HEADER IMMUNE SYSTEM 20-DEC-24 9MMJ TITLE CRYSTAL STRUCTURE OF 19B FAB BOUND TO THE THIRD VARIABLE (V3) LOOP TITLE 2 PEPTIDE FROM THE HIV-1 JR-FL ENVELOPE (ENV) GLYCOPROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: 19B FAB LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 19B FAB HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SURFACE PROTEIN GP120 JR-FL V3 PEPTIDE; 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: 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 IMMUNODEFICIENCY VIRUS 1; SOURCE 14 ORGANISM_TAXID: 11676 KEYWDS 19B, FAB, FRAGMENT ANTIGEN-BINDING, HIV-1 ENVELOPE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.FETICS,P.ACHARYA REVDAT 1 21-JAN-26 9MMJ 0 JRNL AUTH S.FETICS,P.ACHARYA JRNL TITL CRYSTAL STRUCTURE OF 19B FAB BOUND TO HIV-1 ENV JR-FL JRNL TITL 2 PEPTIDE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.78 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.1_5286 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) : 1.78 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.61 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 51826 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.161 REMARK 3 R VALUE (WORKING SET) : 0.159 REMARK 3 FREE R VALUE : 0.199 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090 REMARK 3 FREE R VALUE TEST SET COUNT : 2636 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 34.6100 - 4.7400 0.99 2791 149 0.1885 0.2161 REMARK 3 2 4.7400 - 3.7600 1.00 2669 141 0.1405 0.1618 REMARK 3 3 3.7600 - 3.2900 1.00 2627 144 0.1440 0.1757 REMARK 3 4 3.2900 - 2.9900 1.00 2650 131 0.1526 0.1938 REMARK 3 5 2.9900 - 2.7700 1.00 2644 114 0.1587 0.2165 REMARK 3 6 2.7700 - 2.6100 1.00 2605 131 0.1624 0.2087 REMARK 3 7 2.6100 - 2.4800 1.00 2589 136 0.1647 0.2147 REMARK 3 8 2.4800 - 2.3700 1.00 2575 157 0.1624 0.2223 REMARK 3 9 2.3700 - 2.2800 1.00 2583 132 0.1565 0.1969 REMARK 3 10 2.2800 - 2.2000 1.00 2554 143 0.1543 0.2053 REMARK 3 11 2.2000 - 2.1300 1.00 2601 139 0.1445 0.1846 REMARK 3 12 2.1300 - 2.0700 1.00 2562 143 0.1610 0.1986 REMARK 3 13 2.0700 - 2.0200 1.00 2558 128 0.1643 0.1943 REMARK 3 14 2.0200 - 1.9700 1.00 2558 145 0.1545 0.1969 REMARK 3 15 1.9700 - 1.9200 1.00 2553 146 0.1531 0.1973 REMARK 3 16 1.9200 - 1.8800 1.00 2572 142 0.1587 0.2417 REMARK 3 17 1.8800 - 1.8400 1.00 2529 127 0.1741 0.2322 REMARK 3 18 1.8400 - 1.8100 0.99 2537 139 0.1814 0.2810 REMARK 3 19 1.8100 - 1.7800 0.96 2433 149 0.1923 0.2044 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) : 0.163 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.108 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.82 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.95 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 3452 REMARK 3 ANGLE : 1.139 4724 REMARK 3 CHIRALITY : 0.082 540 REMARK 3 PLANARITY : 0.009 610 REMARK 3 DIHEDRAL : 14.360 1199 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 9MMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291156. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JUN-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 : NSLS-II 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) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51826 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780 REMARK 200 RESOLUTION RANGE LOW (A) : 34.610 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 26.9300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 5.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.800 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 (%): 56.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.18 M AMMONIUM SULFATE, 0.09 M SODIUM REMARK 280 ACETATE TRIHYDRATE PH 4.6, 27% W/V POLYETHYLENE GLYCOL REMARK 280 MONOMETHYL ETHER 2,000, 10% V/V GLYCEROL, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 295K 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 22.95100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.98650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.75350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.98650 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.95100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.75350 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: 5880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 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 SER B 127 REMARK 465 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 LYS B 214 REMARK 465 SER B 215 REMARK 465 GLU D 295 REMARK 465 ILE D 296 REMARK 465 ASN D 297 REMARK 465 CYS D 298 REMARK 465 THR D 299 REMARK 465 ARG D 300 REMARK 465 PRO D 301 REMARK 465 GLY D 321 REMARK 465 GLU D 322 REMARK 465 ILE D 323 REMARK 465 ILE D 324 REMARK 465 GLY D 325 REMARK 465 ASP D 326 REMARK 465 ILE D 327 REMARK 465 ARG D 328 REMARK 465 GLN D 329 REMARK 465 ALA D 330 REMARK 465 HIS D 331 REMARK 465 CYS D 332 REMARK 465 ASN D 333 REMARK 465 ILE D 334 REMARK 465 SER D 335 REMARK 465 ARG D 336 REMARK 465 ALA D 337 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 145 CG CD CE NZ REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 LYS A 188 CG CD CE NZ REMARK 470 GLU A 213 CG CD OE1 OE2 REMARK 470 GLU B 1 CG CD OE1 OE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 SER B 186 OG REMARK 470 LYS B 206 CG CD CE NZ REMARK 470 GLU B 212 CG CD OE1 OE2 REMARK 470 LYS D 307 CG CD CE NZ 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 A 507 O HOH A 630 1.96 REMARK 500 O HOH A 476 O HOH A 593 1.98 REMARK 500 O HOH A 599 O HOH A 638 2.01 REMARK 500 O HOH B 304 O HOH B 346 2.03 REMARK 500 O HOH A 512 O HOH B 434 2.04 REMARK 500 O HOH B 409 O HOH B 415 2.04 REMARK 500 O HOH A 585 O HOH A 653 2.04 REMARK 500 O HOH A 563 O HOH B 325 2.05 REMARK 500 O HOH A 555 O HOH A 580 2.06 REMARK 500 O HOH A 464 O HOH A 647 2.07 REMARK 500 O HOH B 343 O HOH B 482 2.07 REMARK 500 O HOH B 493 O HOH B 494 2.10 REMARK 500 O HOH B 460 O HOH B 472 2.11 REMARK 500 O HOH A 609 O HOH A 624 2.11 REMARK 500 O HOH B 357 O HOH B 374 2.12 REMARK 500 O HOH A 597 O HOH A 610 2.12 REMARK 500 N GLY B 134 O HOH B 301 2.12 REMARK 500 O HOH A 560 O HOH A 601 2.13 REMARK 500 O HOH B 451 O HOH B 492 2.13 REMARK 500 O HOH A 579 O HOH A 598 2.13 REMARK 500 O HOH A 428 O HOH B 403 2.14 REMARK 500 O HOH B 418 O HOH B 478 2.14 REMARK 500 O HOH B 424 O HOH B 459 2.14 REMARK 500 O HOH A 570 O HOH B 485 2.14 REMARK 500 O HOH B 351 O HOH B 377 2.15 REMARK 500 O HOH B 457 O HOH B 462 2.15 REMARK 500 O HOH B 354 O HOH B 476 2.16 REMARK 500 O HOH A 440 O HOH A 499 2.16 REMARK 500 O HOH B 471 O HOH B 492 2.16 REMARK 500 O HOH A 613 O HOH A 642 2.16 REMARK 500 O HOH B 431 O HOH B 444 2.17 REMARK 500 O HOH B 477 O HOH B 494 2.17 REMARK 500 O HOH A 590 O HOH A 648 2.17 REMARK 500 O HOH B 476 O HOH B 504 2.18 REMARK 500 O HOH B 393 O HOH B 470 2.18 REMARK 500 O HOH A 486 O HOH A 558 2.18 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 CYS B 196 CB CYS B 196 SG -0.104 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 CYS B 140 CA - CB - SG ANGL. DEV. = 8.4 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 SER A 30 -129.82 54.87 REMARK 500 SER A 67 138.60 -173.53 REMARK 500 ALA A 84 174.43 178.40 REMARK 500 LYS B 43 4.58 178.32 REMARK 500 VAL B 96 38.21 -80.46 REMARK 500 THR B 160 -34.09 -130.05 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 A 662 DISTANCE = 5.88 ANGSTROMS REMARK 525 HOH A 663 DISTANCE = 6.20 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 307 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 112 O REMARK 620 2 ASN A 137 O 92.9 REMARK 620 3 ASN A 138 O 81.0 66.4 REMARK 620 4 HOH A 459 O 53.6 145.9 98.3 REMARK 620 5 HOH A 592 O 164.4 83.7 111.3 130.2 REMARK 620 N 1 2 3 4 DBREF 9MMJ A 1 213 PDB 9MMJ 9MMJ 1 213 DBREF 9MMJ B 1 215 PDB 9MMJ 9MMJ 1 215 DBREF 9MMJ D 295 337 UNP P20871 ENV_HV1JR 291 333 SEQADV 9MMJ GLU D 295 UNP P20871 LYS 291 CONFLICT SEQADV 9MMJ ASN D 302 UNP P20871 SER 298 CONFLICT SEQADV 9MMJ TRP D 316 UNP P20871 ALA 312 CONFLICT SEQRES 1 A 213 ASP ILE VAL LEU THR GLN SER PRO PRO SER LEU SER ALA SEQRES 2 A 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 A 213 GLN ASP ILE SER ASP HIS LEU SER TRP PHE GLN GLN LYS SEQRES 4 A 213 PRO GLY LYS ALA PRO LYS LEU LEU VAL TYR GLY VAL SER SEQRES 5 A 213 SER LEU GLU ALA GLY VAL PRO SER ARG PHE SER VAL SER SEQRES 6 A 213 GLY SER GLY THR HIS PHE THR PHE THR VAL ASN GLY LEU SEQRES 7 A 213 GLN PRO GLU ASP LEU ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 A 213 ASP ASP LEU PRO TRP THR PHE GLY PRO GLY THR VAL VAL SEQRES 9 A 213 GLU VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 213 PHE ASN ARG GLY GLU SEQRES 1 B 216 GLU VAL GLN LEU VAL GLN SER GLY GLY ALA LEU ILE GLN SEQRES 2 B 216 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 216 PHE THR PHE VAL ASP TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 B 216 ALA PRO GLY LYS GLY LEU GLN TRP VAL SER THR ILE ILE SEQRES 5 B 216 GLY SER GLY ALA ASP THR TYR TYR THR ASP SER VAL LYS SEQRES 6 B 216 GLY ARG PHE THR ILE SER ARG ASP ASN SER ASN ASN THR SEQRES 7 B 216 VAL HIS LEU GLN MET ASN SER LEU ARG ALA ASP ASP THR SEQRES 8 B 216 ALA LEU TYR TYR CYS VAL ARG GLY VAL PHE ASP LEU TRP SEQRES 9 B 216 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 10 B 216 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 B 216 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 B 216 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 B 216 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 B 216 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 B 216 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 B 216 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 B 216 ASP LYS ARG VAL GLU PRO LYS SER SEQRES 1 D 43 GLU ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 2 D 43 SER ILE HIS ILE GLY PRO GLY ARG TRP PHE TYR THR THR SEQRES 3 D 43 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 4 D 43 ILE SER ARG ALA HET ACT A 301 4 HET GOL A 302 6 HET GOL A 303 6 HET SO4 A 304 5 HET SO4 A 305 5 HET NA A 306 1 HET NA A 307 1 HET NA A 308 1 HETNAM ACT ACETATE ION HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETNAM NA SODIUM ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 ACT C2 H3 O2 1- FORMUL 5 GOL 2(C3 H8 O3) FORMUL 7 SO4 2(O4 S 2-) FORMUL 9 NA 3(NA 1+) FORMUL 12 HOH *478(H2 O) HELIX 1 AA1 GLN A 79 LEU A 83 5 5 HELIX 2 AA2 SER A 121 LYS A 126 1 6 HELIX 3 AA3 LYS A 183 HIS A 189 1 7 HELIX 4 AA4 THR B 28 TYR B 32 5 5 HELIX 5 AA5 ASP B 61 LYS B 64 5 4 HELIX 6 AA6 ARG B 83 THR B 87 5 5 HELIX 7 AA7 SER B 156 ALA B 158 5 3 HELIX 8 AA8 SER B 187 LEU B 189 5 3 HELIX 9 AA9 LYS B 201 ASN B 204 5 4 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 ARG A 18 ALA A 25 -1 O GLN A 24 N THR A 5 SHEET 3 AA1 4 HIS A 70 ASN A 76 -1 O VAL A 75 N VAL A 19 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 65 O THR A 72 SHEET 1 AA2 5 SER A 10 ALA A 13 0 SHEET 2 AA2 5 THR A 102 VAL A 106 1 O VAL A 103 N LEU A 11 SHEET 3 AA2 5 ALA A 84 GLN A 90 -1 N ALA A 84 O VAL A 104 SHEET 4 AA2 5 LEU A 33 GLN A 38 -1 N GLN A 38 O THR A 85 SHEET 5 AA2 5 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 1 AA3 4 SER A 10 ALA A 13 0 SHEET 2 AA3 4 THR A 102 VAL A 106 1 O VAL A 103 N LEU A 11 SHEET 3 AA3 4 ALA A 84 GLN A 90 -1 N ALA A 84 O VAL A 104 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 SER A 114 PHE A 118 0 SHEET 2 AA4 4 THR A 129 PHE A 139 -1 O ASN A 137 N SER A 114 SHEET 3 AA4 4 TYR A 173 SER A 182 -1 O LEU A 179 N VAL A 132 SHEET 4 AA4 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AA5 4 ALA A 153 LEU A 154 0 SHEET 2 AA5 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AA5 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 AA5 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 AA6 4 GLN B 3 GLN B 6 0 SHEET 2 AA6 4 LEU B 18 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA6 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA6 4 PHE B 67 ASP B 72 -1 N THR B 68 O GLN B 81 SHEET 1 AA7 6 ALA B 10 ILE B 12 0 SHEET 2 AA7 6 THR B 107 VAL B 111 1 O THR B 110 N ILE B 12 SHEET 3 AA7 6 ALA B 88 ARG B 94 -1 N TYR B 90 O THR B 107 SHEET 4 AA7 6 MET B 34 ALA B 40 -1 N VAL B 37 O TYR B 91 SHEET 5 AA7 6 GLY B 44 ILE B 51 -1 O GLN B 46 N ARG B 38 SHEET 6 AA7 6 THR B 57 TYR B 59 -1 O TYR B 58 N THR B 50 SHEET 1 AA8 4 SER B 120 LEU B 124 0 SHEET 2 AA8 4 THR B 135 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AA8 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AA8 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AA9 4 SER B 120 LEU B 124 0 SHEET 2 AA9 4 THR B 135 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AA9 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AA9 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AB1 3 THR B 151 TRP B 154 0 SHEET 2 AB1 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AB1 3 THR B 205 ARG B 210 -1 O VAL B 207 N VAL B 198 SHEET 1 AB2 2 LYS D 307 GLY D 312 0 SHEET 2 AB2 2 ARG D 315 THR D 319 -1 O THR D 319 N LYS D 307 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.19 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.13 SSBOND 3 CYS B 22 CYS B 92 1555 1555 2.13 SSBOND 4 CYS B 140 CYS B 196 1555 1555 2.08 LINK O ALA A 112 NA NA A 307 1555 1555 2.93 LINK O ASN A 137 NA NA A 307 1555 1555 3.07 LINK O ASN A 138 NA NA A 307 1555 1555 2.85 LINK NA NA A 306 O HOH A 645 1555 1555 3.18 LINK NA NA A 307 O HOH A 459 1555 1555 3.12 LINK NA NA A 307 O HOH A 592 1555 1555 2.73 CISPEP 1 SER A 7 PRO A 8 0 -7.24 CISPEP 2 LEU A 94 PRO A 95 0 -1.92 CISPEP 3 TYR A 140 PRO A 141 0 4.02 CISPEP 4 PHE B 146 PRO B 147 0 -4.22 CISPEP 5 GLU B 148 PRO B 149 0 -0.88 CRYST1 45.902 87.507 131.973 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 0.021786 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011428 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007577 0.00000