 500 CYS A 283 CA - CB - SG ANGL. DEV. = 9.7 DEGREES REMARK 500 CYS A 326 CB - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 CYS A 326 CA - CB - SG ANGL. DEV. = -10.9 DEGREES REMARK 500 CYS A 350 CB - CA - C ANGL. DEV. = 16.1 DEGREES REMARK 500 CYS A 350 CA - CB - SG ANGL. DEV. = 15.4 DEGREES REMARK 500 CYS A 384 CB - CA - C ANGL. DEV. = -13.5 DEGREES REMARK 500 CYS A 384 CA - CB - SG ANGL. DEV. = -13.5 DEGREES REMARK 500 TYR A 385 N - CA - CB ANGL. DEV. = -13.5 DEGREES REMARK 500 CYS B 60 CA - CB - SG ANGL. DEV. = -11.2 DEGREES REMARK 500 PRO B 282 N - CA - CB ANGL. DEV. = -8.9 DEGREES REMARK 500 PRO B 282 N - CD - CG ANGL. DEV. = -10.1 DEGREES REMARK 500 CYS B 283 CA - CB - SG ANGL. DEV. = 8.5 DEGREES REMARK 500 PRO B 290 N - CA - CB ANGL. DEV. = -10.8 DEGREES REMARK 500 CYS B 301 CA - CB - SG ANGL. DEV. = -13.0 DEGREES REMARK 500 CYS C 28 CB - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 CYS C 28 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 ASN C 172 CB - CA - C ANGL. DEV. = 19.4 DEGREES REMARK 500 PRO C 282 N - CA - CB ANGL. DEV. = -7.8 DEGREES REMARK 500 PRO C 282 N - CD - CG ANGL. DEV. = -12.7 DEGREES REMARK 500 CYS C 283 CB - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 CYS C 283 CA - CB - SG ANGL. DEV. = 16.5 DEGREES REMARK 500 CYS C 301 CA - CB - SG ANGL. DEV. = -12.8 DEGREES REMARK 500 PHE C 334 N - CA - CB ANGL. DEV. = -16.1 DEGREES REMARK 500 TYR C 385 CB - CA - C ANGL. DEV. = -12.6 DEGREES REMARK 500 TYR C 385 N - CA - CB ANGL. DEV. = 11.6 DEGREES REMARK 500 LYS C 386 CB - CA - C ANGL. DEV. = -32.1 DEGREES REMARK 500 CYS C 390 CB - CA - C ANGL. DEV. = -13.4 DEGREES REMARK 500 ARG H 38 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 TYR H 52 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 ARG L 24 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG L 27C NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES REMARK 500 TYR L 32 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 ARG L 61 NE - CZ - NH2 ANGL. DEV. = 3.7 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 GLU A 25 -7.09 -40.52 REMARK 500 GLU A 26 -70.96 -56.55 REMARK 500 CYS A 28 129.91 -34.92 REMARK 500 SER A 29 129.24 177.06 REMARK 500 ASP A 54 34.19 -93.70 REMARK 500 ASN A 57 55.39 -90.31 REMARK 500 CYS A 60 104.84 -45.89 REMARK 500 SER A 61 26.23 -145.79 REMARK 500 ASP A 87 19.41 -140.70 REMARK 500 ILE A 177 -70.90 -57.17 REMARK 500 ASN A 178 157.99 58.00 REMARK 500 LYS A 179 -109.81 49.72 REMARK 500 ASP A 185 39.17 -79.69 REMARK 500 LEU A 187 -49.77 59.96 REMARK 500 PRO A 282 50.78 -31.27 REMARK 500 SER A 291 84.84 -59.06 REMARK 500 GLU A 349 -66.45 -24.52 REMARK 500 CYS A 350 9.25 -62.53 REMARK 500 ILE A 352 -95.89 -134.70 REMARK 500 PRO A 360 88.39 -68.40 REMARK 500 LYS A 386 173.60 72.22 REMARK 500 LYS A 405 -89.43 -70.80 REMARK 500 CYS A 407 128.20 -34.73 REMARK 500 ASP A 421 -82.21 17.11 REMARK 500 GLU B 26 6.21 -66.27 REMARK 500 SER B 27 89.78 -173.18 REMARK 500 CYS B 28 125.09 -29.67 REMARK 500 SER B 29 123.72 -177.31 REMARK 500 CYS B 60 -155.56 -110.45 REMARK 500 SER B 61 -60.93 -159.13 REMARK 500 ASP B 62 -20.00 -36.82 REMARK 500 ASN B 180 -1.11 65.20 REMARK 500 ASP B 183 48.45 -76.71 REMARK 500 ASP B 186 -69.04 -29.88 REMARK 500 LEU B 187 -35.74 65.78 REMARK 500 CYS B 283 110.54 -171.08 REMARK 500 TYR B 299 -168.04 -117.05 REMARK 500 ALA B 300 105.78 -172.28 REMARK 500 ARG B 304 141.44 -33.82 REMARK 500 CYS B 326 131.83 179.97 REMARK 500 THR B 337 -64.66 -29.50 REMARK 500 ALA B 338 -30.44 -32.32 REMARK 500 ILE B 352 -50.60 -123.61 REMARK 500 LYS B 386 -133.12 30.32 REMARK 500 ILE B 400 -61.40 -95.27 REMARK 500 SER C 27 51.03 -165.56 REMARK 500 CYS C 28 79.47 14.58 REMARK 500 ASP C 62 29.46 -57.47 REMARK 500 SER C 170 -71.51 -73.33 REMARK 500 ASN C 172 -69.12 -106.80 REMARK 500 REMARK 500 THIS ENTRY HAS 88 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 90 0.21 SIDE CHAIN REMARK 500 ARG C 91 0.23 SIDE CHAIN REMARK 500 TYR H 91 0.08 SIDE CHAIN REMARK 500 PHE H 98 0.08 SIDE CHAIN REMARK 500 TYR L 32 0.08 SIDE CHAIN REMARK 500 TYR L 36 0.06 SIDE CHAIN REMARK 500 ARG L 54 0.15 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLU B 26 -15.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-70773 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF 4F11 FAB BOUND TO STABILIZED MPV-2C HMPV PREF DBREF 9ORE A 20 467 UNP C6F440 C6F440_9MONO 20 467 DBREF 9ORE B 19 467 UNP Q8B9P3 Q8B9P3_9MONO 19 467 DBREF 9ORE C 19 467 UNP Q8B9P3 Q8B9P3_9MONO 19 467 DBREF 9ORE H 1 113 PDB 9ORE 9ORE 1 113 DBREF 9ORE L 1 107 PDB 9ORE 9ORE 1 107 SEQADV 9ORE A UNP C6F440 ALA 90 DELETION SEQADV 9ORE A UNP C6F440 ARG 91 DELETION SEQADV 9ORE A UNP C6F440 GLU 92 DELETION SEQADV 9ORE A UNP C6F440 GLU 93 DELETION SEQADV 9ORE A UNP C6F440 GLN 94 DELETION SEQADV 9ORE A UNP C6F440 ILE 95 DELETION SEQADV 9ORE A UNP C6F440 GLU 96 DELETION SEQADV 9ORE A UNP C6F440 ASN 97 DELETION SEQADV 9ORE A UNP C6F440 PRO 98 DELETION SEQADV 9ORE A UNP C6F440 ARG 99 DELETION SEQADV 9ORE A UNP C6F440 GLN 100 DELETION SEQADV 9ORE A UNP C6F440 SER 101 DELETION SEQADV 9ORE ARG A 112 UNP C6F440 VAL 112 CONFLICT SEQADV 9ORE GLU A 209 UNP C6F440 ASP 209 CONFLICT SEQADV 9ORE ILE A 231 UNP C6F440 VAL 231 CONFLICT SEQADV 9ORE ASN A 368 UNP C6F440 HIS 368 CONFLICT SEQADV 9ORE PRO A 453 UNP C6F440 GLU 453 CONFLICT SEQADV 9ORE ASN A 468 UNP C6F440 EXPRESSION TAG SEQADV 9ORE B UNP Q8B9P3 ALA 90 DELETION SEQADV 9ORE B UNP Q8B9P3 ARG 91 DELETION SEQADV 9ORE B UNP Q8B9P3 GLU 92 DELETION SEQADV 9ORE B UNP Q8B9P3 GLU 93 DELETION SEQADV 9ORE B UNP Q8B9P3 GLN 94 DELETION SEQADV 9ORE B UNP Q8B9P3 ILE 95 DELETION SEQADV 9ORE B UNP Q8B9P3 GLU 96 DELETION SEQADV 9ORE B UNP Q8B9P3 ASN 97 DELETION SEQADV 9ORE B UNP Q8B9P3 PRO 98 DELETION SEQADV 9ORE B UNP Q8B9P3 ARG 99 DELETION SEQADV 9ORE B UNP Q8B9P3 GLN 100 DELETION SEQADV 9ORE B UNP Q8B9P3 SER 101 DELETION SEQADV 9ORE ARG B 112 UNP Q8B9P3 VAL 112 CONFLICT SEQADV 9ORE GLU B 209 UNP Q8B9P3 ASP 209 CONFLICT SEQADV 9ORE ILE B 231 UNP Q8B9P3 VAL 231 CONFLICT SEQADV 9ORE ASN B 368 UNP Q8B9P3 HIS 368 CONFLICT SEQADV 9ORE PRO B 453 UNP Q8B9P3 GLU 453 CONFLICT SEQADV 9ORE ASN B 468 UNP Q8B9P3 EXPRESSION TAG SEQADV 9ORE C UNP Q8B9P3 ALA 90 DELETION SEQADV 9ORE C UNP Q8B9P3 ARG 91 DELETION SEQADV 9ORE C UNP Q8B9P3 GLU 92 DELETION SEQADV 9ORE C UNP Q8B9P3 GLU 93 DELETION SEQADV 9ORE C UNP Q8B9P3 GLN 94 DELETION SEQADV 9ORE C UNP Q8B9P3 ILE 95 DELETION SEQADV 9ORE C UNP Q8B9P3 GLU 96 DELETION SEQADV 9ORE C UNP Q8B9P3 ASN 97 DELETION SEQADV 9ORE C UNP Q8B9P3 PRO 98 DELETION SEQADV 9ORE C UNP Q8B9P3 ARG 99 DELETION SEQADV 9ORE C UNP Q8B9P3 GLN 100 DELETION SEQADV 9ORE ARG C 90 UNP Q8B9P3 SER 101 CONFLICT SEQADV 9ORE ARG C 112 UNP Q8B9P3 VAL 112 CONFLICT SEQADV 9ORE GLU C 209 UNP Q8B9P3 ASP 209 CONFLICT SEQADV 9ORE ILE C 231 UNP Q8B9P3 VAL 231 CONFLICT SEQADV 9ORE ASN C 368 UNP Q8B9P3 HIS 368 CONFLICT SEQADV 9ORE PRO C 453 UNP Q8B9P3 GLU 453 CONFLICT SEQADV 9ORE ASN C 468 UNP Q8B9P3 EXPRESSION TAG SEQRES 1 A 437 LYS GLU SER TYR LEU GLU GLU SER CYS SER THR ILE THR SEQRES 2 A 437 GLU GLY TYR LEU SER VAL LEU ARG THR GLY TRP TYR THR SEQRES 3 A 437 ASN VAL PHE THR LEU GLU VAL GLY ASP VAL GLU ASN LEU SEQRES 4 A 437 THR CYS SER ASP GLY PRO SER LEU ILE LYS THR GLU LEU SEQRES 5 A 437 ASP LEU THR LYS SER ALA LEU ARG GLU LEU LYS THR VAL SEQRES 6 A 437 SER ALA ASP GLN LEU ARG PHE VAL LEU GLY ALA ILE ALA SEQRES 7 A 437 LEU GLY ARG ALA THR ALA ALA ALA VAL THR ALA GLY VAL SEQRES 8 A 437 ALA ILE ALA LYS THR ILE ARG LEU GLU SER GLU VAL THR SEQRES 9 A 437 ALA ILE LYS ASN ALA LEU LYS THR THR ASN GLU ALA VAL SEQRES 10 A 437 SER THR LEU GLY ASN GLY VAL ARG VAL LEU ALA THR ALA SEQRES 11 A 437 VAL ARG GLU LEU LYS ASP PHE VAL SER LYS ASN LEU THR SEQRES 12 A 437 ARG ALA ILE ASN LYS ASN LYS CYS ASP ILE ASP ASP LEU SEQRES 13 A 437 LYS MET ALA VAL SER PHE SER GLN PHE ASN ARG ARG PHE SEQRES 14 A 437 LEU ASN VAL VAL ARG GLN PHE SER GLU ASN ALA GLY ILE SEQRES 15 A 437 THR PRO ALA ILE SER LEU ASP LEU MET THR ASP ALA GLU SEQRES 16 A 437 LEU ALA ARG ALA ILE SER ASN MET PRO THR SER ALA GLY SEQRES 17 A 437 GLN ILE LYS LEU MET LEU GLU ASN ARG ALA MET VAL ARG SEQRES 18 A 437 ARG LYS GLY PHE GLY ILE LEU ILE GLY VAL TYR GLY SER SEQRES 19 A 437 SER VAL ILE TYR MET VAL GLN LEU PRO ILE PHE GLY VAL SEQRES 20 A 437 ILE ASP THR PRO CYS TRP ILE VAL LYS ALA ALA PRO SER SEQRES 21 A 437 CYS SER GLU LYS LYS GLY ASN TYR ALA CYS LEU LEU ARG SEQRES 22 A 437 GLU ASP GLN GLY TRP TYR CYS GLN ASN ALA GLY SER THR SEQRES 23 A 437 VAL TYR TYR PRO ASN GLU LYS ASP CYS GLU THR ARG GLY SEQRES 24 A 437 ASP HIS VAL PHE CYS ASP THR ALA ALA GLY ILE ASN VAL SEQRES 25 A 437 ALA GLU GLN SER LYS GLU CYS ASN ILE ASN ILE SER THR SEQRES 26 A 437 THR ASN TYR PRO CYS LYS VAL SER THR GLY ARG ASN PRO SEQRES 27 A 437 ILE SER MET VAL ALA LEU SER PRO LEU GLY ALA LEU VAL SEQRES 28 A 437 ALA CYS TYR LYS GLY VAL SER CYS SER ILE GLY SER ASN SEQRES 29 A 437 ARG VAL GLY ILE ILE LYS GLN LEU ASN LYS GLY CYS SER SEQRES 30 A 437 TYR ILE THR ASN GLN ASP ALA ASP THR VAL THR ILE ASP SEQRES 31 A 437 ASN THR VAL TYR GLN LEU SER LYS VAL GLU GLY GLU GLN SEQRES 32 A 437 HIS VAL ILE LYS GLY ARG PRO VAL SER SER SER PHE ASP SEQRES 33 A 437 PRO ILE LYS PHE PRO PRO ASP GLN PHE ASN VAL ALA LEU SEQRES 34 A 437 ASP GLN VAL PHE GLU ASN ILE ASN SEQRES 1 B 438 LEU LYS GLU SER TYR LEU GLU GLU SER CYS SER THR ILE SEQRES 2 B 438 THR GLU GLY TYR LEU SER VAL LEU ARG THR GLY TRP TYR SEQRES 3 B 438 THR ASN VAL PHE THR LEU GLU VAL GLY ASP VAL GLU ASN SEQRES 4 B 438 LEU THR CYS SER ASP GLY PRO SER LEU ILE LYS THR GLU SEQRES 5 B 438 LEU ASP LEU THR LYS SER ALA LEU ARG GLU LEU LYS THR SEQRES 6 B 438 VAL SER ALA ASP GLN LEU ARG PHE VAL LEU GLY ALA ILE SEQRES 7 B 438 ALA LEU GLY ARG ALA THR ALA ALA ALA VAL THR ALA GLY SEQRES 8 B 438 VAL ALA ILE ALA LYS THR ILE ARG LEU GLU SER GLU VAL SEQRES 9 B 438 THR ALA ILE LYS ASN ALA LEU LYS THR THR ASN GLU ALA SEQRES 10 B 438 VAL SER THR LEU GLY ASN GLY VAL ARG VAL LEU ALA THR SEQRES 11 B 438 ALA VAL ARG GLU LEU LYS ASP PHE VAL SER LYS ASN LEU SEQRES 12 B 438 THR ARG ALA ILE ASN LYS ASN LYS CYS ASP ILE ASP ASP SEQRES 13 B 438 LEU LYS MET ALA VAL SER PHE SER GLN PHE ASN ARG ARG SEQRES 14 B 438 PHE LEU ASN VAL VAL ARG GLN PHE SER GLU ASN ALA GLY SEQRES 15 B 438 ILE THR PRO ALA ILE SER LEU ASP LEU MET THR ASP ALA SEQRES 16 B 438 GLU LEU ALA ARG ALA ILE SER ASN MET PRO THR SER ALA SEQRES 17 B 438 GLY GLN ILE LYS LEU MET LEU GLU ASN ARG ALA MET VAL SEQRES 18 B 438 ARG ARG LYS GLY PHE GLY ILE LEU ILE GLY VAL TYR GLY SEQRES 19 B 438 SER SER VAL ILE TYR MET VAL GLN LEU PRO ILE PHE GLY SEQRES 20 B 438 VAL ILE ASP THR PRO CYS TRP ILE VAL LYS ALA ALA PRO SEQRES 21 B 438 SER CYS SER GLU LYS LYS GLY ASN TYR ALA CYS LEU LEU SEQRES 22 B 438 ARG GLU ASP GLN GLY TRP TYR CYS GLN ASN ALA GLY SER SEQRES 23 B 438 THR VAL TYR TYR PRO ASN GLU LYS ASP CYS GLU THR ARG SEQRES 24 B 438 GLY ASP HIS VAL PHE CYS ASP THR ALA ALA GLY ILE ASN SEQRES 25 B 438 VAL ALA GLU GLN SER LYS GLU CYS ASN ILE ASN ILE SER SEQRES 26 B 438 THR THR ASN TYR PRO CYS LYS VAL SER THR GLY ARG ASN SEQRES 27 B 438 PRO ILE SER MET VAL ALA LEU SER PRO LEU GLY ALA LEU SEQRES 28 B 438 VAL ALA CYS TYR LYS GLY VAL SER CYS SER ILE GLY SER SEQRES 29 B 438 ASN ARG VAL GLY ILE ILE LYS GLN LEU ASN LYS GLY CYS SEQRES 30 B 438 SER TYR ILE THR ASN GLN ASP ALA ASP THR VAL THR ILE SEQRES 31 B 438 ASP ASN THR VAL TYR GLN LEU SER LYS VAL GLU GLY GLU SEQRES 32 B 438 GLN HIS VAL ILE LYS GLY ARG PRO VAL SER SER SER PHE SEQRES 33 B 438 ASP PRO ILE LYS PHE PRO PRO ASP GLN PHE ASN VAL ALA SEQRES 34 B 438 LEU ASP GLN VAL PHE GLU ASN ILE ASN SEQRES 1 C 439 LEU LYS GLU SER TYR LEU GLU GLU SER CYS SER THR ILE SEQRES 2 C 439 THR GLU GLY TYR LEU SER VAL LEU ARG THR GLY TRP TYR SEQRES 3 C 439 THR ASN VAL PHE THR LEU GLU VAL GLY ASP VAL GLU ASN SEQRES 4 C 439 LEU THR CYS SER ASP GLY PRO SER LEU ILE LYS THR GLU SEQRES 5 C 439 LEU ASP LEU THR LYS SER ALA LEU ARG GLU LEU LYS THR SEQRES 6 C 439 VAL SER ALA ASP GLN LEU ARG ARG PHE VAL LEU GLY ALA SEQRES 7 C 439 ILE ALA LEU GLY ARG ALA THR ALA ALA ALA VAL THR ALA SEQRES 8 C 439 GLY VAL ALA ILE ALA LYS THR ILE ARG LEU GLU SER GLU SEQRES 9 C 439 VAL THR ALA ILE LYS ASN ALA LEU LYS THR THR ASN GLU SEQRES 10 C 439 ALA VAL SER THR LEU GLY ASN GLY VAL ARG VAL LEU ALA SEQRES 11 C 439 THR ALA VAL ARG GLU LEU LYS ASP PHE VAL SER LYS ASN SEQRES 12 C 439 LEU THR ARG ALA ILE ASN LYS ASN LYS CYS ASP ILE ASP SEQRES 13 C 439 ASP LEU LYS MET ALA VAL SER PHE SER GLN PHE ASN ARG SEQRES 14 C 439 ARG PHE LEU ASN VAL VAL ARG GLN PHE SER GLU ASN ALA SEQRES 15 C 439 GLY ILE THR PRO ALA ILE SER LEU ASP LEU MET THR ASP SEQRES 16 C 439 ALA GLU LEU ALA ARG ALA ILE SER ASN MET PRO THR SER SEQRES 17 C 439 ALA GLY GLN ILE LYS LEU MET LEU GLU ASN ARG ALA MET SEQRES 18 C 439 VAL ARG ARG LYS GLY PHE GLY ILE LEU ILE GLY VAL TYR SEQRES 19 C 439 GLY SER SER VAL ILE TYR MET VAL GLN LEU PRO ILE PHE SEQRES 20 C 439 GLY VAL ILE ASP THR PRO CYS TRP ILE VAL LYS ALA ALA SEQRES 21 C 439 PRO SER CYS SER GLU LYS LYS GLY ASN TYR ALA CYS LEU SEQRES 22 C 439 LEU ARG GLU ASP GLN GLY TRP TYR CYS GLN ASN ALA GLY SEQRES 23 C 439 SER THR VAL TYR TYR PRO ASN GLU LYS ASP CYS GLU THR SEQRES 24 C 439 ARG GLY ASP HIS VAL PHE CYS ASP THR ALA ALA GLY ILE SEQRES 25 C 439 ASN VAL ALA GLU GLN SER LYS GLU CYS ASN ILE ASN ILE SEQRES 26 C 439 SER THR THR ASN TYR PRO CYS LYS VAL SER THR GLY ARG SEQRES 27 C 439 ASN PRO ILE SER MET VAL ALA LEU SER PRO LEU GLY ALA SEQRES 28 C 439 LEU VAL ALA CYS TYR LYS GLY VAL SER CYS SER ILE GLY SEQRES 29 C 439 SER ASN ARG VAL GLY ILE ILE LYS GLN LEU ASN LYS GLY SEQRES 30 C 439 CYS SER TYR ILE THR ASN GLN ASP ALA ASP THR VAL THR SEQRES 31 C 439 ILE ASP ASN THR VAL TYR GLN LEU SER LYS VAL GLU GLY SEQRES 32 C 439 GLU GLN HIS VAL ILE LYS GLY ARG PRO VAL SER SER SER SEQRES 33 C 439 PHE ASP PRO ILE LYS PHE PRO PRO ASP GLN PHE ASN VAL SEQRES 34 C 439 ALA LEU ASP GLN VAL PHE GLU ASN ILE ASN SEQRES 1 H 123 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 123 PRO GLY ASP SER LEU LYS ILE SER CYS LYS GLY SER GLY SEQRES 3 H 123 TYR LYS PHE ALA THR TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 H 123 MET PRO GLY LYS GLY LEU GLU TRP MET GLY VAL ILE TYR SEQRES 5 H 123 PRO ASP ASP SER ASP THR ARG TYR SER PRO SER PHE GLN SEQRES 6 H 123 GLY GLN VAL SER ILE SER VAL ASP LYS SER ILE THR THR SEQRES 7 H 123 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 H 123 ALA ILE TYR TYR CYS ALA ARG CYS TYR ASP PHE TRP SER SEQRES 9 H 123 GLY TYR GLN PHE GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 H 123 THR VAL THR VAL SER SER SEQRES 1 L 113 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 L 113 THR PRO GLY GLU THR ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 113 GLN SER LEU ARG HIS ASP ASN GLY TYR ASN TYR LEU ASP SEQRES 4 L 113 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 113 ILE TYR LEU GLY SER LYS ARG ALA SER GLY VAL PRO ASP SEQRES 6 L 113 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 113 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 113 TYR CYS MET GLN THR LEU GLN THR LEU MET PHE THR PHE SEQRES 9 L 113 GLY GLY GLY THR LYS VAL GLU ILE LYS HET NAG D 1 27 HET NAG D 2 27 HET BMA D 3 22 HET NAG E 1 27 HET NAG E 2 28 HET NAG A 501 28 HET NAG B 501 28 HET NAG C 501 28 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 6 NAG 7(C8 H15 N O6) FORMUL 6 BMA C6 H12 O6 HELIX 1 AA1 LEU A 66 LYS A 82 1 17 HELIX 2 AA2 VAL A 104 LEU A 110 1 7 HELIX 3 AA3 GLY A 111 LEU A 130 1 20 HELIX 4 AA4 LEU A 130 LEU A 141 1 12 HELIX 5 AA5 ARG A 163 LYS A 171 1 9 HELIX 6 AA6 LEU A 187 ASN A 197 1 11 HELIX 7 AA7 ASN A 197 ASN A 210 1 14 HELIX 8 AA8 THR A 223 ASN A 233 1 11 HELIX 9 AA9 SER A 237 ASN A 247 1 11 HELIX 10 AB1 ASN A 247 LYS A 254 1 8 HELIX 11 AB2 ASP A 336 GLY A 340 5 5 HELIX 12 AB3 ALA A 344 LYS A 348 5 5 HELIX 13 AB4 PRO A 441 SER A 445 5 5 HELIX 14 AB5 LEU A 460 ILE A 467 1 8 HELIX 15 AB6 ASP B 54 LEU B 58 5 5 HELIX 16 AB7 SER B 65 LYS B 82 1 18 HELIX 17 AB8 VAL B 104 LEU B 110 1 7 HELIX 18 AB9 GLY B 111 ARG B 129 1 19 HELIX 19 AC1 LEU B 130 LEU B 141 1 12 HELIX 20 AC2 ARG B 163 ASN B 172 1 10 HELIX 21 AC3 ASN B 172 ILE B 177 1 6 HELIX 22 AC4 LEU B 187 ASN B 197 1 11 HELIX 23 AC5 ASN B 197 ALA B 211 1 15 HELIX 24 AC6 THR B 223 SER B 232 1 10 HELIX 25 AC7 SER B 237 ASN B 247 1 11 HELIX 26 AC8 ARG B 248 ARG B 253 1 6 HELIX 27 AC9 THR B 337 GLY B 340 5 4 HELIX 28 AD1 ALA B 344 ILE B 352 5 9 HELIX 29 AD2 PRO B 441 SER B 445 5 5 HELIX 30 AD3 LEU B 460 ILE B 467 1 8 HELIX 31 AD4 GLY C 53 LEU C 58 5 6 HELIX 32 AD5 SER C 65 LYS C 82 1 18 HELIX 33 AD6 VAL C 104 ALA C 109 1 6 HELIX 34 AD7 GLY C 111 LEU C 130 1 20 HELIX 35 AD8 LEU C 130 LYS C 142 1 13 HELIX 36 AD9 ARG C 163 ASN C 172 1 10 HELIX 37 AE1 ASN C 172 ILE C 177 1 6 HELIX 38 AE2 LEU C 187 ALA C 211 1 25 HELIX 39 AE3 THR C 223 SER C 232 1 10 HELIX 40 AE4 SER C 237 GLU C 246 1 10 HELIX 41 AE5 ASN C 247 LYS C 254 1 8 HELIX 42 AE6 ASN C 322 LYS C 324 5 3 HELIX 43 AE7 ALA C 338 GLY C 340 5 3 HELIX 44 AE8 GLU C 345 CYS C 350 1 6 HELIX 45 AE9 PRO C 441 PHE C 446 5 6 HELIX 46 AF1 LEU C 460 ILE C 467 1 8 HELIX 47 AF2 LYS H 28 TYR H 32 5 5 HELIX 48 AF3 LYS H 83 THR H 87 5 5 SHEET 1 AA1 7 THR A 328 ARG A 329 0 SHEET 2 AA1 7 HIS A 332 VAL A 333 -1 O HIS A 332 N ARG A 329 SHEET 3 AA1 7 SER A 29 LEU A 39 1 N LEU A 36 O VAL A 333 SHEET 4 AA1 7 VAL A 278 ALA A 288 -1 O ILE A 285 N THR A 32 SHEET 5 AA1 7 GLY A 308 ASN A 313 -1 O TYR A 310 N TRP A 284 SHEET 6 AA1 7 SER A 316 TYR A 320 -1 O TYR A 320 N TRP A 309 SHEET 7 AA1 7 ILE A 341 VAL A 343 -1 O ILE A 341 N TYR A 319 SHEET 1 AA2 5 THR A 328 ARG A 329 0 SHEET 2 AA2 5 HIS A 332 VAL A 333 -1 O HIS A 332 N ARG A 329 SHEET 3 AA2 5 SER A 29 LEU A 39 1 N LEU A 36 O VAL A 333 SHEET 4 AA2 5 GLU A 21 LEU A 24 -1 N SER A 22 O ILE A 31 SHEET 5 AA2 5 GLN A 434 ILE A 437 1 O HIS A 435 N TYR A 23 SHEET 1 AA3 5 GLU A 146 THR A 150 0 SHEET 2 AA3 5 ARG A 156 VAL A 162 -1 O ALA A 159 N ALA A 147 SHEET 3 AA3 5 TYR A 44 GLU A 51 1 N VAL A 47 O LEU A 158 SHEET 4 AA3 5 SER A 266 LEU A 273 -1 O TYR A 269 N PHE A 48 SHEET 5 AA3 5 GLY A 257 TYR A 263 -1 N ILE A 258 O MET A 270 SHEET 1 AA4 4 SER A 291 LYS A 295 0 SHEET 2 AA4 4 ASN A 298 ARG A 304 -1 O ASN A 298 N LYS A 295 SHEET 3 AA4 4 LYS A 362 GLY A 366 -1 O SER A 364 N LEU A 303 SHEET 4 AA4 4 VAL A 458 ALA A 459 -1 O VAL A 458 N VAL A 363 SHEET 1 AA5 3 MET A 372 LEU A 375 0 SHEET 2 AA5 3 GLY A 379 ALA A 383 -1 O ALA A 383 N MET A 372 SHEET 3 AA5 3 SER A 408 THR A 411 -1 O SER A 408 N VAL A 382 SHEET 1 AA6 4 GLY A 398 GLN A 402 0 SHEET 2 AA6 4 CYS A 390 SER A 394 -1 N SER A 394 O GLY A 398 SHEET 3 AA6 4 THR A 417 ILE A 420 -1 O THR A 419 N SER A 391 SHEET 4 AA6 4 THR A 423 GLN A 426 -1 O THR A 423 N ILE A 420 SHEET 1 AA7 7 ILE B 341 VAL B 343 0 SHEET 2 AA7 7 SER B 316 TYR B 320 -1 N THR B 317 O VAL B 343 SHEET 3 AA7 7 GLY B 308 ASN B 313 -1 N CYS B 311 O VAL B 318 SHEET 4 AA7 7 ILE B 285 LYS B 287 -1 N VAL B 286 O GLY B 308 SHEET 5 AA7 7 SER B 29 GLU B 33 -1 N THR B 30 O LYS B 287 SHEET 6 AA7 7 LYS B 20 LEU B 24 -1 N SER B 22 O ILE B 31 SHEET 7 AA7 7 GLU B 433 ILE B 437 1 O HIS B 435 N TYR B 23 SHEET 1 AA8 3 LEU B 36 LEU B 39 0 SHEET 2 AA8 3 HIS B 332 CYS B 335 1 O VAL B 333 N LEU B 36 SHEET 3 AA8 3 CYS B 326 ARG B 329 -1 N GLU B 327 O PHE B 334 SHEET 1 AA9 5 GLU B 146 THR B 150 0 SHEET 2 AA9 5 ARG B 156 VAL B 162 -1 O ALA B 159 N ALA B 147 SHEET 3 AA9 5 TYR B 44 GLU B 51 1 N THR B 49 O VAL B 162 SHEET 4 AA9 5 SER B 266 LEU B 273 -1 O VAL B 267 N LEU B 50 SHEET 5 AA9 5 GLY B 257 TYR B 263 -1 N ILE B 258 O MET B 270 SHEET 1 AB1 3 CYS B 301 ARG B 304 0 SHEET 2 AB1 3 LYS B 362 GLY B 366 -1 O GLY B 366 N CYS B 301 SHEET 3 AB1 3 VAL B 458 ALA B 459 -1 O VAL B 458 N VAL B 363 SHEET 1 AB2 3 MET B 372 SER B 376 0 SHEET 2 AB2 3 GLY B 379 CYS B 384 -1 O GLY B 379 N SER B 376 SHEET 3 AB2 3 GLY B 406 THR B 411 -1 O GLY B 406 N CYS B 384 SHEET 1 AB3 4 GLY B 398 GLN B 402 0 SHEET 2 AB3 4 CYS B 390 SER B 394 -1 N ILE B 392 O ILE B 400 SHEET 3 AB3 4 THR B 417 ILE B 420 -1 O THR B 417 N GLY B 393 SHEET 4 AB3 4 VAL B 424 GLN B 426 -1 O TYR B 425 N VAL B 418 SHEET 1 AB4 3 SER C 29 GLU C 33 0 SHEET 2 AB4 3 LYS C 20 LEU C 24 -1 N SER C 22 O ILE C 31 SHEET 3 AB4 3 GLU C 433 ILE C 437 1 O HIS C 435 N TYR C 23 SHEET 1 AB5 4 VAL C 278 CYS C 283 0 SHEET 2 AB5 4 TYR C 35 ARG C 40 -1 N SER C 37 O THR C 281 SHEET 3 AB5 4 HIS C 332 ASP C 336 1 O VAL C 333 N LEU C 36 SHEET 4 AB5 4 CYS C 326 ARG C 329 -1 N ARG C 329 O HIS C 332 SHEET 1 AB6 5 GLU C 146 THR C 150 0 SHEET 2 AB6 5 ARG C 156 THR C 160 -1 O ALA C 159 N ALA C 147 SHEET 3 AB6 5 TYR C 44 LEU C 50 1 N VAL C 47 O LEU C 158 SHEET 4 AB6 5 SER C 266 LEU C 273 -1 O TYR C 269 N PHE C 48 SHEET 5 AB6 5 PHE C 256 TYR C 263 -1 N PHE C 256 O GLN C 272 SHEET 1 AB7 4 SER C 291 LYS C 295 0 SHEET 2 AB7 4 ASN C 298 ARG C 304 -1 O ASN C 298 N LYS C 295 SHEET 3 AB7 4 LYS C 362 GLY C 366 -1 O SER C 364 N LEU C 303 SHEET 4 AB7 4 VAL C 458 ALA C 459 -1 O VAL C 458 N VAL C 363 SHEET 1 AB8 3 TRP C 309 ASN C 313 0 SHEET 2 AB8 3 SER C 316 TYR C 320 -1 O VAL C 318 N CYS C 311 SHEET 3 AB8 3 ILE C 341 VAL C 343 -1 O VAL C 343 N THR C 317 SHEET 1 AB9 3 VAL C 373 SER C 376 0 SHEET 2 AB9 3 GLY C 379 VAL C 382 -1 O GLY C 379 N SER C 376 SHEET 3 AB9 3 SER C 408 THR C 411 -1 O SER C 408 N VAL C 382 SHEET 1 AC1 4 GLY C 398 GLN C 402 0 SHEET 2 AC1 4 SER C 391 SER C 394 -1 N ILE C 392 O ILE C 400 SHEET 3 AC1 4 THR C 417 THR C 419 -1 O THR C 417 N GLY C 393 SHEET 4 AC1 4 VAL C 424 GLN C 426 -1 O TYR C 425 N VAL C 418 SHEET 1 AC2 4 GLN H 3 GLN H 6 0 SHEET 2 AC2 4 ILE H 20 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AC2 4 THR H 77 LEU H 80 -1 O ALA H 78 N CYS H 22 SHEET 4 AC2 4 ILE H 69 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AC3 3 VAL H 50 ILE H 51 0 SHEET 2 AC3 3 ILE H 34 GLY H 35 -1 N ILE H 34 O ILE H 51 SHEET 3 AC3 3 ALA H 93 ARG H 94 -1 O ALA H 93 N GLY H 35 SHEET 1 AC4 3 ARG H 38 GLN H 39 0 SHEET 2 AC4 3 ALA H 88 TYR H 90 -1 O ILE H 89 N GLN H 39 SHEET 3 AC4 3 THR H 107 VAL H 109 -1 O THR H 107 N TYR H 90 SHEET 1 AC5 2 PRO L 12 VAL L 13 0 SHEET 2 AC5 2 GLU L 105 ILE L 106 1 O GLU L 105 N VAL L 13 SHEET 1 AC6 3 THR L 18 ARG L 24 0 SHEET 2 AC6 3 ASP L 70 SER L 76 -1 O LEU L 73 N ILE L 21 SHEET 3 AC6 3 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74 SHEET 1 AC7 4 PRO L 44 LEU L 46 0 SHEET 2 AC7 4 TRP L 35 GLN L 38 -1 N LEU L 37 O GLN L 45 SHEET 3 AC7 4 VAL L 85 CYS L 88 -1 O TYR L 87 N TYR L 36 SHEET 4 AC7 4 THR L 102 LYS L 103 -1 O THR L 102 N TYR L 86 SSBOND 1 CYS A 28 CYS A 407 1555 1555 2.06 SSBOND 2 CYS A 60 CYS A 182 1555 1555 1.99 SSBOND 3 CYS A 283 CYS A 311 1555 1555 2.19 SSBOND 4 CYS A 292 CYS A 301 1555 1555 2.30 SSBOND 5 CYS A 326 CYS A 335 1555 1555 2.06 SSBOND 6 CYS A 350 CYS A 361 1555 1555 2.01 SSBOND 7 CYS A 384 CYS A 390 1555 1555 2.23 SSBOND 8 CYS B 28 CYS B 407 1555 1555 2.19 SSBOND 9 CYS B 60 CYS B 182 1555 1555 2.25 SSBOND 10 CYS B 283 CYS B 311 1555 1555 2.24 SSBOND 11 CYS B 292 CYS B 301 1555 1555 1.87 SSBOND 12 CYS B 326 CYS B 335 1555 1555 2.07 SSBOND 13 CYS B 350 CYS B 361 1555 1555 2.04 SSBOND 14 CYS B 384 CYS B 390 1555 1555 2.30 SSBOND 15 CYS C 28 CYS C 407 1555 1555 2.07 SSBOND 16 CYS C 60 CYS C 182 1555 1555 2.20 SSBOND 17 CYS C 283 CYS C 311 1555 1555 2.26 SSBOND 18 CYS C 292 CYS C 301 1555 1555 2.23 SSBOND 19 CYS C 326 CYS C 335 1555 1555 2.01 SSBOND 20 CYS C 350 CYS C 361 1555 1555 2.28 SSBOND 21 CYS C 384 CYS C 390 1555 1555 2.02 SSBOND 22 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 23 CYS L 23 CYS L 88 1555 1555 2.04 LINK ND2 ASN A 57 C1 NAG A 501 1555 1555 1.42 LINK ND2 ASN A 172 C1 NAG D 1 1555 1555 1.45 LINK ND2 ASN B 57 C1 NAG B 501 1555 1555 1.47 LINK ND2 ASN B 172 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN C 172 C1 NAG C 501 1555 1555 1.47 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.48 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.46 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -1.93 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000