HEADER IMMUNE SYSTEM/VIRAL PROTEIN 10-NOV-21 7SSC TITLE TRL345 LINEAGE ANCESTOR I8 FAB BOUND TO AN HCMV GB-DERIVED PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRL345-I8 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TRL345-I8 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN B PEPTIDE; COMPND 11 CHAIN: P; COMPND 12 FRAGMENT: ANTIGENIC DOMAIN-2 (UNP RESIDUES 65-79); COMPND 13 SYNONYM: GB, GB-P17; COMPND 14 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; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN BETAHERPESVIRUS 5; SOURCE 14 ORGANISM_COMMON: HHV-5; SOURCE 15 ORGANISM_TAXID: 10359 KEYWDS IMMUNOGLOBULIN, FUSION PROTEIN, HCMV, IMMUNE SYSTEM-VIRAL PROTEIN KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.R.SPONHOLTZ,J.S.MCLELLAN REVDAT 1 19-OCT-22 7SSC 0 JRNL AUTH J.A.JENKS,S.AMIN,A.KUMAR,M.R.SPONHOLTZ,D.WRAPP, JRNL AUTH 2 S.VENKATAYOGI,J.TU,J.S.MCLELLAN,K.WIEHE,S.R.PERMAR JRNL TITL SINGLE, IMPROBABLE B CELL RECEPTOR MUTATION CONFERS POTENT JRNL TITL 2 NEUTRALIZATION AGAINST CYTOMEGALOVIRUS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.39 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 3 NUMBER OF REFLECTIONS : 48141 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.152 REMARK 3 R VALUE (WORKING SET) : 0.150 REMARK 3 FREE R VALUE : 0.174 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 2377 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 56.3900 - 4.6300 0.98 2887 158 0.1635 0.1844 REMARK 3 2 4.6300 - 3.6700 0.95 2696 153 0.1338 0.1416 REMARK 3 3 3.6700 - 3.2100 0.99 2775 143 0.1376 0.1392 REMARK 3 4 3.2100 - 2.9200 0.94 2612 135 0.1542 0.1722 REMARK 3 5 2.9200 - 2.7100 0.99 2750 147 0.1599 0.2021 REMARK 3 6 2.7100 - 2.5500 0.98 2732 114 0.1584 0.1873 REMARK 3 7 2.5500 - 2.4200 0.99 2761 120 0.1595 0.1986 REMARK 3 8 2.4200 - 2.3100 0.95 2605 133 0.1537 0.1870 REMARK 3 9 2.3100 - 2.2300 0.98 2658 154 0.1438 0.1727 REMARK 3 10 2.2300 - 2.1500 0.99 2709 139 0.1419 0.1556 REMARK 3 11 2.1500 - 2.0800 0.99 2694 146 0.1460 0.1700 REMARK 3 12 2.0800 - 2.0200 0.98 2668 135 0.1448 0.1885 REMARK 3 13 2.0200 - 1.9700 0.98 2686 128 0.1450 0.2008 REMARK 3 14 1.9700 - 1.9200 0.94 2607 109 0.1493 0.1956 REMARK 3 15 1.9200 - 1.8800 0.97 2640 150 0.1550 0.1841 REMARK 3 16 1.8800 - 1.8400 0.98 2650 156 0.1629 0.2010 REMARK 3 17 1.8400 - 1.8000 0.98 2634 157 0.1791 0.2070 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) : 0.160 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.410 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 13.44 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.20 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN H REMARK 3 ORIGIN FOR THE GROUP (A): -16.6242 -32.4210 1.7042 REMARK 3 T TENSOR REMARK 3 T11: 0.0423 T22: 0.0851 REMARK 3 T33: 0.0503 T12: 0.0129 REMARK 3 T13: -0.0075 T23: 0.0040 REMARK 3 L TENSOR REMARK 3 L11: 0.8637 L22: 1.4405 REMARK 3 L33: 0.2374 L12: 0.8036 REMARK 3 L13: 0.0884 L23: -0.0274 REMARK 3 S TENSOR REMARK 3 S11: -0.0041 S12: -0.0212 S13: 0.0021 REMARK 3 S21: -0.0370 S22: 0.0155 S23: 0.0659 REMARK 3 S31: 0.0150 S32: -0.0139 S33: -0.0115 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN L REMARK 3 ORIGIN FOR THE GROUP (A): -8.8502 -42.8604 14.4655 REMARK 3 T TENSOR REMARK 3 T11: 0.0749 T22: 0.0977 REMARK 3 T33: 0.0424 T12: 0.0067 REMARK 3 T13: -0.0213 T23: 0.0087 REMARK 3 L TENSOR REMARK 3 L11: 0.4289 L22: 1.5161 REMARK 3 L33: 0.0250 L12: 0.5340 REMARK 3 L13: -0.0247 L23: 0.1012 REMARK 3 S TENSOR REMARK 3 S11: 0.0477 S12: -0.0323 S13: -0.0147 REMARK 3 S21: 0.0469 S22: -0.0622 S23: 0.0091 REMARK 3 S31: 0.0246 S32: 0.0227 S33: 0.0219 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN P REMARK 3 ORIGIN FOR THE GROUP (A): 1.8257 -8.7622 10.7589 REMARK 3 T TENSOR REMARK 3 T11: 0.0620 T22: 0.0511 REMARK 3 T33: 0.0802 T12: -0.0021 REMARK 3 T13: -0.0148 T23: -0.0247 REMARK 3 L TENSOR REMARK 3 L11: 5.3071 L22: 4.8032 REMARK 3 L33: 7.7759 L12: 0.7174 REMARK 3 L13: -1.7606 L23: -0.5273 REMARK 3 S TENSOR REMARK 3 S11: 0.0033 S12: -0.2078 S13: 0.3430 REMARK 3 S21: 0.2674 S22: 0.0423 S23: 0.1272 REMARK 3 S31: -0.2998 S32: -0.1666 S33: -0.0655 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 7SSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-21. REMARK 100 THE DEPOSITION ID IS D_1000260969. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-JUN-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID 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 : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48200 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 66.880 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : 0.06400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.00 REMARK 200 R MERGE FOR SHELL (I) : 0.13900 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 2.8.3 REMARK 200 STARTING MODEL: 6UOE, 6ZFO REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE, REMARK 280 25% (W/V) PEG 3350, 0.1 M BIS-TRIS PH 5.5, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 298K 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 33.43950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.44000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.33450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.44000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.43950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.33450 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: 5080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 HIS P 65 REMARK 465 ARG P 66 REMARK 465 ALA P 67 REMARK 465 ASN P 68 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 569 O HOH H 599 1.80 REMARK 500 O HOH L 678 O HOH L 737 1.81 REMARK 500 O HOH H 520 O HOH H 601 1.85 REMARK 500 O HOH H 466 O HOH H 548 1.87 REMARK 500 O HOH L 603 O HOH L 711 1.91 REMARK 500 O HOH L 660 O HOH L 692 1.92 REMARK 500 O HOH H 453 O HOH H 547 1.96 REMARK 500 O HOH L 541 O HOH L 666 1.97 REMARK 500 O HOH L 685 O HOH L 743 1.98 REMARK 500 O HOH H 548 O HOH H 557 1.98 REMARK 500 O HOH H 481 O HOH H 588 1.99 REMARK 500 O HOH H 457 O HOH H 620 2.00 REMARK 500 O HOH H 545 O HOH H 623 2.05 REMARK 500 O HOH L 602 O HOH L 655 2.06 REMARK 500 O HOH L 624 O HOH L 637 2.06 REMARK 500 O HOH L 409 O HOH L 477 2.06 REMARK 500 O HOH H 595 O HOH L 540 2.07 REMARK 500 O HOH L 546 O HOH L 658 2.10 REMARK 500 O HOH L 563 O HOH L 624 2.11 REMARK 500 O HOH L 717 O HOH L 734 2.12 REMARK 500 O HOH H 529 O HOH H 582 2.14 REMARK 500 OE1 GLN H 105 O HOH H 301 2.16 REMARK 500 O HOH H 583 O HOH H 614 2.16 REMARK 500 O GLY L 128 O HOH L 401 2.17 REMARK 500 OE2 GLU L 187 O HOH L 402 2.17 REMARK 500 O HOH H 397 O HOH H 544 2.18 REMARK 500 O HOH H 645 O HOH H 649 2.18 REMARK 500 O HOH H 496 O HOH H 551 2.19 REMARK 500 OE1 GLN L 42 O HOH L 403 2.19 REMARK 500 O HOH H 646 O HOH H 648 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 H 556 O HOH L 639 4435 2.11 REMARK 500 O HOH H 605 O HOH L 710 2444 2.11 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 ASP H 101 118.97 -165.87 REMARK 500 ALA L 51 -38.34 74.31 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 648 DISTANCE = 6.26 ANGSTROMS REMARK 525 HOH H 649 DISTANCE = 6.29 ANGSTROMS REMARK 525 HOH L 752 DISTANCE = 6.17 ANGSTROMS DBREF 7SSC H 1 213 PDB 7SSC 7SSC 1 213 DBREF 7SSC L 1 213 PDB 7SSC 7SSC 1 213 DBREF 7SSC P 65 79 UNP P06473 GB_HCMVA 65 79 SEQRES 1 H 223 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 223 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 223 PHE THR PHE SER SER TYR ASN MET HIS TRP VAL ARG GLN SEQRES 4 H 223 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5 H 223 ASN ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 223 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 223 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 223 ALA VAL TYR TYR CYS ALA ARG ASP GLY ARG SER VAL GLY SEQRES 9 H 223 GLY PHE SER GLY ILE LEU ASP PRO TRP GLY GLN GLY THR SEQRES 10 H 223 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 223 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 223 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 223 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 223 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 223 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 223 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 223 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 223 GLU PRO SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL GLY SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 214 ASP ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 L 214 SER ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 L 214 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 214 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 214 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 214 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 214 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 214 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 214 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 214 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 214 SER PHE ASN ARG GLY GLU SEQRES 1 P 15 HIS ARG ALA ASN GLU THR ILE TYR ASN THR THR LEU LYS SEQRES 2 P 15 TYR GLY HET GOL L 301 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL C3 H8 O3 FORMUL 5 HOH *723(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 ASP H 61 LYS H 64 5 4 HELIX 3 AA3 ASN H 73 LYS H 75 5 3 HELIX 4 AA4 ARG H 83 THR H 87 5 5 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 LEU H 189 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 GLU L 79 PHE L 83 5 5 HELIX 9 AA9 SER L 121 GLY L 128 1 8 HELIX 10 AB1 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 6 VAL H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 LYS H 57 TYR H 59 -1 O TYR H 58 N VAL H 50 SHEET 1 AA3 4 VAL H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 LEU H 100F TRP H 103 -1 O ASP H 101 N ARG H 94 SHEET 1 AA4 2 GLY H 100A PHE H 100B 0 SHEET 2 AA4 2 LEU P 76 LYS P 77 -1 O LEU P 76 N PHE H 100B SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA6 4 SER H 120 LEU H 124 0 SHEET 2 AA6 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA6 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA6 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA7 3 THR H 151 TRP H 154 0 SHEET 2 AA7 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA7 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA8 4 LEU L 4 SER L 7 0 SHEET 2 AA8 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA8 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA8 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA9 6 THR L 10 LEU L 13 0 SHEET 2 AA9 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA9 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA9 6 ASP L 53 ARG L 54 -1 O ASP L 53 N TYR L 49 SHEET 1 AB1 4 THR L 10 LEU L 13 0 SHEET 2 AB1 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB1 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB1 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB2 4 SER L 114 PHE L 118 0 SHEET 2 AB2 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB2 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB2 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB3 4 ALA L 153 LEU L 154 0 SHEET 2 AB3 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB3 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB3 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.09 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.02 CISPEP 1 ASP H 101 PRO H 102 0 -4.18 CISPEP 2 PHE H 146 PRO H 147 0 -5.82 CISPEP 3 GLU H 148 PRO H 149 0 1.65 CISPEP 4 SER L 7 PRO L 8 0 -13.29 CISPEP 5 TRP L 94 PRO L 95 0 1.30 CISPEP 6 PRO L 95 PRO L 95A 0 -3.61 CISPEP 7 TYR L 140 PRO L 141 0 -2.01 CRYST1 66.879 74.669 104.880 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 0.014952 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013392 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009535 0.00000