HEADER PROTEIN TRANSPORT 07-FEB-24 8YA0 TITLE STRUCTURE OF THE SECA-SECY COMPLEX WITH THE SUBSTRATE FTSQ-LACY(+7C) 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: NANOBODY; COMPND 17 CHAIN: V; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: CELL DIVISION PROTEIN FTSQ,LACTOSE PERMEASE; COMPND 21 CHAIN: B; COMPND 22 SYNONYM: LACTOSE-PROTON SYMPORT; COMPND 23 ENGINEERED: YES; COMPND 24 MUTATION: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: NANOBODY; COMPND 27 CHAIN: C; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 7; COMPND 30 MOLECULE: GREEN FLUORESCENT PROTEIN; COMPND 31 CHAIN: G; COMPND 32 ENGINEERED: YES; COMPND 33 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: LAMA GLAMA; SOURCE 24 ORGANISM_TAXID: 9844; SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 27 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12; SOURCE 30 ORGANISM_TAXID: 83333; SOURCE 31 STRAIN: K-12; SOURCE 32 GENE: FTSQ, LACY; 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: LAMA GLAMA; SOURCE 38 ORGANISM_TAXID: 9844; SOURCE 39 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 41 EXPRESSION_SYSTEM_STRAIN: K-12; SOURCE 42 MOL_ID: 7; SOURCE 43 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA; SOURCE 44 ORGANISM_TAXID: 6100; SOURCE 45 GENE: GFP; SOURCE 46 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 47 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 48 EXPRESSION_SYSTEM_STRAIN: K-12 KEYWDS PROTEIN TRANSLOCATION, MEMBRANE PROTEIN INSERTION, PROTEIN CHAPERONE, KEYWDS 2 PROTEIN TRANSPORT EXPDTA ELECTRON MICROSCOPY AUTHOR X.OU,C.MA,D.SUN,J.XU,X.WU,N.GAO,L.LI REVDAT 2 05-MAR-25 8YA0 1 JRNL REVDAT 1 26-FEB-25 8YA0 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 JRNL REFN ISSN 1097-4172 JRNL PMID 39978345 JRNL DOI 10.1016/J.CELL.2025.01.037 REMARK 2 REMARK 2 RESOLUTION. 2.97 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) : 2.970 REMARK 3 NUMBER OF PARTICLES : 443770 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 8YA0 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_1300045212. 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(+7C) 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) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 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: HEPTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Y, E, V, 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 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 ALA B 52A REMARK 465 PHE B 52B REMARK 465 SER B 52C REMARK 465 ASN B 52D REMARK 465 ALA B 52E REMARK 465 ASP B 52F REMARK 465 THR B 52G REMARK 465 SER B 52H REMARK 465 ILE B 52I REMARK 465 SER B 52J REMARK 465 GLY B 52K REMARK 465 ASP B 52L REMARK 465 GLY B 52M 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 V 86 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 CB ALA C 53 NH2 ARG C 71 1.45 REMARK 500 OE1 GLN A 745 NZ LYS Y 265 1.65 REMARK 500 F1 BEF A 1002 O3B ADP A 1003 1.84 REMARK 500 O ALA A 778 N VAL C 2 1.86 REMARK 500 OH GYS G 66 OH TYR G 145 1.87 REMARK 500 CA ALA C 53 NH2 ARG C 71 2.06 REMARK 500 O LEU G 60 OG1 THR G 63 2.09 REMARK 500 OG SER Y 289 CG2 VAL B 23 2.11 REMARK 500 F3 BEF A 1002 O1B ADP A 1003 2.16 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 0.253 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: 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 GLY C 54 N - CA - C ANGL. DEV. = 21.3 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 ASP A 39 -8.28 73.58 REMARK 500 LYS A 54 -70.95 -71.60 REMARK 500 ALA A 227 -167.57 -101.98 REMARK 500 THR A 243 79.60 -119.94 REMARK 500 LEU A 244 14.22 -147.45 REMARK 500 LYS A 245 84.00 52.57 REMARK 500 ALA A 246 -13.95 -49.99 REMARK 500 LYS A 302 -71.06 -66.03 REMARK 500 MET A 350 116.15 -162.90 REMARK 500 GLU A 365 -19.07 70.38 REMARK 500 PRO A 393 -175.59 -65.18 REMARK 500 ASN A 395 -7.03 73.00 REMARK 500 THR A 436 -167.39 -101.27 REMARK 500 VAL A 437 -53.07 -120.87 REMARK 500 LYS A 452 -6.49 82.62 REMARK 500 THR A 484 -157.57 -90.06 REMARK 500 ARG A 489 -41.52 -132.10 REMARK 500 LEU A 505 76.29 57.13 REMARK 500 ARG A 528 68.51 62.32 REMARK 500 ASP A 564 -58.00 -123.03 REMARK 500 ASP A 565 71.01 53.68 REMARK 500 GLN A 570 56.67 -96.30 REMARK 500 GLU A 668 -16.71 72.15 REMARK 500 ASN Y 40 70.20 61.53 REMARK 500 VAL Y 91 -54.25 -125.94 REMARK 500 ASN Y 143 72.88 52.80 REMARK 500 GLU Y 250 58.68 38.06 REMARK 500 ASN Y 253 76.25 53.14 REMARK 500 HIS Y 258 53.36 -92.00 REMARK 500 ASN Y 332 77.78 58.87 REMARK 500 SER V 25 -60.46 -100.64 REMARK 500 ASN V 30 58.78 -94.83 REMARK 500 ARG V 38 -66.48 -96.64 REMARK 500 LYS V 43 -159.59 -75.47 REMARK 500 ARG V 44 75.77 63.61 REMARK 500 ARG V 45 137.32 -39.32 REMARK 500 GLU B 29 -3.35 66.17 REMARK 500 ALA C 3 95.03 -174.63 REMARK 500 VAL C 48 -62.75 -100.47 REMARK 500 ALA C 53 -120.22 71.54 REMARK 500 LEU C 80 -150.86 -105.16 REMARK 500 PHE G 8 40.01 -98.57 REMARK 500 PHE G 71 36.39 -94.78 REMARK 500 HIS G 81 38.65 -99.72 REMARK 500 ASP G 133 30.96 -89.92 REMARK 500 ASN G 159 48.43 34.77 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 O3B REMARK 620 2 BEF A1002 F1 70.4 REMARK 620 3 BEF A1002 F2 124.8 115.9 REMARK 620 4 BEF A1002 F3 99.8 117.9 118.5 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39087 RELATED DB: EMDB REMARK 900 STRUCTURE OF THE SECA-SECY COMPLEX WITH THE SUBSTRATE FTSQ-LACY(+7C) DBREF 8YA0 A 14 778 UNP P28366 SECA_BACSU 14 778 DBREF 8YA0 Y 2 430 UNP A4IJK8 A4IJK8_GEOTN 2 430 DBREF 8YA0 E 2 59 UNP A4IJH4 A4IJH4_GEOTN 2 59 DBREF 8YA0 V 1 116 PDB 8YA0 8YA0 1 116 DBREF 8YA0 B 2 25 UNP Q7CR81 FTSQ_SALTY 25 48 DBREF 8YA0 B 36 52 UNP P02920 LACY_ECOLI 316 332 DBREF 8YA0 C 2 112 PDB 8YA0 8YA0 2 112 DBREF 8YA0 G 3 229 UNP P42212 GFP_AEQVI 3 229 SEQADV 8YA0 CYS Y 60 UNP A4IJK8 GLY 60 ENGINEERED MUTATION SEQADV 8YA0 THR Y 202 UNP A4IJK8 GLN 202 ENGINEERED MUTATION SEQADV 8YA0 THR Y 211 UNP A4IJK8 PHE 211 ENGINEERED MUTATION SEQADV 8YA0 ASN Y 213 UNP A4IJK8 ARG 213 ENGINEERED MUTATION SEQADV 8YA0 ALA B 2 UNP Q7CR81 ARG 25 ENGINEERED MUTATION SEQADV 8YA0 LYS B 3 UNP Q7CR81 LEU 26 ENGINEERED MUTATION SEQADV 8YA0 LYS B 4 UNP Q7CR81 ALA 27 ENGINEERED MUTATION SEQADV 8YA0 THR B 5 UNP Q7CR81 GLY 28 ENGINEERED MUTATION SEQADV 8YA0 THR B 14 UNP Q7CR81 CYS 37 ENGINEERED MUTATION SEQADV 8YA0 LEU B 17 UNP Q7CR81 PHE 40 ENGINEERED MUTATION SEQADV 8YA0 ALA B 26 UNP Q7CR81 LINKER SEQADV 8YA0 GLN B 27 UNP Q7CR81 LINKER SEQADV 8YA0 TYR B 28 UNP Q7CR81 LINKER SEQADV 8YA0 GLU B 29 UNP Q7CR81 LINKER SEQADV 8YA0 ASP B 30 UNP Q7CR81 LINKER SEQADV 8YA0 GLY B 31 UNP Q7CR81 LINKER SEQADV 8YA0 CYS B 32 UNP Q7CR81 LINKER SEQADV 8YA0 SER B 33 UNP Q7CR81 LINKER SEQADV 8YA0 GLY B 34 UNP Q7CR81 LINKER SEQADV 8YA0 VAL B 35 UNP Q7CR81 LINKER SEQADV 8YA0 ALA B 52A UNP P02920 LINKER SEQADV 8YA0 PHE B 52B UNP P02920 LINKER SEQADV 8YA0 SER B 52C UNP P02920 LINKER SEQADV 8YA0 ASN B 52D UNP P02920 LINKER SEQADV 8YA0 ALA B 52E UNP P02920 LINKER SEQADV 8YA0 ASP B 52F UNP P02920 LINKER SEQADV 8YA0 THR B 52G UNP P02920 LINKER SEQADV 8YA0 SER B 52H UNP P02920 LINKER SEQADV 8YA0 ILE B 52I UNP P02920 LINKER SEQADV 8YA0 SER B 52J UNP P02920 LINKER SEQADV 8YA0 GLY B 52K UNP P02920 LINKER SEQADV 8YA0 ASP B 52L UNP P02920 LINKER SEQADV 8YA0 GLY B 52M UNP P02920 LINKER SEQADV 8YA0 ASP B 61 UNP P02920 LINKER SEQADV 8YA0 SER B 62 UNP P02920 LINKER SEQADV 8YA0 PRO B 63 UNP P02920 LINKER SEQADV 8YA0 HIS B 64 UNP P02920 LINKER SEQADV 8YA0 SER B 65 UNP P02920 LINKER SEQADV 8YA0 TYR B 66 UNP P02920 LINKER SEQADV 8YA0 HIS B 67 UNP P02920 LINKER SEQADV 8YA0 SER B 68 UNP P02920 LINKER SEQADV 8YA0 GYS G 66 UNP P42212 SER 65 CHROMOPHORE SEQADV 8YA0 GYS G 66 UNP P42212 TYR 66 CHROMOPHORE SEQADV 8YA0 ARG G 80 UNP P42212 GLN 80 ENGINEERED MUTATION SEQADV 8YA0 SER G 99 UNP P42212 PHE 99 ENGINEERED MUTATION SEQADV 8YA0 THR G 153 UNP P42212 MET 153 ENGINEERED MUTATION SEQADV 8YA0 ALA G 163 UNP P42212 VAL 163 ENGINEERED MUTATION SEQRES 1 A 765 ARG THR LEU ASN ARG TYR GLU LYS ILE ALA ASN ASP ILE SEQRES 2 A 765 ASP ALA ILE ARG GLY ASP TYR GLU ASN LEU SER ASP ASP SEQRES 3 A 765 ALA LEU LYS HIS LYS THR ILE GLU PHE LYS GLU ARG LEU SEQRES 4 A 765 GLU LYS GLY ALA THR THR ASP ASP LEU LEU VAL GLU ALA SEQRES 5 A 765 PHE ALA VAL VAL ARG GLU ALA SER ARG ARG VAL THR GLY SEQRES 6 A 765 MET PHE PRO PHE LYS VAL GLN LEU MET GLY GLY VAL ALA SEQRES 7 A 765 LEU HIS ASP GLY ASN ILE ALA GLU MET LYS THR GLY GLU SEQRES 8 A 765 GLY LYS THR LEU THR SER THR LEU PRO VAL TYR LEU ASN SEQRES 9 A 765 ALA LEU THR GLY LYS GLY VAL HIS VAL VAL THR VAL ASN SEQRES 10 A 765 GLU TYR LEU ALA SER ARG ASP ALA GLU GLN MET GLY LYS SEQRES 11 A 765 ILE PHE GLU PHE LEU GLY LEU THR VAL GLY LEU ASN LEU SEQRES 12 A 765 ASN SER MET SER LYS ASP GLU LYS ARG GLU ALA TYR ALA SEQRES 13 A 765 ALA ASP ILE THR TYR SER THR ASN ASN GLU LEU GLY PHE SEQRES 14 A 765 ASP TYR LEU ARG ASP ASN MET VAL LEU TYR LYS GLU GLN SEQRES 15 A 765 MET VAL GLN ARG PRO LEU HIS PHE ALA VAL ILE ASP GLU SEQRES 16 A 765 VAL ASP SER ILE LEU ILE ASP GLU ALA ARG THR PRO LEU SEQRES 17 A 765 ILE ILE SER GLY GLN ALA ALA LYS SER THR LYS LEU TYR SEQRES 18 A 765 VAL GLN ALA ASN ALA PHE VAL ARG THR LEU LYS ALA GLU SEQRES 19 A 765 LYS ASP TYR THR TYR ASP ILE LYS THR LYS ALA VAL GLN SEQRES 20 A 765 LEU THR GLU GLU GLY MET THR LYS ALA GLU LYS ALA PHE SEQRES 21 A 765 GLY ILE ASP ASN LEU PHE ASP VAL LYS HIS VAL ALA LEU SEQRES 22 A 765 ASN HIS HIS ILE ASN GLN ALA LEU LYS ALA HIS VAL ALA SEQRES 23 A 765 MET GLN LYS ASP VAL ASP TYR VAL VAL GLU ASP GLY GLN SEQRES 24 A 765 VAL VAL ILE VAL ASP SER PHE THR GLY ARG LEU MET LYS SEQRES 25 A 765 GLY ARG ARG TYR SER GLU GLY LEU HIS GLN ALA ILE GLU SEQRES 26 A 765 ALA LYS GLU GLY LEU GLU ILE GLN ASN GLU SER MET THR SEQRES 27 A 765 LEU ALA THR ILE THR PHE GLN ASN TYR PHE ARG MET TYR SEQRES 28 A 765 GLU LYS LEU ALA GLY MET THR GLY THR ALA LYS THR GLU SEQRES 29 A 765 GLU GLU GLU PHE ARG ASN ILE TYR ASN MET GLN VAL VAL SEQRES 30 A 765 THR ILE PRO THR ASN ARG PRO VAL VAL ARG ASP ASP ARG SEQRES 31 A 765 PRO ASP LEU ILE TYR ARG THR MET GLU GLY LYS PHE LYS SEQRES 32 A 765 ALA VAL ALA GLU ASP VAL ALA GLN ARG TYR MET THR GLY SEQRES 33 A 765 GLN PRO VAL LEU VAL GLY THR VAL ALA VAL GLU THR SER SEQRES 34 A 765 GLU LEU ILE SER LYS LEU LEU LYS ASN LYS GLY ILE PRO SEQRES 35 A 765 HIS GLN VAL LEU ASN ALA LYS ASN HIS GLU ARG GLU ALA SEQRES 36 A 765 GLN ILE ILE GLU GLU ALA GLY GLN LYS GLY ALA VAL THR SEQRES 37 A 765 ILE ALA THR ASN MET ALA GLY ARG GLY THR ASP ILE LYS SEQRES 38 A 765 LEU GLY GLU GLY VAL LYS GLU LEU GLY GLY LEU ALA VAL SEQRES 39 A 765 VAL GLY THR GLU ARG HIS GLU SER ARG ARG ILE ASP ASN SEQRES 40 A 765 GLN LEU ARG GLY ARG SER GLY ARG GLN GLY ASP PRO GLY SEQRES 41 A 765 ILE THR GLN PHE TYR LEU SER MET GLU ASP GLU LEU MET SEQRES 42 A 765 ARG ARG PHE GLY ALA GLU ARG THR MET ALA MET LEU ASP SEQRES 43 A 765 ARG PHE GLY MET ASP ASP SER THR PRO ILE GLN SER LYS SEQRES 44 A 765 MET VAL SER ARG ALA VAL GLU SER SER GLN LYS ARG VAL SEQRES 45 A 765 GLU GLY ASN ASN PHE ASP SER ARG LYS GLN LEU LEU GLN SEQRES 46 A 765 TYR ASP ASP VAL LEU ARG GLN GLN ARG GLU VAL ILE TYR SEQRES 47 A 765 LYS GLN ARG PHE GLU VAL ILE ASP SER GLU ASN LEU ARG SEQRES 48 A 765 GLU ILE VAL GLU ASN MET ILE LYS SER SER LEU GLU ARG SEQRES 49 A 765 ALA ILE ALA ALA TYR THR PRO ARG GLU GLU LEU PRO GLU SEQRES 50 A 765 GLU TRP LYS LEU ASP GLY LEU VAL ASP LEU ILE ASN THR SEQRES 51 A 765 THR TYR LEU ASP GLU GLY ALA LEU GLU LYS SER ASP ILE SEQRES 52 A 765 PHE GLY LYS GLU PRO ASP GLU MET LEU GLU LEU ILE MET SEQRES 53 A 765 ASP ARG ILE ILE THR LYS TYR ASN GLU LYS GLU GLU GLN SEQRES 54 A 765 PHE GLY LYS GLU GLN MET ARG GLU PHE GLU LYS VAL ILE SEQRES 55 A 765 VAL LEU ARG ALA VAL ASP SER LYS TRP MET ASP HIS ILE SEQRES 56 A 765 ASP ALA MET ASP GLN LEU ARG GLN GLY ILE HIS LEU ARG SEQRES 57 A 765 ALA TYR ALA GLN THR ASN PRO LEU ARG GLU TYR GLN MET SEQRES 58 A 765 GLU GLY PHE ALA MET PHE GLU HIS MET ILE GLU SER ILE SEQRES 59 A 765 GLU ASP GLU VAL ALA LYS PHE VAL MET LYS ALA SEQRES 1 Y 429 PHE ARG THR ILE SER ASN PHE MET ARG VAL SER ASP ILE SEQRES 2 Y 429 ARG ASN LYS ILE ILE PHE THR LEU LEU MET LEU ILE VAL SEQRES 3 Y 429 PHE ARG ILE GLY THR PHE ILE PRO VAL PRO SER VAL ASN SEQRES 4 Y 429 THR ASP VAL LEU LYS LEU GLN ASP GLN LEU ASN ALA PHE SEQRES 5 Y 429 GLY VAL LEU ASN ILE PHE CYS GLY GLY ALA LEU GLN ASN SEQRES 6 Y 429 PHE SER ILE PHE ALA MET GLY VAL MET PRO TYR ILE THR SEQRES 7 Y 429 ALA SER ILE ILE VAL GLN LEU LEU GLN MET ASP VAL VAL SEQRES 8 Y 429 PRO LYS PHE ALA GLU TRP SER LYS GLN GLY GLU MET GLY SEQRES 9 Y 429 ARG ARG LYS LEU ALA GLN PHE THR ARG TYR PHE THR ILE SEQRES 10 Y 429 VAL LEU GLY PHE ILE GLN ALA LEU GLY MET SER TYR GLY SEQRES 11 Y 429 PHE ASN ASN LEU ALA GLY GLY MET LEU ILE GLN ASN PRO SEQRES 12 Y 429 GLY ILE GLY THR TYR LEU LEU ILE ALA VAL VAL LEU THR SEQRES 13 Y 429 ALA GLY THR ALA PHE LEU MET TRP LEU GLY GLU GLN ILE SEQRES 14 Y 429 THR ALA LYS GLY VAL GLY ASN GLY ILE SER ILE ILE ILE SEQRES 15 Y 429 PHE ALA GLY ILE VAL SER GLY ILE PRO THR ILE LEU ASN SEQRES 16 Y 429 GLN ILE TYR ALA GLN THR PHE GLU ASN VAL GLY GLU ASP SEQRES 17 Y 429 LEU THR LEU ASN ILE VAL ARG LEU LEU LEU VAL ALA LEU SEQRES 18 Y 429 ALA VAL VAL ALA VAL ILE VAL GLY VAL ILE TYR ILE GLN SEQRES 19 Y 429 GLN ALA PHE ARG LYS ILE PRO ILE GLN TYR ALA LYS ARG SEQRES 20 Y 429 LEU GLU GLY ARG ASN PRO VAL GLY GLY HIS SER THR HIS SEQRES 21 Y 429 LEU PRO LEU LYS VAL ASN PRO ALA GLY VAL ILE PRO VAL SEQRES 22 Y 429 ILE PHE ALA VAL SER PHE LEU ILE ALA PRO PRO THR ILE SEQRES 23 Y 429 ALA SER PHE PHE GLY THR ASN ASP VAL THR LEU TRP ILE SEQRES 24 Y 429 ARG ARG THR PHE ASP TYR THR HIS PRO VAL GLY MET THR SEQRES 25 Y 429 ILE TYR VAL VAL LEU ILE ILE ALA PHE THR TYR PHE TYR SEQRES 26 Y 429 ALA PHE VAL GLN VAL ASN PRO GLU GLN MET ALA ASP ASN SEQRES 27 Y 429 LEU LYS LYS GLN GLY GLY TYR ILE PRO GLY ILE ARG PRO SEQRES 28 Y 429 GLY LYS ASN THR GLN GLU TYR VAL THR ARG ILE LEU TYR SEQRES 29 Y 429 ARG LEU THR LEU VAL GLY SER LEU PHE LEU ALA PHE ILE SEQRES 30 Y 429 ALA VAL LEU PRO VAL PHE PHE VAL ASN PHE ALA ASN LEU SEQRES 31 Y 429 PRO PRO SER ALA GLN ILE GLY GLY THR SER LEU LEU ILE SEQRES 32 Y 429 VAL VAL GLY VAL ALA LEU GLU THR MET LYS GLN LEU GLU SEQRES 33 Y 429 SER GLN LEU VAL LYS ARG HIS TYR ARG GLY PHE ILE LYS SEQRES 1 E 58 GLN ARG VAL THR ASN PHE PHE LYS GLU VAL VAL ARG GLU SEQRES 2 E 58 LEU LYS LYS VAL SER TRP PRO ASN ARG LYS GLU LEU VAL SEQRES 3 E 58 ASN TYR THR ALA VAL VAL LEU ALA THR VAL ALA PHE PHE SEQRES 4 E 58 THR VAL PHE PHE ALA VAL ILE ASP LEU GLY ILE SER GLN SEQRES 5 E 58 LEU ILE ARG LEU VAL PHE SEQRES 1 V 116 GLN VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 V 116 PRO GLY GLY SER LEU ARG LEU SER CYS GLY ALA SER GLY SEQRES 3 V 116 SER ILE PHE ASN MET TYR ALA MET GLY TRP TYR ARG GLN SEQRES 4 V 116 ALA PRO GLY LYS ARG ARG GLU VAL VAL ALA ARG ILE ALA SEQRES 5 V 116 THR ASP ASP SER THR MET TYR PRO ASP SER VAL LYS GLY SEQRES 6 V 116 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 V 116 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 V 116 VAL TYR TYR CYS TYR TYR GLN ARG THR VAL MET SER GLN SEQRES 9 V 116 PRO TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 1 B 72 ALA LYS LYS THR ILE LEU PHE LEU LEU THR VAL LEU THR SEQRES 2 B 72 THR VAL LEU VAL SER GLY TRP VAL VAL LEU GLY ALA GLN SEQRES 3 B 72 TYR GLU ASP GLY CYS SER GLY VAL VAL ILE LEU LYS THR SEQRES 4 B 72 LEU HIS MET PHE GLU VAL PRO PHE LEU LEU VAL GLY ALA SEQRES 5 B 72 PHE SER ASN ALA ASP THR SER ILE SER GLY ASP GLY ASP SEQRES 6 B 72 SER PRO HIS SER TYR HIS SER SEQRES 1 C 113 VAL ALA LEU VAL GLU SER GLY GLY ALA LEU VAL GLN PRO SEQRES 2 C 113 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE SEQRES 3 C 113 PRO VAL ASN ARG TYR SER MET ARG TRP TYR ARG GLN ALA SEQRES 4 C 113 PRO GLY LYS GLU ARG GLU TRP VAL ALA GLY MET SER SER SEQRES 5 C 113 ALA GLY ASP ARG SER SER TYR GLU ASP SER VAL LYS GLY SEQRES 6 C 113 ARG PHE THR ILE SER ARG ASP ASP ALA ARG ASN THR VAL SEQRES 7 C 113 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 C 113 VAL TYR TYR CYS ASN VAL ASN VAL GLY PHE GLU TYR TRP SEQRES 9 C 113 GLY GLN GLY THR GLN VAL THR VAL 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 8YA0 GYS G 66 SER CHROMOPHORE MODRES 8YA0 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 7 GYS C14 H15 N3 O5 FORMUL 8 MG MG 2+ FORMUL 9 BEF BE F3 1- FORMUL 10 ADP C10 H15 N5 O10 P2 HELIX 1 AA1 ARG A 14 TYR A 33 1 20 HELIX 2 AA2 LYS A 42 GLY A 55 1 14 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 ASN A 188 1 12 HELIX 9 AA9 TYR A 192 MET A 196 5 5 HELIX 10 AB1 GLU A 208 ILE A 214 1 7 HELIX 11 AB2 ASP A 215 ARG A 218 5 4 HELIX 12 AB3 THR A 231 ARG A 242 1 12 HELIX 13 AB4 THR A 262 PHE A 273 1 12 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 GLY A 342 1 11 HELIX 17 AB8 PHE A 357 ARG A 362 1 6 HELIX 18 AB9 ALA A 374 THR A 376 5 3 HELIX 19 AC1 GLU A 377 ILE A 384 1 8 HELIX 20 AC2 THR A 410 MET A 427 1 18 HELIX 21 AC3 ALA A 438 ASN A 451 1 14 HELIX 22 AC4 ASN A 463 GLU A 465 5 3 HELIX 23 AC5 ARG A 466 ALA A 474 1 9 HELIX 24 AC6 GLY A 498 LEU A 502 5 5 HELIX 25 AC7 SER A 515 ARG A 528 1 14 HELIX 26 AC8 ASP A 543 GLY A 550 1 8 HELIX 27 AC9 ARG A 553 MET A 557 5 5 HELIX 28 AD1 LYS A 572 ASP A 619 1 48 HELIX 29 AD2 LEU A 623 TYR A 642 1 20 HELIX 30 AD3 LYS A 653 TYR A 665 1 13 HELIX 31 AD4 GLU A 672 ILE A 676 5 5 HELIX 32 AD5 GLU A 680 GLY A 704 1 25 HELIX 33 AD6 LYS A 705 ALA A 742 1 38 HELIX 34 AD7 TYR A 743 GLN A 745 5 3 HELIX 35 AD8 ASN A 747 LYS A 777 1 31 HELIX 36 AD9 ARG Y 3 MET Y 9 1 7 HELIX 37 AE1 VAL Y 11 PHE Y 33 1 23 HELIX 38 AE2 ASN Y 40 GLN Y 47 1 8 HELIX 39 AE3 VAL Y 74 MET Y 89 1 16 HELIX 40 AE4 VAL Y 92 GLY Y 102 1 11 HELIX 41 AE5 MET Y 104 GLY Y 137 1 34 HELIX 42 AE6 GLY Y 145 LYS Y 173 1 29 HELIX 43 AE7 ASN Y 177 THR Y 202 1 26 HELIX 44 AE8 ASN Y 213 GLN Y 236 1 24 HELIX 45 AE9 VAL Y 271 PHE Y 290 1 20 HELIX 46 AF1 ASN Y 294 PHE Y 304 1 11 HELIX 47 AF2 HIS Y 308 VAL Y 331 1 24 HELIX 48 AF3 ASN Y 332 GLY Y 344 1 13 HELIX 49 AF4 GLY Y 353 PHE Y 388 1 36 HELIX 50 AF5 GLY Y 399 VAL Y 421 1 23 HELIX 51 AF6 LYS Y 422 HIS Y 424 5 3 HELIX 52 AF7 ARG E 3 LYS E 16 1 14 HELIX 53 AF8 ASN E 22 PHE E 59 1 38 HELIX 54 AF9 LYS V 86 THR V 90 5 5 HELIX 55 AG1 LYS B 3 GLY B 20 1 18 HELIX 56 AG2 TRP B 21 LEU B 24 5 4 HELIX 57 AG3 VAL B 36 MET B 43 1 8 HELIX 58 AG4 PRO C 28 TYR C 32 5 5 HELIX 59 AG5 LYS C 83 THR C 87 5 5 HELIX 60 AG6 TRP G 57 THR G 62 1 6 SHEET 1 AA1 7 VAL A 152 LEU A 154 0 SHEET 2 AA1 7 ILE A 172 THR A 176 1 O ILE A 172 N GLY A 153 SHEET 3 AA1 7 VAL A 124 THR A 128 1 N VAL A 126 O THR A 173 SHEET 4 AA1 7 PHE A 203 ASP A 207 1 O PHE A 203 N HIS A 125 SHEET 5 AA1 7 LEU A 367 THR A 371 1 O ALA A 368 N ALA A 204 SHEET 6 AA1 7 ILE A 97 GLU A 99 1 N ALA A 98 O GLY A 369 SHEET 7 AA1 7 VAL A 389 THR A 391 1 O VAL A 390 N GLU A 99 SHEET 1 AA2 4 ARG A 327 TYR A 329 0 SHEET 2 AA2 4 HIS B 64 HIS B 67 -1 O SER B 65 N ARG A 328 SHEET 3 AA2 4 PRO A 220 GLN A 226 1 N ILE A 222 O TYR B 66 SHEET 4 AA2 4 SER A 349 THR A 356 -1 O LEU A 352 N ILE A 223 SHEET 1 AA3 2 TYR A 250 ASP A 253 0 SHEET 2 AA3 2 ALA A 258 LEU A 261 -1 O ALA A 258 N ASP A 253 SHEET 1 AA4 3 TYR A 306 GLU A 309 0 SHEET 2 AA4 3 GLN A 312 VAL A 316 -1 O VAL A 314 N VAL A 307 SHEET 3 AA4 3 LEU A 323 MET A 324 -1 O MET A 324 N ILE A 315 SHEET 1 AA5 3 ARG A 400 ASP A 402 0 SHEET 2 AA5 3 GLY A 533 SER A 540 1 O GLY A 533 N ASP A 401 SHEET 3 AA5 3 LEU A 406 TYR A 408 1 N LEU A 406 O PHE A 537 SHEET 1 AA6 6 ARG A 400 ASP A 402 0 SHEET 2 AA6 6 GLY A 533 SER A 540 1 O GLY A 533 N ASP A 401 SHEET 3 AA6 6 ALA A 506 GLY A 509 1 N VAL A 507 O ILE A 534 SHEET 4 AA6 6 VAL A 432 GLY A 435 1 N LEU A 433 O VAL A 508 SHEET 5 AA6 6 VAL A 480 ALA A 483 1 O ALA A 483 N VAL A 434 SHEET 6 AA6 6 HIS A 456 LEU A 459 1 N GLN A 457 O ILE A 482 SHEET 1 AA7 2 ASN Y 57 CYS Y 60 0 SHEET 2 AA7 2 ALA Y 63 ASN Y 66 -1 O GLN Y 65 N ILE Y 58 SHEET 1 AA8 3 HIS Y 261 LYS Y 265 0 SHEET 2 AA8 3 PHE Y 238 PRO Y 242 -1 N ARG Y 239 O LEU Y 264 SHEET 3 AA8 3 VAL E 18 SER E 19 -1 O SER E 19 N PHE Y 238 SHEET 1 AA9 2 GLN Y 244 TYR Y 245 0 SHEET 2 AA9 2 GLY Y 345 TYR Y 346 -1 O TYR Y 346 N GLN Y 244 SHEET 1 AB1 4 LEU V 4 THR V 7 0 SHEET 2 AB1 4 SER V 17 ALA V 24 -1 O SER V 21 N THR V 7 SHEET 3 AB1 4 THR V 77 ASN V 83 -1 O VAL V 78 N CYS V 22 SHEET 4 AB1 4 PHE V 67 ASP V 72 -1 N SER V 70 O TYR V 79 SHEET 1 AB2 4 VAL V 47 ALA V 52 0 SHEET 2 AB2 4 ALA V 33 TYR V 37 -1 N TRP V 36 O ALA V 49 SHEET 3 AB2 4 ALA V 91 GLN V 98 -1 O TYR V 94 N TYR V 37 SHEET 4 AB2 4 THR V 111 VAL V 113 -1 O VAL V 113 N ALA V 91 SHEET 1 AB3 4 VAL C 5 SER C 7 0 SHEET 2 AB3 4 SER C 21 ALA C 23 -1 O ALA C 23 N VAL C 5 SHEET 3 AB3 4 THR C 77 TYR C 79 -1 O VAL C 78 N CYS C 22 SHEET 4 AB3 4 SER C 70 ASP C 72 -1 N SER C 70 O TYR C 79 SHEET 1 AB4 5 SER C 57 TYR C 59 0 SHEET 2 AB4 5 GLU C 46 MET C 51 -1 N GLY C 50 O SER C 58 SHEET 3 AB4 5 MET C 34 GLN C 39 -1 N TRP C 36 O ALA C 49 SHEET 4 AB4 5 ALA C 88 VAL C 94 -1 O ASN C 93 N ARG C 35 SHEET 5 AB4 5 TYR C 102 TRP C 103 -1 O TYR C 102 N VAL C 94 SHEET 1 AB5 5 SER C 57 TYR C 59 0 SHEET 2 AB5 5 GLU C 46 MET C 51 -1 N GLY C 50 O SER C 58 SHEET 3 AB5 5 MET C 34 GLN C 39 -1 N TRP C 36 O ALA C 49 SHEET 4 AB5 5 ALA C 88 VAL C 94 -1 O ASN C 93 N ARG C 35 SHEET 5 AB5 5 THR C 107 VAL C 109 -1 O THR C 107 N TYR C 90 SHEET 1 AB612 VAL G 12 VAL G 22 0 SHEET 2 AB612 HIS G 25 ASP G 36 -1 O GLY G 33 N ILE G 14 SHEET 3 AB612 LYS G 41 CYS G 48 -1 O THR G 43 N GLU G 34 SHEET 4 AB612 HIS G 217 ALA G 227 -1 O LEU G 220 N LEU G 44 SHEET 5 AB612 HIS G 199 SER G 208 -1 N GLN G 204 O PHE G 223 SHEET 6 AB612 HIS G 148 ASP G 155 -1 N ILE G 152 O HIS G 199 SHEET 7 AB612 GLY G 160 ASN G 170 -1 O GLY G 160 N ASP G 155 SHEET 8 AB612 VAL G 176 PRO G 187 -1 O ALA G 179 N ILE G 167 SHEET 9 AB612 TYR G 92 PHE G 100 -1 N VAL G 93 O THR G 186 SHEET 10 AB612 ASN G 105 GLU G 115 -1 O ALA G 110 N GLN G 94 SHEET 11 AB612 THR G 118 ILE G 128 -1 O VAL G 120 N LYS G 113 SHEET 12 AB612 VAL G 12 VAL G 22 1 N GLU G 17 O ILE G 123 SSBOND 1 CYS Y 60 CYS B 32 1555 1555 2.03 SSBOND 2 CYS V 22 CYS V 95 1555 1555 2.04 SSBOND 3 CYS C 22 CYS C 92 1555 1555 2.04 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 O1B ADP A1003 1555 1555 2.11 LINK BE BEF A1002 O3B ADP A1003 1555 1555 1.40 CISPEP 1 MET G 88 PRO G 89 0 8.54 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