HEADER IMMUNE SYSTEM 15-DEC-23 8VDL TITLE HB3VAR03 CIDRA1.4 DOMAIN WITH C7 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HB3VAR03 CIDRA1.4 DOMAIN; COMPND 3 CHAIN: C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: C7 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: C7 LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM HB3; SOURCE 3 ORGANISM_TAXID: 137071; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK 293E; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: HEK 293E KEYWDS MALARIA, PLASMODIUM FALCIPARUM, PFEMP1, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR N.K.HURLBURT,M.PANCERA REVDAT 1 09-OCT-24 8VDL 0 JRNL AUTH N.K.HURLBURT,M.PANCERA JRNL TITL BROADLY INHIBITORY ANTIBODIES AGAINST SEVERE JRNL TITL 2 MALARIA-ASSOCIATED PFEMP1 FUNCTION THROUGH A STRUCTURALLY JRNL TITL 3 CONVERGENT MODE OF BINDING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.68 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) : 2.68 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.30 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 26372 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.219 REMARK 3 R VALUE (WORKING SET) : 0.217 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 1350 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 46.3000 - 5.7800 1.00 2698 145 0.2359 0.2598 REMARK 3 2 5.7800 - 4.5900 1.00 2567 128 0.1801 0.2013 REMARK 3 3 4.5900 - 4.0100 1.00 2520 134 0.1742 0.2374 REMARK 3 4 4.0100 - 3.6400 1.00 2499 140 0.2063 0.2459 REMARK 3 5 3.6400 - 3.3800 1.00 2501 127 0.2112 0.2734 REMARK 3 6 3.3800 - 3.1800 1.00 2472 133 0.2124 0.2783 REMARK 3 7 3.1800 - 3.0200 1.00 2478 146 0.2251 0.2521 REMARK 3 8 3.0200 - 2.8900 1.00 2459 138 0.2418 0.3267 REMARK 3 9 2.8900 - 2.7800 1.00 2454 127 0.2650 0.3292 REMARK 3 10 2.7800 - 2.6800 0.97 2374 132 0.2941 0.3823 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) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.160 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 : 0.008 NULL REMARK 3 ANGLE : 1.061 NULL REMARK 3 CHIRALITY : 0.057 604 REMARK 3 PLANARITY : 0.018 692 REMARK 3 DIHEDRAL : 18.000 1433 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 8VDL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1000279941. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-OCT-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97387 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS, AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26449 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.680 REMARK 200 RESOLUTION RANGE LOW (A) : 50.070 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 9.500 REMARK 200 R MERGE (I) : 0.14300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 9.30 REMARK 200 R MERGE FOR SHELL (I) : 1.53100 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 (%): 63.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PH 6.0, 0.2M ZN ACETATE, 10% REMARK 280 PEG 8K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 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,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.67650 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 125.17050 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.67650 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 125.17050 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: 5360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS C 567 REMARK 465 ILE C 568 REMARK 465 THR C 569 REMARK 465 SER C 570 REMARK 465 PHE C 571 REMARK 465 ASP C 572 REMARK 465 GLU C 573 REMARK 465 PHE C 574 REMARK 465 THR C 591 REMARK 465 GLU C 592 REMARK 465 LEU C 593 REMARK 465 THR C 594 REMARK 465 TYR C 595 REMARK 465 CYS C 596 REMARK 465 ILE C 597 REMARK 465 ASN C 598 REMARK 465 ASN C 599 REMARK 465 THR C 600 REMARK 465 ASP C 601 REMARK 465 VAL C 602 REMARK 465 THR C 603 REMARK 465 ASP C 604 REMARK 465 CYS C 605 REMARK 465 ASN C 606 REMARK 465 LYS C 607 REMARK 465 CYS C 608 REMARK 465 ASN C 609 REMARK 465 LYS C 610 REMARK 465 ASN C 611 REMARK 465 CYS C 612 REMARK 465 VAL C 613 REMARK 465 ASN C 628 REMARK 465 ILE C 629 REMARK 465 MET C 630 REMARK 465 LYS C 631 REMARK 465 LEU C 632 REMARK 465 PHE C 633 REMARK 465 THR C 634 REMARK 465 ASN C 635 REMARK 465 LYS C 636 REMARK 465 HIS C 637 REMARK 465 ASP C 638 REMARK 465 ILE C 639 REMARK 465 PRO C 640 REMARK 465 LYS C 641 REMARK 465 LYS C 642 REMARK 465 TYR C 643 REMARK 465 TYR C 644 REMARK 465 LEU C 645 REMARK 465 ASN C 646 REMARK 465 ILE C 647 REMARK 465 ALA C 681 REMARK 465 SER C 682 REMARK 465 SER C 683 REMARK 465 LYS C 684 REMARK 465 ALA C 685 REMARK 465 ASN C 686 REMARK 465 ASN C 687 REMARK 465 GLY C 688 REMARK 465 THR C 689 REMARK 465 LYS C 690 REMARK 465 ASP C 691 REMARK 465 SER C 692 REMARK 465 GLU C 693 REMARK 465 ALA C 694 REMARK 465 ALA C 695 REMARK 465 ILE C 696 REMARK 465 CYS C 710 REMARK 465 LYS C 711 REMARK 465 ASP C 712 REMARK 465 ASN C 713 REMARK 465 ASN C 714 REMARK 465 THR C 715 REMARK 465 ASN C 716 REMARK 465 GLU C 717 REMARK 465 GLY C 718 REMARK 465 CYS C 719 REMARK 465 ARG C 720 REMARK 465 THR C 721 REMARK 465 GLY C 722 REMARK 465 TRP C 723 REMARK 465 SER C 724 REMARK 465 HIS C 725 REMARK 465 PRO C 726 REMARK 465 GLN C 727 REMARK 465 PHE C 728 REMARK 465 GLU C 729 REMARK 465 LYS C 730 REMARK 465 SER H 144 REMARK 465 LYS H 145 REMARK 465 SER H 146 REMARK 465 THR H 147 REMARK 465 SER H 148 REMARK 465 SER H 231 REMARK 465 CYS H 232 REMARK 465 ASP H 233 REMARK 465 LYS H 234 REMARK 465 THR H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 HIS H 239 REMARK 465 HIS H 240 REMARK 465 HIS H 241 REMARK 465 GLN L 1 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 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 LEU C 582 OG1 THR C 586 2.07 REMARK 500 OH TYR H 59 O HOH H 401 2.15 REMARK 500 O SER H 143 O HOH H 402 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 ZN ZN C 802 ZN ZN C 802 2576 0.72 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 GLN L 108 C - N - CA ANGL. DEV. = -16.2 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 LYS C 661 -3.20 46.26 REMARK 500 GLN C 679 75.50 -68.87 REMARK 500 LEU H 48 -62.02 -109.44 REMARK 500 ARG H 67 -33.35 -155.07 REMARK 500 GLU H 89 1.95 -65.42 REMARK 500 CYS H 103 82.19 -150.19 REMARK 500 ASP H 160 85.90 48.94 REMARK 500 SER H 203 4.38 -69.67 REMARK 500 PRO L 37 121.65 -37.28 REMARK 500 ASP L 48 -43.99 67.30 REMARK 500 LYS L 93 79.97 48.30 REMARK 500 LYS L 110 132.09 -39.61 REMARK 500 ASP L 151 -100.98 50.00 REMARK 500 ASN L 170 -6.52 70.72 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 H 65 0.24 SIDE CHAIN REMARK 500 ARG L 36 0.08 SIDE CHAIN 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 C 907 DISTANCE = 7.06 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 ZN C 802 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LYS C 622 NZ REMARK 620 2 LYS C 622 NZ 0.0 REMARK 620 3 GLU C 625 OE2 77.8 77.8 REMARK 620 4 GLU C 625 OE2 77.8 77.8 0.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 32 NE2 REMARK 620 2 HOH H 430 O 72.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 88 OD1 REMARK 620 2 ASP H 88 OD2 53.9 REMARK 620 3 GLU H 89 OE2 84.2 101.4 REMARK 620 4 HOH H 408 O 109.9 56.3 115.2 REMARK 620 5 GLU L 198 OE2 94.8 58.6 64.6 51.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN H 303 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS H 180 NE2 REMARK 620 2 ASP L 138 OD1 120.4 REMARK 620 3 ASP L 138 OD2 103.5 52.1 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN L 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 65 OE2 REMARK 620 2 HIS L 188 NE2 95.4 REMARK 620 N 1 DBREF 8VDL C 567 730 PDB 8VDL 8VDL 567 730 DBREF 8VDL H 1 241 PDB 8VDL 8VDL 1 241 DBREF 8VDL L 1 212 PDB 8VDL 8VDL 1 212 SEQRES 1 C 164 LYS ILE THR SER PHE ASP GLU PHE PHE ASP PHE TRP VAL SEQRES 2 C 164 ARG LYS LEU LEU ILE ASP THR ILE LYS TRP GLU THR GLU SEQRES 3 C 164 LEU THR TYR CYS ILE ASN ASN THR ASP VAL THR ASP CYS SEQRES 4 C 164 ASN LYS CYS ASN LYS ASN CYS VAL CYS PHE ASP LYS TRP SEQRES 5 C 164 VAL LYS GLN LYS GLU ASP GLU TRP THR ASN ILE MET LYS SEQRES 6 C 164 LEU PHE THR ASN LYS HIS ASP ILE PRO LYS LYS TYR TYR SEQRES 7 C 164 LEU ASN ILE ASN ASP LEU PHE ASP SER PHE PHE PHE GLN SEQRES 8 C 164 VAL ILE TYR LYS PHE ASN GLU GLY GLU ALA LYS TRP ASN SEQRES 9 C 164 GLU LEU LYS GLU ASN LEU LYS LYS GLN ILE ALA SER SER SEQRES 10 C 164 LYS ALA ASN ASN GLY THR LYS ASP SER GLU ALA ALA ILE SEQRES 11 C 164 LYS VAL LEU PHE ASN HIS ILE LYS GLU ILE ALA THR ILE SEQRES 12 C 164 CYS LYS ASP ASN ASN THR ASN GLU GLY CYS ARG THR GLY SEQRES 13 C 164 TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 H 241 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA GLN SEQRES 2 H 241 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 241 PHE THR PHE ARG ASP HIS GLY MET THR TRP VAL ARG GLN SEQRES 4 H 241 VAL SER GLY LYS GLY LEU GLU TRP LEU SER TYR ILE THR SEQRES 5 H 241 ALA GLY SER LYS MET SER TYR TYR SER ASP SER VAL ARG SEQRES 6 H 241 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 241 LEU TYR LEU GLN MET ASN GLY LEU THR ASP GLU ASP SER SEQRES 8 H 241 ALA ILE TYR TYR CYS VAL LYS GLY GLY GLY ASN CYS PRO SEQRES 9 H 241 SER ASP THR CYS TYR PRO SER GLY TYR PHE GLY LEU ASP SEQRES 10 H 241 VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SEQRES 11 H 241 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 241 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 241 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 H 241 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 H 241 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 241 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 H 241 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 H 241 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS SEQRES 19 H 241 THR HIS HIS HIS HIS HIS HIS SEQRES 1 L 212 GLN SER GLU LEU THR GLN PRO PRO SER MET SER VAL SER SEQRES 2 L 212 PRO GLY GLN THR ALA MET ILE THR CYS SER MET ASN LYS SEQRES 3 L 212 TYR SER TYR ILE SER TRP TYR GLN GLN ARG PRO GLY GLN SEQRES 4 L 212 SER PRO ALA LEU VAL ILE TYR GLN ASP THR ARG ARG PRO SEQRES 5 L 212 SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SER GLU SEQRES 6 L 212 ASN THR ALA ILE LEU THR ILE THR GLY THR ARG ASP LEU SEQRES 7 L 212 ASP GLU ALA ASP TYR PHE CYS GLN GLY TRP ASP SER ASN SEQRES 8 L 212 VAL LYS ALA VAL LEU PHE GLY GLY GLY THR LYS LEU THR SEQRES 9 L 212 VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU SEQRES 10 L 212 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA SEQRES 11 L 212 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA SEQRES 12 L 212 VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS SEQRES 13 L 212 ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN SEQRES 14 L 212 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO SEQRES 15 L 212 GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL SEQRES 16 L 212 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO SEQRES 17 L 212 THR GLU CYS SER HET ZN C 801 1 HET ZN C 802 1 HET ZN H 301 1 HET ZN H 302 1 HET ZN H 303 1 HET ZN L 301 1 HETNAM ZN ZINC ION FORMUL 4 ZN 6(ZN 2+) FORMUL 10 HOH *140(H2 O) HELIX 1 AA1 PHE C 575 TRP C 589 1 15 HELIX 2 AA2 PHE C 615 THR C 627 1 13 HELIX 3 AA3 ASP C 649 SER C 653 1 5 HELIX 4 AA4 PHE C 654 TYR C 660 1 7 HELIX 5 AA5 GLU C 664 GLN C 679 1 16 HELIX 6 AA6 VAL C 698 ALA C 707 1 10 HELIX 7 AA7 THR H 28 HIS H 32 5 5 HELIX 8 AA8 THR H 87 SER H 91 5 5 HELIX 9 AA9 CYS H 103 THR H 107 5 5 HELIX 10 AB1 SER H 172 ALA H 174 5 3 HELIX 11 AB2 SER H 203 LEU H 205 5 3 HELIX 12 AB3 LYS H 217 ASN H 220 5 4 HELIX 13 AB4 SER L 121 ALA L 127 1 7 HELIX 14 AB5 THR L 181 SER L 187 1 7 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 SER H 17 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA1 4 SER H 78 ASN H 84 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA2 6 GLY H 10 ALA H 12 0 SHEET 2 AA2 6 THR H 123 VAL H 127 1 O THR H 126 N GLY H 10 SHEET 3 AA2 6 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 123 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 SER H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AA3 4 GLY H 10 ALA H 12 0 SHEET 2 AA3 4 THR H 123 VAL H 127 1 O THR H 126 N GLY H 10 SHEET 3 AA3 4 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 123 SHEET 4 AA3 4 LEU H 116 TRP H 119 -1 O VAL H 118 N LYS H 98 SHEET 1 AA4 4 SER H 136 LEU H 140 0 SHEET 2 AA4 4 THR H 151 TYR H 161 -1 O GLY H 155 N LEU H 140 SHEET 3 AA4 4 TYR H 192 PRO H 201 -1 O VAL H 198 N LEU H 154 SHEET 4 AA4 4 VAL H 179 THR H 181 -1 N HIS H 180 O VAL H 197 SHEET 1 AA5 4 SER H 136 LEU H 140 0 SHEET 2 AA5 4 THR H 151 TYR H 161 -1 O GLY H 155 N LEU H 140 SHEET 3 AA5 4 TYR H 192 PRO H 201 -1 O VAL H 198 N LEU H 154 SHEET 4 AA5 4 VAL H 185 LEU H 186 -1 N VAL H 185 O SER H 193 SHEET 1 AA6 3 THR H 167 TRP H 170 0 SHEET 2 AA6 3 ILE H 211 HIS H 216 -1 O ASN H 213 N SER H 169 SHEET 3 AA6 3 THR H 221 LYS H 226 -1 O VAL H 223 N VAL H 214 SHEET 1 AA7 5 SER L 9 VAL L 12 0 SHEET 2 AA7 5 THR L 101 VAL L 105 1 O THR L 104 N MET L 10 SHEET 3 AA7 5 ALA L 81 ASP L 89 -1 N ALA L 81 O LEU L 103 SHEET 4 AA7 5 SER L 31 GLN L 35 -1 N GLN L 35 O ASP L 82 SHEET 5 AA7 5 ALA L 42 ILE L 45 -1 O VAL L 44 N TRP L 32 SHEET 1 AA8 4 SER L 9 VAL L 12 0 SHEET 2 AA8 4 THR L 101 VAL L 105 1 O THR L 104 N MET L 10 SHEET 3 AA8 4 ALA L 81 ASP L 89 -1 N ALA L 81 O LEU L 103 SHEET 4 AA8 4 ALA L 94 PHE L 97 -1 O LEU L 96 N GLY L 87 SHEET 1 AA9 3 ALA L 18 SER L 23 0 SHEET 2 AA9 3 THR L 67 ILE L 72 -1 O ILE L 72 N ALA L 18 SHEET 3 AA9 3 PHE L 59 SER L 64 -1 N SER L 60 O THR L 71 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AB1 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AB1 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AB2 4 SER L 114 PHE L 118 0 SHEET 2 AB2 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AB2 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AB2 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AB3 4 SER L 153 PRO L 154 0 SHEET 2 AB3 4 VAL L 144 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AB3 4 TYR L 191 HIS L 197 -1 O THR L 196 N THR L 145 SHEET 4 AB3 4 SER L 200 VAL L 206 -1 O VAL L 202 N VAL L 195 SSBOND 1 CYS C 614 CYS C 614 1555 2576 2.04 SSBOND 2 CYS H 22 CYS H 96 1555 1555 2.06 SSBOND 3 CYS H 103 CYS H 108 1555 1555 2.07 SSBOND 4 CYS H 156 CYS H 212 1555 1555 2.03 SSBOND 5 CYS L 22 CYS L 85 1555 1555 2.08 SSBOND 6 CYS L 134 CYS L 193 1555 1555 2.05 LINK NZ LYS C 622 ZN ZN C 802 1555 1555 2.68 LINK NZ LYS C 622 ZN ZN C 802 1555 2576 2.00 LINK OE2 GLU C 625 ZN ZN C 802 1555 1555 1.92 LINK OE2 GLU C 625 ZN ZN C 802 1555 2576 2.03 LINK NE2 HIS C 702 ZN ZN C 801 1555 1555 2.30 LINK NE2 HIS H 32 ZN ZN H 301 1555 1555 2.27 LINK OD1 ASP H 88 ZN ZN H 302 1555 1555 2.23 LINK OD2 ASP H 88 ZN ZN H 302 1555 1555 2.55 LINK OE2 GLU H 89 ZN ZN H 302 1555 1555 1.91 LINK NE2 HIS H 180 ZN ZN H 303 1555 1555 2.25 LINK ZN ZN H 301 O HOH H 430 1555 1555 2.67 LINK ZN ZN H 302 O HOH H 408 1555 1555 2.66 LINK ZN ZN H 302 OE2 GLU L 198 3655 1555 1.84 LINK ZN ZN H 303 OD1 ASP L 138 1555 1555 2.56 LINK ZN ZN H 303 OD2 ASP L 138 1555 1555 2.50 LINK OE2 GLU L 65 ZN ZN L 301 1555 3655 2.08 LINK NE2 HIS L 188 ZN ZN L 301 1555 1555 2.26 CISPEP 1 PHE H 162 PRO H 163 0 -9.31 CISPEP 2 GLU H 164 PRO H 165 0 4.37 CISPEP 3 TYR L 140 PRO L 141 0 -0.29 CRYST1 55.653 65.353 250.341 90.00 90.00 90.00 P 2 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 0.017968 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015302 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003995 0.00000