HEADER PROTEIN TRANSPORT 07-FEB-24 8YA2 TITLE STRUCTURE OF THE SECA-SECY COMPLEX WITH THE SUBSTRATE FTSQ-LACY(+20C) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECA; COMPND 3 CHAIN: A; COMPND 4 EC: 7.4.2.8; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECY; COMPND 8 CHAIN: Y; COMPND 9 ENGINEERED: YES; COMPND 10 MUTATION: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECE; COMPND 13 CHAIN: E; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: CELL DIVISION PROTEIN FTSQ,LACTOSE PERMEASE; COMPND 17 CHAIN: B; COMPND 18 SYNONYM: LACTOSE-PROTON SYMPORT; COMPND 19 ENGINEERED: YES; COMPND 20 MUTATION: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: NANOBODY; COMPND 23 CHAIN: C; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: GREEN FLUORESCENT PROTEIN; COMPND 27 CHAIN: G; COMPND 28 ENGINEERED: YES; COMPND 29 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168; SOURCE 3 ORGANISM_TAXID: 224308; SOURCE 4 GENE: SECA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: GEOBACILLUS THERMODENITRIFICANS NG80-2; SOURCE 10 ORGANISM_TAXID: 420246; SOURCE 11 GENE: SECY; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: GEOBACILLUS THERMODENITRIFICANS NG80-2; SOURCE 17 ORGANISM_TAXID: 420246; SOURCE 18 GENE: SECE; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 21 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12; SOURCE 24 ORGANISM_TAXID: 83333; SOURCE 25 STRAIN: K-12; SOURCE 26 GENE: FTSQ, LACY; SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 29 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 30 MOL_ID: 5; SOURCE 31 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 32 ORGANISM_TAXID: 9844; SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 35 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA; SOURCE 38 ORGANISM_TAXID: 6100; SOURCE 39 GENE: GFP; SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 41 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 42 EXPRESSION_SYSTEM_STRAIN: K-12 KEYWDS PROTEIN TRANSLOCATION, SECY, MEMBRANE PROTEIN INSERTION, PROTEIN KEYWDS 2 CHAPERONE, PROTEIN TRANSPORT EXPDTA ELECTRON MICROSCOPY AUTHOR X.OU,C.MA,D.SUN,J.XU,X.WU,N.GAO,L.LI REVDAT 1 26-FEB-25 8YA2 0 JRNL AUTH X.OU,C.MA,D.SUN,J.XU,Y.WANG,X.WU,D.WANG,S.YANG,N.GAO,C.SONG, JRNL AUTH 2 L.LI JRNL TITL SECY TRANSLOCON CHAPERONES PROTEIN FOLDING DURING MEMBRANE JRNL TITL 2 PROTEIN INSERTION JRNL REF CELL 2025 REMARK 2 REMARK 2 RESOLUTION. 3.84 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 3.840 REMARK 3 NUMBER OF PARTICLES : 186802 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 8YA2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1300045224. 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 : SECA-SECY COMPLEX WITH THE REMARK 245 SUBSTRATE FTSQ-LACY(+20C) REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.00 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 5760.00 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) : 300 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Y, E, B, C, G 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 MET A 1 REMARK 465 LEU A 2 REMARK 465 GLY A 3 REMARK 465 ILE A 4 REMARK 465 LEU A 5 REMARK 465 ASN A 6 REMARK 465 LYS A 7 REMARK 465 MET A 8 REMARK 465 PHE A 9 REMARK 465 ASP A 10 REMARK 465 PRO A 11 REMARK 465 THR A 12 REMARK 465 LYS A 13 REMARK 465 MET Y 1 REMARK 465 ASN Y 51 REMARK 465 ALA Y 52 REMARK 465 PHE Y 53 REMARK 465 GLY Y 54 REMARK 465 VAL Y 55 REMARK 465 LEU Y 56 REMARK 465 ASN Y 57 REMARK 465 ILE Y 58 REMARK 465 PHE Y 203 REMARK 465 GLU Y 204 REMARK 465 ASN Y 205 REMARK 465 VAL Y 206 REMARK 465 GLY Y 207 REMARK 465 GLU Y 208 REMARK 465 ASP Y 209 REMARK 465 LEU Y 210 REMARK 465 THR Y 211 REMARK 465 MET E 1 REMARK 465 GLU E 60 REMARK 465 GLY E 61 REMARK 465 GLY E 62 REMARK 465 HIS E 63 REMARK 465 HIS E 64 REMARK 465 HIS E 65 REMARK 465 HIS E 66 REMARK 465 HIS E 67 REMARK 465 HIS E 68 REMARK 465 HIS E 69 REMARK 465 HIS E 70 REMARK 465 MET B 1 REMARK 465 GLY B 25 REMARK 465 ALA B 26 REMARK 465 GLN B 27 REMARK 465 TYR B 28 REMARK 465 GLU B 29 REMARK 465 ASP B 30 REMARK 465 GLY B 31 REMARK 465 SER B 32 REMARK 465 SER B 33 REMARK 465 GLY B 34 REMARK 465 VAL B 35 REMARK 465 THR B 59 REMARK 465 SER B 60 REMARK 465 ILE B 61 REMARK 465 SER B 62 REMARK 465 HIS B 69 REMARK 465 SER B 70 REMARK 465 TYR B 71 REMARK 465 HIS B 72 REMARK 465 SER B 73 REMARK 465 GLY B 74 REMARK 465 ASP B 75 REMARK 465 GLY B 76 REMARK 465 ASP B 77 REMARK 465 LYS B 78 REMARK 465 LEU B 79 REMARK 465 PRO B 80 REMARK 465 GLU B 81 REMARK 465 GLY B 82 REMARK 465 VAL B 83 REMARK 465 SER C 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 BE BEF A 1002 O3B ADP A 1003 1.40 REMARK 500 F1 BEF A 1002 O3B ADP A 1003 1.70 REMARK 500 BE BEF A 1002 PB ADP A 1003 1.71 REMARK 500 F2 BEF A 1002 O3B ADP A 1003 1.78 REMARK 500 OH GYS G 66 OH TYR G 145 1.87 REMARK 500 O LEU G 60 OG1 THR G 63 2.09 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 THR G 63 C PHE G 64 N 0.254 REMARK 500 VAL G 68 C GLN G 69 N 0.226 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 A 39 -5.06 68.50 REMARK 500 LEU A 61 32.11 -95.86 REMARK 500 VAL A 76 -61.37 -94.88 REMARK 500 ILE A 214 -52.08 -126.32 REMARK 500 ALA A 227 -168.16 -105.11 REMARK 500 THR A 231 -37.37 -130.38 REMARK 500 THR A 243 79.60 -101.95 REMARK 500 ALA A 246 -112.19 66.75 REMARK 500 GLN A 346 -168.94 -114.85 REMARK 500 GLU A 365 -16.50 72.55 REMARK 500 THR A 373 45.26 -142.08 REMARK 500 ILE A 384 -60.16 -100.22 REMARK 500 ASN A 395 -8.42 68.31 REMARK 500 ARG A 409 -155.57 -82.72 REMARK 500 VAL A 437 -58.79 -121.45 REMARK 500 LYS A 452 -2.34 75.37 REMARK 500 ASN A 463 32.55 -98.63 REMARK 500 GLN A 529 61.59 60.83 REMARK 500 ASP A 564 -30.96 -131.30 REMARK 500 ASP A 619 73.30 -100.60 REMARK 500 LEU A 623 50.33 -93.40 REMARK 500 GLU A 647 -74.28 -94.85 REMARK 500 LEU A 648 165.31 177.45 REMARK 500 GLU A 651 22.35 -140.60 REMARK 500 PRO Y 37 1.20 -60.66 REMARK 500 VAL Y 175 -60.29 -96.44 REMARK 500 ASN Y 332 74.63 57.67 REMARK 500 ARG Y 426 -65.58 -91.08 REMARK 500 ASN B 56 57.44 -98.71 REMARK 500 VAL C 48 -60.53 -109.67 REMARK 500 PHE G 8 40.01 -98.55 REMARK 500 PHE G 71 36.40 -94.79 REMARK 500 HIS G 81 38.66 -99.72 REMARK 500 ASP G 133 30.92 -89.90 REMARK 500 ASN G 159 48.42 34.82 REMARK 500 REMARK 500 REMARK: NULL 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 BEF A1002 BE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ADP A1003 O2B REMARK 620 2 BEF A1002 F1 137.0 REMARK 620 3 BEF A1002 F2 80.9 117.6 REMARK 620 4 BEF A1002 F3 76.7 118.5 117.4 REMARK 620 5 ADP A1003 O3A 72.5 69.8 140.9 84.1 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39088 RELATED DB: EMDB REMARK 900 STRUCTURE OF THE SECA-SECY COMPLEX WITH THE SUBSTRATE FTSQ-LACY(+ REMARK 900 20C) DBREF 8YA2 A 1 778 UNP P28366 SECA_BACSU 1 778 DBREF 8YA2 Y 1 430 UNP A4IJK8 A4IJK8_GEOTN 1 430 DBREF 8YA2 E 1 60 UNP A4IJH4 A4IJH4_GEOTN 1 60 DBREF 8YA2 B 1 25 UNP P06136 FTSQ_ECOLI 23 47 DBREF 8YA2 B 35 54 UNP P02920 LACY_ECOLI 315 334 DBREF 8YA2 C 2 113 PDB 8YA2 8YA2 2 113 DBREF 8YA2 G 3 229 UNP P42212 GFP_AEQVI 3 229 SEQADV 8YA2 CYS Y 60 UNP A4IJK8 GLY 60 ENGINEERED MUTATION SEQADV 8YA2 THR Y 202 UNP A4IJK8 GLN 202 ENGINEERED MUTATION SEQADV 8YA2 THR Y 211 UNP A4IJK8 PHE 211 ENGINEERED MUTATION SEQADV 8YA2 ASN Y 213 UNP A4IJK8 ARG 213 ENGINEERED MUTATION SEQADV 8YA2 GLY E 61 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 GLY E 62 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 63 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 64 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 65 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 66 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 67 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 68 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 69 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 HIS E 70 UNP A4IJH4 EXPRESSION TAG SEQADV 8YA2 MET B 1 UNP P06136 THR 23 ENGINEERED MUTATION SEQADV 8YA2 ALA B 2 UNP P06136 ARG 24 ENGINEERED MUTATION SEQADV 8YA2 LYS B 3 UNP P06136 LEU 25 ENGINEERED MUTATION SEQADV 8YA2 LYS B 4 UNP P06136 ALA 26 ENGINEERED MUTATION SEQADV 8YA2 THR B 5 UNP P06136 GLY 27 ENGINEERED MUTATION SEQADV 8YA2 ALA B 26 UNP P06136 LINKER SEQADV 8YA2 GLN B 27 UNP P06136 LINKER SEQADV 8YA2 TYR B 28 UNP P06136 LINKER SEQADV 8YA2 GLU B 29 UNP P06136 LINKER SEQADV 8YA2 ASP B 30 UNP P06136 LINKER SEQADV 8YA2 GLY B 31 UNP P06136 LINKER SEQADV 8YA2 SER B 32 UNP P06136 LINKER SEQADV 8YA2 SER B 33 UNP P06136 LINKER SEQADV 8YA2 GLY B 34 UNP P06136 LINKER SEQADV 8YA2 CYS B 45 UNP P02920 GLU 325 ENGINEERED MUTATION SEQADV 8YA2 ALA B 53 UNP P02920 CYS 333 ENGINEERED MUTATION SEQADV 8YA2 SER B 55 UNP P02920 LINKER SEQADV 8YA2 ASN B 56 UNP P02920 LINKER SEQADV 8YA2 ALA B 57 UNP P02920 LINKER SEQADV 8YA2 ASP B 58 UNP P02920 LINKER SEQADV 8YA2 THR B 59 UNP P02920 LINKER SEQADV 8YA2 SER B 60 UNP P02920 LINKER SEQADV 8YA2 ILE B 61 UNP P02920 LINKER SEQADV 8YA2 SER B 62 UNP P02920 LINKER SEQADV 8YA2 GLY B 63 UNP P02920 LINKER SEQADV 8YA2 ASP B 64 UNP P02920 LINKER SEQADV 8YA2 GLY B 65 UNP P02920 LINKER SEQADV 8YA2 ASP B 66 UNP P02920 LINKER SEQADV 8YA2 SER B 67 UNP P02920 LINKER SEQADV 8YA2 PRO B 68 UNP P02920 LINKER SEQADV 8YA2 HIS B 69 UNP P02920 LINKER SEQADV 8YA2 SER B 70 UNP P02920 LINKER SEQADV 8YA2 TYR B 71 UNP P02920 LINKER SEQADV 8YA2 HIS B 72 UNP P02920 LINKER SEQADV 8YA2 SER B 73 UNP P02920 LINKER SEQADV 8YA2 GLY B 74 UNP P02920 LINKER SEQADV 8YA2 ASP B 75 UNP P02920 LINKER SEQADV 8YA2 GLY B 76 UNP P02920 LINKER SEQADV 8YA2 ASP B 77 UNP P02920 LINKER SEQADV 8YA2 LYS B 78 UNP P02920 LINKER SEQADV 8YA2 LEU B 79 UNP P02920 LINKER SEQADV 8YA2 PRO B 80 UNP P02920 LINKER SEQADV 8YA2 GLU B 81 UNP P02920 LINKER SEQADV 8YA2 GLY B 82 UNP P02920 LINKER SEQADV 8YA2 VAL B 83 UNP P02920 LINKER SEQADV 8YA2 GYS G 66 UNP P42212 SER 65 CHROMOPHORE SEQADV 8YA2 GYS G 66 UNP P42212 TYR 66 CHROMOPHORE SEQADV 8YA2 ARG G 80 UNP P42212 GLN 80 ENGINEERED MUTATION SEQADV 8YA2 SER G 99 UNP P42212 PHE 99 ENGINEERED MUTATION SEQADV 8YA2 THR G 153 UNP P42212 MET 153 ENGINEERED MUTATION SEQADV 8YA2 ALA G 163 UNP P42212 VAL 163 ENGINEERED MUTATION SEQRES 1 A 778 MET LEU GLY ILE LEU ASN LYS MET PHE ASP PRO THR LYS SEQRES 2 A 778 ARG THR LEU ASN ARG TYR GLU LYS ILE ALA ASN ASP ILE SEQRES 3 A 778 ASP ALA ILE ARG GLY ASP TYR GLU ASN LEU SER ASP ASP SEQRES 4 A 778 ALA LEU LYS HIS LYS THR ILE GLU PHE LYS GLU ARG LEU SEQRES 5 A 778 GLU LYS GLY ALA THR THR ASP ASP LEU LEU VAL GLU ALA SEQRES 6 A 778 PHE ALA VAL VAL ARG GLU ALA SER ARG ARG VAL THR GLY SEQRES 7 A 778 MET PHE PRO PHE LYS VAL GLN LEU MET GLY GLY VAL ALA SEQRES 8 A 778 LEU HIS ASP GLY ASN ILE ALA GLU MET LYS THR GLY GLU SEQRES 9 A 778 GLY LYS THR LEU THR SER THR LEU PRO VAL TYR LEU ASN SEQRES 10 A 778 ALA LEU THR GLY LYS GLY VAL HIS VAL VAL THR VAL ASN SEQRES 11 A 778 GLU TYR LEU ALA SER ARG ASP ALA GLU GLN MET GLY LYS SEQRES 12 A 778 ILE PHE GLU PHE LEU GLY LEU THR VAL GLY LEU ASN LEU SEQRES 13 A 778 ASN SER MET SER LYS ASP GLU LYS ARG GLU ALA TYR ALA SEQRES 14 A 778 ALA ASP ILE THR TYR SER THR ASN ASN GLU LEU GLY PHE SEQRES 15 A 778 ASP TYR LEU ARG ASP ASN MET VAL LEU TYR LYS GLU GLN SEQRES 16 A 778 MET VAL GLN ARG PRO LEU HIS PHE ALA VAL ILE ASP GLU SEQRES 17 A 778 VAL ASP SER ILE LEU ILE ASP GLU ALA ARG THR PRO LEU SEQRES 18 A 778 ILE ILE SER GLY GLN ALA ALA LYS SER THR LYS LEU TYR SEQRES 19 A 778 VAL GLN ALA ASN ALA PHE VAL ARG THR LEU LYS ALA GLU SEQRES 20 A 778 LYS ASP TYR THR TYR ASP ILE LYS THR LYS ALA VAL GLN SEQRES 21 A 778 LEU THR GLU GLU GLY MET THR LYS ALA GLU LYS ALA PHE SEQRES 22 A 778 GLY ILE ASP ASN LEU PHE ASP VAL LYS HIS VAL ALA LEU SEQRES 23 A 778 ASN HIS HIS ILE ASN GLN ALA LEU LYS ALA HIS VAL ALA SEQRES 24 A 778 MET GLN LYS ASP VAL ASP TYR VAL VAL GLU ASP GLY GLN SEQRES 25 A 778 VAL VAL ILE VAL ASP SER PHE THR GLY ARG LEU MET LYS SEQRES 26 A 778 GLY ARG ARG TYR SER GLU GLY LEU HIS GLN ALA ILE GLU SEQRES 27 A 778 ALA LYS GLU GLY LEU GLU ILE GLN ASN GLU SER MET THR SEQRES 28 A 778 LEU ALA THR ILE THR PHE GLN ASN TYR PHE ARG MET TYR SEQRES 29 A 778 GLU LYS LEU ALA GLY MET THR GLY THR ALA LYS THR GLU SEQRES 30 A 778 GLU GLU GLU PHE ARG ASN ILE TYR ASN MET GLN VAL VAL SEQRES 31 A 778 THR ILE PRO THR ASN ARG PRO VAL VAL ARG ASP ASP ARG SEQRES 32 A 778 PRO ASP LEU ILE TYR ARG THR MET GLU GLY LYS PHE LYS SEQRES 33 A 778 ALA VAL ALA GLU ASP VAL ALA GLN ARG TYR MET THR GLY SEQRES 34 A 778 GLN PRO VAL LEU VAL GLY THR VAL ALA VAL GLU THR SER SEQRES 35 A 778 GLU LEU ILE SER LYS LEU LEU LYS ASN LYS GLY ILE PRO SEQRES 36 A 778 HIS GLN VAL LEU ASN ALA LYS ASN HIS GLU ARG GLU ALA SEQRES 37 A 778 GLN ILE ILE GLU GLU ALA GLY GLN LYS GLY ALA VAL THR SEQRES 38 A 778 ILE ALA THR ASN MET ALA GLY ARG GLY THR ASP ILE LYS SEQRES 39 A 778 LEU GLY GLU GLY VAL LYS GLU LEU GLY GLY LEU ALA VAL SEQRES 40 A 778 VAL GLY THR GLU ARG HIS GLU SER ARG ARG ILE ASP ASN SEQRES 41 A 778 GLN LEU ARG GLY ARG SER GLY ARG GLN GLY ASP PRO GLY SEQRES 42 A 778 ILE THR GLN PHE TYR LEU SER MET GLU ASP GLU LEU MET SEQRES 43 A 778 ARG ARG PHE GLY ALA GLU ARG THR MET ALA MET LEU ASP SEQRES 44 A 778 ARG PHE GLY MET ASP ASP SER THR PRO ILE GLN SER LYS SEQRES 45 A 778 MET VAL SER ARG ALA VAL GLU SER SER GLN LYS ARG VAL SEQRES 46 A 778 GLU GLY ASN ASN PHE ASP SER ARG LYS GLN LEU LEU GLN SEQRES 47 A 778 TYR ASP ASP VAL LEU ARG GLN GLN ARG GLU VAL ILE TYR SEQRES 48 A 778 LYS GLN ARG PHE GLU VAL ILE ASP SER GLU ASN LEU ARG SEQRES 49 A 778 GLU ILE VAL GLU ASN MET ILE LYS SER SER LEU GLU ARG SEQRES 50 A 778 ALA ILE ALA ALA TYR THR PRO ARG GLU GLU LEU PRO GLU SEQRES 51 A 778 GLU TRP LYS LEU ASP GLY LEU VAL ASP LEU ILE ASN THR SEQRES 52 A 778 THR TYR LEU ASP GLU GLY ALA LEU GLU LYS SER ASP ILE SEQRES 53 A 778 PHE GLY LYS GLU PRO ASP GLU MET LEU GLU LEU ILE MET SEQRES 54 A 778 ASP ARG ILE ILE THR LYS TYR ASN GLU LYS GLU GLU GLN SEQRES 55 A 778 PHE GLY LYS GLU GLN MET ARG GLU PHE GLU LYS VAL ILE SEQRES 56 A 778 VAL LEU ARG ALA VAL ASP SER LYS TRP MET ASP HIS ILE SEQRES 57 A 778 ASP ALA MET ASP GLN LEU ARG GLN GLY ILE HIS LEU ARG SEQRES 58 A 778 ALA TYR ALA GLN THR ASN PRO LEU ARG GLU TYR GLN MET SEQRES 59 A 778 GLU GLY PHE ALA MET PHE GLU HIS MET ILE GLU SER ILE SEQRES 60 A 778 GLU ASP GLU VAL ALA LYS PHE VAL MET LYS ALA SEQRES 1 Y 430 MET PHE ARG THR ILE SER ASN PHE MET ARG VAL SER ASP SEQRES 2 Y 430 ILE ARG ASN LYS ILE ILE PHE THR LEU LEU MET LEU ILE SEQRES 3 Y 430 VAL PHE ARG ILE GLY THR PHE ILE PRO VAL PRO SER VAL SEQRES 4 Y 430 ASN THR ASP VAL LEU LYS LEU GLN ASP GLN LEU ASN ALA SEQRES 5 Y 430 PHE GLY VAL LEU ASN ILE PHE CYS GLY GLY ALA LEU GLN SEQRES 6 Y 430 ASN PHE SER ILE PHE ALA MET GLY VAL MET PRO TYR ILE SEQRES 7 Y 430 THR ALA SER ILE ILE VAL GLN LEU LEU GLN MET ASP VAL SEQRES 8 Y 430 VAL PRO LYS PHE ALA GLU TRP SER LYS GLN GLY GLU MET SEQRES 9 Y 430 GLY ARG ARG LYS LEU ALA GLN PHE THR ARG TYR PHE THR SEQRES 10 Y 430 ILE VAL LEU GLY PHE ILE GLN ALA LEU GLY MET SER TYR SEQRES 11 Y 430 GLY PHE ASN ASN LEU ALA GLY GLY MET LEU ILE GLN ASN SEQRES 12 Y 430 PRO GLY ILE GLY THR TYR LEU LEU ILE ALA VAL VAL LEU SEQRES 13 Y 430 THR ALA GLY THR ALA PHE LEU MET TRP LEU GLY GLU GLN SEQRES 14 Y 430 ILE THR ALA LYS GLY VAL GLY ASN GLY ILE SER ILE ILE SEQRES 15 Y 430 ILE PHE ALA GLY ILE VAL SER GLY ILE PRO THR ILE LEU SEQRES 16 Y 430 ASN GLN ILE TYR ALA GLN THR PHE GLU ASN VAL GLY GLU SEQRES 17 Y 430 ASP LEU THR LEU ASN ILE VAL ARG LEU LEU LEU VAL ALA SEQRES 18 Y 430 LEU ALA VAL VAL ALA VAL ILE VAL GLY VAL ILE TYR ILE SEQRES 19 Y 430 GLN GLN ALA PHE ARG LYS ILE PRO ILE GLN TYR ALA LYS SEQRES 20 Y 430 ARG LEU GLU GLY ARG ASN PRO VAL GLY GLY HIS SER THR SEQRES 21 Y 430 HIS LEU PRO LEU LYS VAL ASN PRO ALA GLY VAL ILE PRO SEQRES 22 Y 430 VAL ILE PHE ALA VAL SER PHE LEU ILE ALA PRO PRO THR SEQRES 23 Y 430 ILE ALA SER PHE PHE GLY THR ASN ASP VAL THR LEU TRP SEQRES 24 Y 430 ILE ARG ARG THR PHE ASP TYR THR HIS PRO VAL GLY MET SEQRES 25 Y 430 THR ILE TYR VAL VAL LEU ILE ILE ALA PHE THR TYR PHE SEQRES 26 Y 430 TYR ALA PHE VAL GLN VAL ASN PRO GLU GLN MET ALA ASP SEQRES 27 Y 430 ASN LEU LYS LYS GLN GLY GLY TYR ILE PRO GLY ILE ARG SEQRES 28 Y 430 PRO GLY LYS ASN THR GLN GLU TYR VAL THR ARG ILE LEU SEQRES 29 Y 430 TYR ARG LEU THR LEU VAL GLY SER LEU PHE LEU ALA PHE SEQRES 30 Y 430 ILE ALA VAL LEU PRO VAL PHE PHE VAL ASN PHE ALA ASN SEQRES 31 Y 430 LEU PRO PRO SER ALA GLN ILE GLY GLY THR SER LEU LEU SEQRES 32 Y 430 ILE VAL VAL GLY VAL ALA LEU GLU THR MET LYS GLN LEU SEQRES 33 Y 430 GLU SER GLN LEU VAL LYS ARG HIS TYR ARG GLY PHE ILE SEQRES 34 Y 430 LYS SEQRES 1 E 70 MET GLN ARG VAL THR ASN PHE PHE LYS GLU VAL VAL ARG SEQRES 2 E 70 GLU LEU LYS LYS VAL SER TRP PRO ASN ARG LYS GLU LEU SEQRES 3 E 70 VAL ASN TYR THR ALA VAL VAL LEU ALA THR VAL ALA PHE SEQRES 4 E 70 PHE THR VAL PHE PHE ALA VAL ILE ASP LEU GLY ILE SER SEQRES 5 E 70 GLN LEU ILE ARG LEU VAL PHE GLU GLY GLY HIS HIS HIS SEQRES 6 E 70 HIS HIS HIS HIS HIS SEQRES 1 B 83 MET ALA LYS LYS THR ILE LEU PHE LEU LEU THR VAL LEU SEQRES 2 B 83 THR THR VAL LEU VAL SER GLY TRP VAL VAL LEU GLY ALA SEQRES 3 B 83 GLN TYR GLU ASP GLY SER SER GLY VAL VAL ILE LEU LYS SEQRES 4 B 83 THR LEU HIS MET PHE CYS VAL PRO PHE LEU LEU VAL GLY SEQRES 5 B 83 ALA PHE SER ASN ALA ASP THR SER ILE SER GLY ASP GLY SEQRES 6 B 83 ASP SER PRO HIS SER TYR HIS SER GLY ASP GLY ASP LYS SEQRES 7 B 83 LEU PRO GLU GLY VAL SEQRES 1 C 114 VAL ALA LEU VAL GLU SER GLY GLY ALA LEU VAL GLN PRO SEQRES 2 C 114 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE SEQRES 3 C 114 PRO VAL ASN ARG TYR SER MET ARG TRP TYR ARG GLN ALA SEQRES 4 C 114 PRO GLY LYS GLU ARG GLU TRP VAL ALA GLY MET SER SER SEQRES 5 C 114 ALA GLY ASP ARG SER SER TYR GLU ASP SER VAL LYS GLY SEQRES 6 C 114 ARG PHE THR ILE SER ARG ASP ASP ALA ARG ASN THR VAL SEQRES 7 C 114 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 C 114 VAL TYR TYR CYS ASN VAL ASN VAL GLY PHE GLU TYR TRP SEQRES 9 C 114 GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 G 225 LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO ILE LEU SEQRES 2 G 225 VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS PHE SER SEQRES 3 G 225 VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR GLY LYS SEQRES 4 G 225 LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS LEU PRO SEQRES 5 G 225 VAL PRO TRP PRO THR LEU VAL THR THR PHE GYS VAL GLN SEQRES 6 G 225 CYS PHE SER ARG TYR PRO ASP HIS MET LYS ARG HIS ASP SEQRES 7 G 225 PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL GLN GLU SEQRES 8 G 225 ARG THR ILE SER PHE LYS ASP ASP GLY ASN TYR LYS THR SEQRES 9 G 225 ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU VAL ASN SEQRES 10 G 225 ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU ASP GLY SEQRES 11 G 225 ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN TYR ASN SER SEQRES 12 G 225 HIS ASN VAL TYR ILE THR ALA ASP LYS GLN LYS ASN GLY SEQRES 13 G 225 ILE LYS ALA ASN PHE LYS ILE ARG HIS ASN ILE GLU ASP SEQRES 14 G 225 GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN ASN THR SEQRES 15 G 225 PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP ASN HIS SEQRES 16 G 225 TYR LEU SER THR GLN SER ALA LEU SER LYS ASP PRO ASN SEQRES 17 G 225 GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE VAL THR SEQRES 18 G 225 ALA ALA GLY ILE MODRES 8YA2 GYS G 66 SER CHROMOPHORE MODRES 8YA2 GYS G 66 TYR CHROMOPHORE HET GYS G 66 21 HET MG A1001 1 HET BEF A1002 4 HET ADP A1003 27 HETNAM GYS [(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4- HETNAM 2 GYS HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1- HETNAM 3 GYS YL]ACETIC ACID HETNAM MG MAGNESIUM ION HETNAM BEF BERYLLIUM TRIFLUORIDE ION HETNAM ADP ADENOSINE-5'-DIPHOSPHATE HETSYN GYS CHROMOPHORE (SER-TYR-GLY) FORMUL 6 GYS C14 H15 N3 O5 FORMUL 7 MG MG 2+ FORMUL 8 BEF BE F3 1- FORMUL 9 ADP C10 H15 N5 O10 P2 HELIX 1 AA1 ARG A 14 GLU A 34 1 21 HELIX 2 AA2 ASP A 39 GLU A 53 1 15 HELIX 3 AA3 LEU A 61 THR A 77 1 17 HELIX 4 AA4 PHE A 82 ASP A 94 1 13 HELIX 5 AA5 GLY A 105 ALA A 118 1 14 HELIX 6 AA6 ASN A 130 GLY A 149 1 20 HELIX 7 AA7 SER A 160 ALA A 169 1 10 HELIX 8 AA8 ASN A 177 ASP A 187 1 11 HELIX 9 AA9 GLU A 208 ILE A 214 1 7 HELIX 10 AB1 THR A 231 THR A 243 1 13 HELIX 11 AB2 LYS A 245 LYS A 248 5 4 HELIX 12 AB3 THR A 262 GLY A 274 1 13 HELIX 13 AB4 ASP A 280 LYS A 282 5 3 HELIX 14 AB5 HIS A 283 ALA A 299 1 17 HELIX 15 AB6 GLN A 301 ASP A 305 1 5 HELIX 16 AB7 GLY A 332 GLU A 341 1 10 HELIX 17 AB8 THR A 356 MET A 363 1 8 HELIX 18 AB9 GLU A 377 ILE A 384 1 8 HELIX 19 AC1 THR A 410 MET A 427 1 18 HELIX 20 AC2 VAL A 439 LEU A 449 1 11 HELIX 21 AC3 ASN A 463 GLU A 465 5 3 HELIX 22 AC4 ARG A 466 GLU A 473 1 8 HELIX 23 AC5 ALA A 474 GLN A 476 5 3 HELIX 24 AC6 THR A 484 GLY A 488 5 5 HELIX 25 AC7 VAL A 499 GLY A 503 5 5 HELIX 26 AC8 SER A 515 ARG A 525 1 11 HELIX 27 AC9 ASP A 543 GLY A 550 1 8 HELIX 28 AD1 GLU A 552 ALA A 556 5 5 HELIX 29 AD2 MET A 557 GLY A 562 5 6 HELIX 30 AD3 SER A 571 ASP A 619 1 49 HELIX 31 AD4 LEU A 623 TYR A 642 1 20 HELIX 32 AD5 LYS A 653 THR A 664 1 12 HELIX 33 AD6 ASP A 667 LEU A 671 5 5 HELIX 34 AD7 GLU A 672 ILE A 676 5 5 HELIX 35 AD8 GLU A 680 GLY A 704 1 25 HELIX 36 AD9 LYS A 705 ALA A 742 1 38 HELIX 37 AE1 ASN A 747 MET A 776 1 30 HELIX 38 AE2 ARG Y 3 VAL Y 11 1 9 HELIX 39 AE3 VAL Y 11 THR Y 32 1 22 HELIX 40 AE4 ASN Y 40 LEU Y 50 1 11 HELIX 41 AE5 CYS Y 60 ASN Y 66 1 7 HELIX 42 AE6 VAL Y 74 GLN Y 88 1 15 HELIX 43 AE7 VAL Y 92 LYS Y 100 1 9 HELIX 44 AE8 GLY Y 102 GLY Y 137 1 36 HELIX 45 AE9 THR Y 148 GLY Y 174 1 27 HELIX 46 AF1 ASN Y 177 THR Y 202 1 26 HELIX 47 AF2 ILE Y 214 GLN Y 236 1 23 HELIX 48 AF3 VAL Y 271 GLY Y 292 1 22 HELIX 49 AF4 ASN Y 294 PHE Y 304 1 11 HELIX 50 AF5 GLY Y 311 VAL Y 331 1 21 HELIX 51 AF6 ASN Y 332 GLN Y 343 1 12 HELIX 52 AF7 GLY Y 353 ALA Y 389 1 37 HELIX 53 AF8 GLY Y 399 HIS Y 424 1 26 HELIX 54 AF9 VAL E 4 LYS E 16 1 13 HELIX 55 AG1 ASN E 22 VAL E 58 1 37 HELIX 56 AG2 LYS B 3 SER B 19 1 17 HELIX 57 AG3 ILE B 37 CYS B 45 1 9 HELIX 58 AG4 LYS C 83 THR C 87 5 5 HELIX 59 AG5 TRP G 57 THR G 62 1 6 SHEET 1 AA1 2 ILE A 97 GLU A 99 0 SHEET 2 AA1 2 VAL A 389 THR A 391 1 O VAL A 390 N ILE A 97 SHEET 1 AA2 5 VAL A 152 LEU A 154 0 SHEET 2 AA2 5 ILE A 172 THR A 176 1 O ILE A 172 N GLY A 153 SHEET 3 AA2 5 VAL A 124 THR A 128 1 N VAL A 126 O SER A 175 SHEET 4 AA2 5 PHE A 203 ILE A 206 1 O VAL A 205 N VAL A 127 SHEET 5 AA2 5 LEU A 367 GLY A 369 1 O ALA A 368 N ILE A 206 SHEET 1 AA3 2 LEU A 221 GLN A 226 0 SHEET 2 AA3 2 SER A 349 ILE A 355 -1 O ILE A 355 N LEU A 221 SHEET 1 AA4 2 TYR A 250 ASP A 253 0 SHEET 2 AA4 2 ALA A 258 LEU A 261 -1 O GLN A 260 N THR A 251 SHEET 1 AA5 2 TYR A 306 GLU A 309 0 SHEET 2 AA5 2 GLN A 312 ILE A 315 -1 O GLN A 312 N GLU A 309 SHEET 1 AA6 5 ARG A 400 ASP A 402 0 SHEET 2 AA6 5 GLY A 533 GLN A 536 1 O THR A 535 N ASP A 401 SHEET 3 AA6 5 ALA A 506 VAL A 508 1 N VAL A 507 O ILE A 534 SHEET 4 AA6 5 VAL A 432 GLY A 435 1 N LEU A 433 O VAL A 508 SHEET 5 AA6 5 VAL A 480 ALA A 483 1 O ALA A 483 N VAL A 434 SHEET 1 AA7 2 ILE A 407 TYR A 408 0 SHEET 2 AA7 2 LEU A 539 SER A 540 1 O LEU A 539 N TYR A 408 SHEET 1 AA8 2 PHE Y 238 PRO Y 242 0 SHEET 2 AA8 2 HIS Y 261 LYS Y 265 -1 O LEU Y 262 N ILE Y 241 SHEET 1 AA9 4 VAL C 5 SER C 7 0 SHEET 2 AA9 4 SER C 21 ALA C 23 -1 O ALA C 23 N VAL C 5 SHEET 3 AA9 4 THR C 77 TYR C 79 -1 O VAL C 78 N CYS C 22 SHEET 4 AA9 4 SER C 70 ASP C 72 -1 N SER C 70 O TYR C 79 SHEET 1 AB1 5 ARG C 56 TYR C 59 0 SHEET 2 AB1 5 GLU C 46 SER C 52 -1 N GLY C 50 O SER C 58 SHEET 3 AB1 5 MET C 34 GLN C 39 -1 N TRP C 36 O ALA C 49 SHEET 4 AB1 5 ALA C 88 ASN C 95 -1 O TYR C 91 N TYR C 37 SHEET 5 AB1 5 GLU C 101 TRP C 103 -1 O TYR C 102 N VAL C 94 SHEET 1 AB2 5 ARG C 56 TYR C 59 0 SHEET 2 AB2 5 GLU C 46 SER C 52 -1 N GLY C 50 O SER C 58 SHEET 3 AB2 5 MET C 34 GLN C 39 -1 N TRP C 36 O ALA C 49 SHEET 4 AB2 5 ALA C 88 ASN C 95 -1 O TYR C 91 N TYR C 37 SHEET 5 AB2 5 THR C 107 VAL C 109 -1 O THR C 107 N TYR C 90 SHEET 1 AB312 VAL G 12 VAL G 22 0 SHEET 2 AB312 HIS G 25 ASP G 36 -1 O GLY G 33 N ILE G 14 SHEET 3 AB312 LYS G 41 CYS G 48 -1 O THR G 43 N GLU G 34 SHEET 4 AB312 HIS G 217 ALA G 227 -1 O LEU G 220 N LEU G 44 SHEET 5 AB312 HIS G 199 SER G 208 -1 N GLN G 204 O PHE G 223 SHEET 6 AB312 HIS G 148 ASP G 155 -1 N ILE G 152 O HIS G 199 SHEET 7 AB312 GLY G 160 ASN G 170 -1 O GLY G 160 N ASP G 155 SHEET 8 AB312 VAL G 176 PRO G 187 -1 O ALA G 179 N ILE G 167 SHEET 9 AB312 TYR G 92 PHE G 100 -1 N VAL G 93 O THR G 186 SHEET 10 AB312 ASN G 105 GLU G 115 -1 O ALA G 110 N GLN G 94 SHEET 11 AB312 THR G 118 ILE G 128 -1 O VAL G 120 N LYS G 113 SHEET 12 AB312 VAL G 12 VAL G 22 1 N GLU G 17 O ILE G 123 SSBOND 1 CYS Y 60 CYS B 45 1555 1555 2.04 SSBOND 2 CYS C 22 CYS C 92 1555 1555 2.03 LINK C PHE G 64 N1 GYS G 66 1555 1555 1.60 LINK C3 GYS G 66 N VAL G 68 1555 1555 1.31 LINK MG MG A1001 O2B ADP A1003 1555 1555 2.33 LINK BE BEF A1002 O2B ADP A1003 1555 1555 2.01 LINK BE BEF A1002 O3A ADP A1003 1555 1555 2.11 CISPEP 1 MET G 88 PRO G 89 0 8.55 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