HEADER UNKNOWN FUNCTION 29-OCT-16 5M8R
TITLE CRYSTAL STRUCTURE OF HUMAN TYROSINASE RELATED PROTEIN 1 (T391V-R374S-
TITLE 2 Y362F) IN COMPLEX WITH MIMOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5,6-DIHYDROXYINDOLE-2-CARBOXYLIC ACID OXIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DHICA OXIDASE,CATALASE B,GLYCOPROTEIN 75,MELANOMA ANTIGEN
COMPND 5 GP75,TYROSINASE-RELATED PROTEIN 1,TRP1;
COMPND 6 EC: 1.14.18.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TYRP1, CAS2, TYRP, TYRRP;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS HUMAN TYROSINASE RELATED PROTEIN 1, MELANIN BIOSYNTHESIS, TYROSINASE,
KEYWDS 2 OXIDOREDUCTASE, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LAI,M.SOLER-LOPEZ,H.J.WICHERS,B.W.DIJKSTRA
REVDAT 4 29-JUL-20 5M8R 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 16-OCT-19 5M8R 1 REMARK
REVDAT 2 09-AUG-17 5M8R 1 JRNL
REVDAT 1 12-JUL-17 5M8R 0
JRNL AUTH X.LAI,H.J.WICHERS,M.SOLER-LOPEZ,B.W.DIJKSTRA
JRNL TITL STRUCTURE OF HUMAN TYROSINASE RELATED PROTEIN 1 REVEALS A
JRNL TITL 2 BINUCLEAR ZINC ACTIVE SITE IMPORTANT FOR MELANOGENESIS.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 9812 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 28661582
JRNL DOI 10.1002/ANIE.201704616
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 94043
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 4651
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 5M8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1200002092.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 290
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94135
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 58.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS (PH 7.0), 0.2 M NACL AND
REMARK 280 30% (W/V) PEG 3000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 290K
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 44.67650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.47550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.86350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.47550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.67650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.86350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, G, H
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I, J, K, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, M
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 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 NH2 ARG D 118 O HOH D 601 1.95
REMARK 500 O4 NAG M 1 O HOH D 602 2.10
REMARK 500 NH1 ARG C 269 OD1 ASN C 314 2.11
REMARK 500 ND2 ASN D 181 O5 NAG D 503 2.15
REMARK 500 O4 NAG B 511 O HOH B 601 2.19
REMARK 500 O4 NAG C 513 O HOH C 601 2.19
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 LEU A 427 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG B 114 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 LEU D 265 CA - CB - CG ANGL. DEV. = 16.8 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 LEU A 45 -72.94 -103.59
REMARK 500 SER A 60 -158.13 -82.93
REMARK 500 ASP A 212 107.35 -165.11
REMARK 500 MET A 266 -23.28 76.71
REMARK 500 ASP A 273 111.99 -164.72
REMARK 500 CYS A 290 31.79 73.06
REMARK 500 SER A 292 55.79 -114.15
REMARK 500 ASN A 304 -165.04 -109.92
REMARK 500 ASP A 308 -111.83 -133.12
REMARK 500 ASN A 314 70.20 -160.38
REMARK 500 LEU A 376 -119.34 37.18
REMARK 500 ASN A 385 71.02 42.56
REMARK 500 PRO A 442 47.08 -109.66
REMARK 500 ALA B 31 36.09 -88.00
REMARK 500 LEU B 45 -72.05 -88.84
REMARK 500 GLN B 178 55.96 -97.66
REMARK 500 ASP B 212 109.47 -170.82
REMARK 500 ASN B 250 94.86 -69.97
REMARK 500 LEU B 265 95.60 -161.09
REMARK 500 MET B 266 -10.49 80.67
REMARK 500 SER B 292 57.34 -112.90
REMARK 500 ASP B 308 -109.39 -129.44
REMARK 500 ASN B 314 69.54 -151.49
REMARK 500 LEU B 376 -118.90 35.67
REMARK 500 PRO B 442 50.15 -113.12
REMARK 500 ALA C 31 45.20 -83.87
REMARK 500 LEU C 45 -61.68 -108.67
REMARK 500 HIS C 81 33.48 -98.26
REMARK 500 THR C 112 -163.53 -127.65
REMARK 500 GLN C 178 56.83 -94.49
REMARK 500 ASP C 212 110.52 -165.38
REMARK 500 SER C 214 -5.30 -141.57
REMARK 500 MET C 266 -27.84 92.31
REMARK 500 PRO C 279 -8.66 -58.93
REMARK 500 ASP C 308 -106.62 -132.70
REMARK 500 ALA C 320 0.30 -60.68
REMARK 500 ARG C 321 80.09 -153.66
REMARK 500 LEU C 376 -118.52 40.87
REMARK 500 PRO C 442 51.03 -113.79
REMARK 500 PHE C 453 57.86 -90.09
REMARK 500 ALA D 31 41.13 -89.45
REMARK 500 LEU D 45 -73.23 -102.14
REMARK 500 THR D 112 -159.36 -132.24
REMARK 500 GLU D 210 49.03 -90.61
REMARK 500 ASP D 212 100.34 -165.44
REMARK 500 ASN D 250 89.22 -66.19
REMARK 500 MET D 266 -9.98 77.11
REMARK 500 ASP D 273 113.31 -161.54
REMARK 500 SER D 292 62.11 -105.08
REMARK 500 ASN D 304 -169.75 -111.07
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
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 ZN A 510 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 66 OE2
REMARK 620 2 HIS A 100 ND1 110.2
REMARK 620 3 GLU B 66 OE2 108.5 111.0
REMARK 620 4 HIS B 100 ND1 110.3 99.7 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 509 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 192 NE2
REMARK 620 2 HIS A 215 NE2 99.7
REMARK 620 3 HIS A 224 NE2 106.0 108.0
REMARK 620 4 HOH A 602 O 111.1 105.5 123.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 508 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 377 NE2
REMARK 620 2 HIS A 381 NE2 94.6
REMARK 620 3 HIS A 404 NE2 97.3 129.1
REMARK 620 4 HOH A 602 O 125.3 101.0 111.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 512 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 192 NE2
REMARK 620 2 HIS B 215 NE2 105.2
REMARK 620 3 HIS B 224 NE2 103.2 103.6
REMARK 620 4 HOH B 602 O 117.7 102.1 122.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 513 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 377 NE2
REMARK 620 2 HIS B 381 NE2 95.6
REMARK 620 3 HIS B 404 NE2 105.6 116.1
REMARK 620 4 HOH B 602 O 124.5 105.8 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 515 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 192 NE2
REMARK 620 2 HIS C 215 NE2 98.1
REMARK 620 3 HIS C 224 NE2 111.3 109.9
REMARK 620 4 HOH C 603 O 112.7 110.8 113.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 514 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 377 NE2
REMARK 620 2 HIS C 381 NE2 97.9
REMARK 620 3 HIS C 404 NE2 103.8 112.9
REMARK 620 4 HOH C 603 O 124.3 108.5 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 507 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 192 NE2
REMARK 620 2 HIS D 215 NE2 98.2
REMARK 620 3 HIS D 224 NE2 104.7 105.7
REMARK 620 4 HOH D 606 O 121.3 111.3 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 508 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 377 NE2
REMARK 620 2 HIS D 381 NE2 88.8
REMARK 620 3 HIS D 404 NE2 106.8 109.7
REMARK 620 4 HOH D 606 O 131.0 115.1 104.1
REMARK 620 N 1 2 3
DBREF 5M8R A 25 470 UNP P17643 TYRP1_HUMAN 25 470
DBREF 5M8R B 25 470 UNP P17643 TYRP1_HUMAN 25 470
DBREF 5M8R C 25 470 UNP P17643 TYRP1_HUMAN 25 470
DBREF 5M8R D 25 470 UNP P17643 TYRP1_HUMAN 25 470
SEQADV 5M8R PHE A 362 UNP P17643 TYR 362 ENGINEERED MUTATION
SEQADV 5M8R SER A 374 UNP P17643 ARG 374 ENGINEERED MUTATION
SEQADV 5M8R VAL A 391 UNP P17643 THR 391 ENGINEERED MUTATION
SEQADV 5M8R PHE B 362 UNP P17643 TYR 362 ENGINEERED MUTATION
SEQADV 5M8R SER B 374 UNP P17643 ARG 374 ENGINEERED MUTATION
SEQADV 5M8R VAL B 391 UNP P17643 THR 391 ENGINEERED MUTATION
SEQADV 5M8R PHE C 362 UNP P17643 TYR 362 ENGINEERED MUTATION
SEQADV 5M8R SER C 374 UNP P17643 ARG 374 ENGINEERED MUTATION
SEQADV 5M8R VAL C 391 UNP P17643 THR 391 ENGINEERED MUTATION
SEQADV 5M8R PHE D 362 UNP P17643 TYR 362 ENGINEERED MUTATION
SEQADV 5M8R SER D 374 UNP P17643 ARG 374 ENGINEERED MUTATION
SEQADV 5M8R VAL D 391 UNP P17643 THR 391 ENGINEERED MUTATION
SEQRES 1 A 446 GLN PHE PRO ARG GLN CYS ALA THR VAL GLU ALA LEU ARG
SEQRES 2 A 446 SER GLY MET CYS CYS PRO ASP LEU SER PRO VAL SER GLY
SEQRES 3 A 446 PRO GLY THR ASP ARG CYS GLY SER SER SER GLY ARG GLY
SEQRES 4 A 446 ARG CYS GLU ALA VAL THR ALA ASP SER ARG PRO HIS SER
SEQRES 5 A 446 PRO GLN TYR PRO HIS ASP GLY ARG ASP ASP ARG GLU VAL
SEQRES 6 A 446 TRP PRO LEU ARG PHE PHE ASN ARG THR CYS HIS CYS ASN
SEQRES 7 A 446 GLY ASN PHE SER GLY HIS ASN CYS GLY THR CYS ARG PRO
SEQRES 8 A 446 GLY TRP ARG GLY ALA ALA CYS ASP GLN ARG VAL LEU ILE
SEQRES 9 A 446 VAL ARG ARG ASN LEU LEU ASP LEU SER LYS GLU GLU LYS
SEQRES 10 A 446 ASN HIS PHE VAL ARG ALA LEU ASP MET ALA LYS ARG THR
SEQRES 11 A 446 THR HIS PRO LEU PHE VAL ILE ALA THR ARG ARG SER GLU
SEQRES 12 A 446 GLU ILE LEU GLY PRO ASP GLY ASN THR PRO GLN PHE GLU
SEQRES 13 A 446 ASN ILE SER ILE TYR ASN TYR PHE VAL TRP THR HIS TYR
SEQRES 14 A 446 TYR SER VAL LYS LYS THR PHE LEU GLY VAL GLY GLN GLU
SEQRES 15 A 446 SER PHE GLY GLU VAL ASP PHE SER HIS GLU GLY PRO ALA
SEQRES 16 A 446 PHE LEU THR TRP HIS ARG TYR HIS LEU LEU ARG LEU GLU
SEQRES 17 A 446 LYS ASP MET GLN GLU MET LEU GLN GLU PRO SER PHE SER
SEQRES 18 A 446 LEU PRO TYR TRP ASN PHE ALA THR GLY LYS ASN VAL CYS
SEQRES 19 A 446 ASP ILE CYS THR ASP ASP LEU MET GLY SER ARG SER ASN
SEQRES 20 A 446 PHE ASP SER THR LEU ILE SER PRO ASN SER VAL PHE SER
SEQRES 21 A 446 GLN TRP ARG VAL VAL CYS ASP SER LEU GLU ASP TYR ASP
SEQRES 22 A 446 THR LEU GLY THR LEU CYS ASN SER THR GLU ASP GLY PRO
SEQRES 23 A 446 ILE ARG ARG ASN PRO ALA GLY ASN VAL ALA ARG PRO MET
SEQRES 24 A 446 VAL GLN ARG LEU PRO GLU PRO GLN ASP VAL ALA GLN CYS
SEQRES 25 A 446 LEU GLU VAL GLY LEU PHE ASP THR PRO PRO PHE TYR SER
SEQRES 26 A 446 ASN SER THR ASN SER PHE ARG ASN THR VAL GLU GLY PHE
SEQRES 27 A 446 SER ASP PRO THR GLY LYS TYR ASP PRO ALA VAL SER SER
SEQRES 28 A 446 LEU HIS ASN LEU ALA HIS LEU PHE LEU ASN GLY THR GLY
SEQRES 29 A 446 GLY GLN VAL HIS LEU SER PRO ASN ASP PRO ILE PHE VAL
SEQRES 30 A 446 LEU LEU HIS THR PHE THR ASP ALA VAL PHE ASP GLU TRP
SEQRES 31 A 446 LEU ARG ARG TYR ASN ALA ASP ILE SER THR PHE PRO LEU
SEQRES 32 A 446 GLU ASN ALA PRO ILE GLY HIS ASN ARG GLN TYR ASN MET
SEQRES 33 A 446 VAL PRO PHE TRP PRO PRO VAL THR ASN THR GLU MET PHE
SEQRES 34 A 446 VAL THR ALA PRO ASP ASN LEU GLY TYR THR TYR GLU ILE
SEQRES 35 A 446 GLN TRP PRO SER
SEQRES 1 B 446 GLN PHE PRO ARG GLN CYS ALA THR VAL GLU ALA LEU ARG
SEQRES 2 B 446 SER GLY MET CYS CYS PRO ASP LEU SER PRO VAL SER GLY
SEQRES 3 B 446 PRO GLY THR ASP ARG CYS GLY SER SER SER GLY ARG GLY
SEQRES 4 B 446 ARG CYS GLU ALA VAL THR ALA ASP SER ARG PRO HIS SER
SEQRES 5 B 446 PRO GLN TYR PRO HIS ASP GLY ARG ASP ASP ARG GLU VAL
SEQRES 6 B 446 TRP PRO LEU ARG PHE PHE ASN ARG THR CYS HIS CYS ASN
SEQRES 7 B 446 GLY ASN PHE SER GLY HIS ASN CYS GLY THR CYS ARG PRO
SEQRES 8 B 446 GLY TRP ARG GLY ALA ALA CYS ASP GLN ARG VAL LEU ILE
SEQRES 9 B 446 VAL ARG ARG ASN LEU LEU ASP LEU SER LYS GLU GLU LYS
SEQRES 10 B 446 ASN HIS PHE VAL ARG ALA LEU ASP MET ALA LYS ARG THR
SEQRES 11 B 446 THR HIS PRO LEU PHE VAL ILE ALA THR ARG ARG SER GLU
SEQRES 12 B 446 GLU ILE LEU GLY PRO ASP GLY ASN THR PRO GLN PHE GLU
SEQRES 13 B 446 ASN ILE SER ILE TYR ASN TYR PHE VAL TRP THR HIS TYR
SEQRES 14 B 446 TYR SER VAL LYS LYS THR PHE LEU GLY VAL GLY GLN GLU
SEQRES 15 B 446 SER PHE GLY GLU VAL ASP PHE SER HIS GLU GLY PRO ALA
SEQRES 16 B 446 PHE LEU THR TRP HIS ARG TYR HIS LEU LEU ARG LEU GLU
SEQRES 17 B 446 LYS ASP MET GLN GLU MET LEU GLN GLU PRO SER PHE SER
SEQRES 18 B 446 LEU PRO TYR TRP ASN PHE ALA THR GLY LYS ASN VAL CYS
SEQRES 19 B 446 ASP ILE CYS THR ASP ASP LEU MET GLY SER ARG SER ASN
SEQRES 20 B 446 PHE ASP SER THR LEU ILE SER PRO ASN SER VAL PHE SER
SEQRES 21 B 446 GLN TRP ARG VAL VAL CYS ASP SER LEU GLU ASP TYR ASP
SEQRES 22 B 446 THR LEU GLY THR LEU CYS ASN SER THR GLU ASP GLY PRO
SEQRES 23 B 446 ILE ARG ARG ASN PRO ALA GLY ASN VAL ALA ARG PRO MET
SEQRES 24 B 446 VAL GLN ARG LEU PRO GLU PRO GLN ASP VAL ALA GLN CYS
SEQRES 25 B 446 LEU GLU VAL GLY LEU PHE ASP THR PRO PRO PHE TYR SER
SEQRES 26 B 446 ASN SER THR ASN SER PHE ARG ASN THR VAL GLU GLY PHE
SEQRES 27 B 446 SER ASP PRO THR GLY LYS TYR ASP PRO ALA VAL SER SER
SEQRES 28 B 446 LEU HIS ASN LEU ALA HIS LEU PHE LEU ASN GLY THR GLY
SEQRES 29 B 446 GLY GLN VAL HIS LEU SER PRO ASN ASP PRO ILE PHE VAL
SEQRES 30 B 446 LEU LEU HIS THR PHE THR ASP ALA VAL PHE ASP GLU TRP
SEQRES 31 B 446 LEU ARG ARG TYR ASN ALA ASP ILE SER THR PHE PRO LEU
SEQRES 32 B 446 GLU ASN ALA PRO ILE GLY HIS ASN ARG GLN TYR ASN MET
SEQRES 33 B 446 VAL PRO PHE TRP PRO PRO VAL THR ASN THR GLU MET PHE
SEQRES 34 B 446 VAL THR ALA PRO ASP ASN LEU GLY TYR THR TYR GLU ILE
SEQRES 35 B 446 GLN TRP PRO SER
SEQRES 1 C 446 GLN PHE PRO ARG GLN CYS ALA THR VAL GLU ALA LEU ARG
SEQRES 2 C 446 SER GLY MET CYS CYS PRO ASP LEU SER PRO VAL SER GLY
SEQRES 3 C 446 PRO GLY THR ASP ARG CYS GLY SER SER SER GLY ARG GLY
SEQRES 4 C 446 ARG CYS GLU ALA VAL THR ALA ASP SER ARG PRO HIS SER
SEQRES 5 C 446 PRO GLN TYR PRO HIS ASP GLY ARG ASP ASP ARG GLU VAL
SEQRES 6 C 446 TRP PRO LEU ARG PHE PHE ASN ARG THR CYS HIS CYS ASN
SEQRES 7 C 446 GLY ASN PHE SER GLY HIS ASN CYS GLY THR CYS ARG PRO
SEQRES 8 C 446 GLY TRP ARG GLY ALA ALA CYS ASP GLN ARG VAL LEU ILE
SEQRES 9 C 446 VAL ARG ARG ASN LEU LEU ASP LEU SER LYS GLU GLU LYS
SEQRES 10 C 446 ASN HIS PHE VAL ARG ALA LEU ASP MET ALA LYS ARG THR
SEQRES 11 C 446 THR HIS PRO LEU PHE VAL ILE ALA THR ARG ARG SER GLU
SEQRES 12 C 446 GLU ILE LEU GLY PRO ASP GLY ASN THR PRO GLN PHE GLU
SEQRES 13 C 446 ASN ILE SER ILE TYR ASN TYR PHE VAL TRP THR HIS TYR
SEQRES 14 C 446 TYR SER VAL LYS LYS THR PHE LEU GLY VAL GLY GLN GLU
SEQRES 15 C 446 SER PHE GLY GLU VAL ASP PHE SER HIS GLU GLY PRO ALA
SEQRES 16 C 446 PHE LEU THR TRP HIS ARG TYR HIS LEU LEU ARG LEU GLU
SEQRES 17 C 446 LYS ASP MET GLN GLU MET LEU GLN GLU PRO SER PHE SER
SEQRES 18 C 446 LEU PRO TYR TRP ASN PHE ALA THR GLY LYS ASN VAL CYS
SEQRES 19 C 446 ASP ILE CYS THR ASP ASP LEU MET GLY SER ARG SER ASN
SEQRES 20 C 446 PHE ASP SER THR LEU ILE SER PRO ASN SER VAL PHE SER
SEQRES 21 C 446 GLN TRP ARG VAL VAL CYS ASP SER LEU GLU ASP TYR ASP
SEQRES 22 C 446 THR LEU GLY THR LEU CYS ASN SER THR GLU ASP GLY PRO
SEQRES 23 C 446 ILE ARG ARG ASN PRO ALA GLY ASN VAL ALA ARG PRO MET
SEQRES 24 C 446 VAL GLN ARG LEU PRO GLU PRO GLN ASP VAL ALA GLN CYS
SEQRES 25 C 446 LEU GLU VAL GLY LEU PHE ASP THR PRO PRO PHE TYR SER
SEQRES 26 C 446 ASN SER THR ASN SER PHE ARG ASN THR VAL GLU GLY PHE
SEQRES 27 C 446 SER ASP PRO THR GLY LYS TYR ASP PRO ALA VAL SER SER
SEQRES 28 C 446 LEU HIS ASN LEU ALA HIS LEU PHE LEU ASN GLY THR GLY
SEQRES 29 C 446 GLY GLN VAL HIS LEU SER PRO ASN ASP PRO ILE PHE VAL
SEQRES 30 C 446 LEU LEU HIS THR PHE THR ASP ALA VAL PHE ASP GLU TRP
SEQRES 31 C 446 LEU ARG ARG TYR ASN ALA ASP ILE SER THR PHE PRO LEU
SEQRES 32 C 446 GLU ASN ALA PRO ILE GLY HIS ASN ARG GLN TYR ASN MET
SEQRES 33 C 446 VAL PRO PHE TRP PRO PRO VAL THR ASN THR GLU MET PHE
SEQRES 34 C 446 VAL THR ALA PRO ASP ASN LEU GLY TYR THR TYR GLU ILE
SEQRES 35 C 446 GLN TRP PRO SER
SEQRES 1 D 446 GLN PHE PRO ARG GLN CYS ALA THR VAL GLU ALA LEU ARG
SEQRES 2 D 446 SER GLY MET CYS CYS PRO ASP LEU SER PRO VAL SER GLY
SEQRES 3 D 446 PRO GLY THR ASP ARG CYS GLY SER SER SER GLY ARG GLY
SEQRES 4 D 446 ARG CYS GLU ALA VAL THR ALA ASP SER ARG PRO HIS SER
SEQRES 5 D 446 PRO GLN TYR PRO HIS ASP GLY ARG ASP ASP ARG GLU VAL
SEQRES 6 D 446 TRP PRO LEU ARG PHE PHE ASN ARG THR CYS HIS CYS ASN
SEQRES 7 D 446 GLY ASN PHE SER GLY HIS ASN CYS GLY THR CYS ARG PRO
SEQRES 8 D 446 GLY TRP ARG GLY ALA ALA CYS ASP GLN ARG VAL LEU ILE
SEQRES 9 D 446 VAL ARG ARG ASN LEU LEU ASP LEU SER LYS GLU GLU LYS
SEQRES 10 D 446 ASN HIS PHE VAL ARG ALA LEU ASP MET ALA LYS ARG THR
SEQRES 11 D 446 THR HIS PRO LEU PHE VAL ILE ALA THR ARG ARG SER GLU
SEQRES 12 D 446 GLU ILE LEU GLY PRO ASP GLY ASN THR PRO GLN PHE GLU
SEQRES 13 D 446 ASN ILE SER ILE TYR ASN TYR PHE VAL TRP THR HIS TYR
SEQRES 14 D 446 TYR SER VAL LYS LYS THR PHE LEU GLY VAL GLY GLN GLU
SEQRES 15 D 446 SER PHE GLY GLU VAL ASP PHE SER HIS GLU GLY PRO ALA
SEQRES 16 D 446 PHE LEU THR TRP HIS ARG TYR HIS LEU LEU ARG LEU GLU
SEQRES 17 D 446 LYS ASP MET GLN GLU MET LEU GLN GLU PRO SER PHE SER
SEQRES 18 D 446 LEU PRO TYR TRP ASN PHE ALA THR GLY LYS ASN VAL CYS
SEQRES 19 D 446 ASP ILE CYS THR ASP ASP LEU MET GLY SER ARG SER ASN
SEQRES 20 D 446 PHE ASP SER THR LEU ILE SER PRO ASN SER VAL PHE SER
SEQRES 21 D 446 GLN TRP ARG VAL VAL CYS ASP SER LEU GLU ASP TYR ASP
SEQRES 22 D 446 THR LEU GLY THR LEU CYS ASN SER THR GLU ASP GLY PRO
SEQRES 23 D 446 ILE ARG ARG ASN PRO ALA GLY ASN VAL ALA ARG PRO MET
SEQRES 24 D 446 VAL GLN ARG LEU PRO GLU PRO GLN ASP VAL ALA GLN CYS
SEQRES 25 D 446 LEU GLU VAL GLY LEU PHE ASP THR PRO PRO PHE TYR SER
SEQRES 26 D 446 ASN SER THR ASN SER PHE ARG ASN THR VAL GLU GLY PHE
SEQRES 27 D 446 SER ASP PRO THR GLY LYS TYR ASP PRO ALA VAL SER SER
SEQRES 28 D 446 LEU HIS ASN LEU ALA HIS LEU PHE LEU ASN GLY THR GLY
SEQRES 29 D 446 GLY GLN VAL HIS LEU SER PRO ASN ASP PRO ILE PHE VAL
SEQRES 30 D 446 LEU LEU HIS THR PHE THR ASP ALA VAL PHE ASP GLU TRP
SEQRES 31 D 446 LEU ARG ARG TYR ASN ALA ASP ILE SER THR PHE PRO LEU
SEQRES 32 D 446 GLU ASN ALA PRO ILE GLY HIS ASN ARG GLN TYR ASN MET
SEQRES 33 D 446 VAL PRO PHE TRP PRO PRO VAL THR ASN THR GLU MET PHE
SEQRES 34 D 446 VAL THR ALA PRO ASP ASN LEU GLY TYR THR TYR GLU ILE
SEQRES 35 D 446 GLN TRP PRO SER
HET NAG E 1 14
HET NAG E 2 14
HET FUC E 3 10
HET NAG F 1 14
HET NAG F 2 14
HET FUC F 3 10
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET MAN H 3 11
HET MAN H 4 11
HET NAG I 1 14
HET NAG I 2 14
HET FUC I 3 10
HET NAG J 1 14
HET NAG J 2 14
HET FUC J 3 10
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET MAN L 3 11
HET MAN L 4 11
HET NAG M 1 14
HET FUC M 2 10
HET NAG A 504 14
HET NAG A 505 14
HET NAG A 506 14
HET NAG A 507 14
HET ZN A 508 1
HET ZN A 509 1
HET ZN A 510 1
HET MMS A 511 14
HET NAG B 504 14
HET NAG B 511 14
HET ZN B 512 1
HET ZN B 513 1
HET MMS B 514 14
HET NAG C 513 14
HET ZN C 514 1
HET ZN C 515 1
HET MMS C 516 14
HET NAG D 503 14
HET NAG D 504 14
HET NAG D 505 14
HET NAG D 506 14
HET ZN D 507 1
HET ZN D 508 1
HET MMS D 509 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM MMS MIMOSINE
HETSYN MMS 3-HYDROXY-4-OXO-1(4H)-PYRIDINEALANINE
FORMUL 5 NAG 28(C8 H15 N O6)
FORMUL 5 FUC 5(C6 H12 O5)
FORMUL 8 MAN 4(C6 H12 O6)
FORMUL 18 ZN 9(ZN 2+)
FORMUL 21 MMS 4(C8 H10 N2 O4)
FORMUL 38 HOH *39(H2 O)
HELIX 1 AA1 THR A 32 GLY A 39 1 8
HELIX 2 AA2 ASP A 54 SER A 58 5 5
HELIX 3 AA3 LEU A 133 LEU A 136 5 4
HELIX 4 AA4 SER A 137 THR A 154 1 18
HELIX 5 AA5 ARG A 165 ILE A 169 5 5
HELIX 6 AA6 SER A 183 LYS A 197 1 15
HELIX 7 AA7 ALA A 219 GLN A 240 1 22
HELIX 8 AA8 SER A 281 TRP A 286 5 6
HELIX 9 AA9 SER A 292 GLY A 300 1 9
HELIX 10 AB1 ARG A 321 ARG A 326 5 6
HELIX 11 AB2 GLU A 329 LEU A 337 1 9
HELIX 12 AB3 SER A 354 GLY A 361 1 8
HELIX 13 AB4 SER A 375 LEU A 384 1 10
HELIX 14 AB5 ASN A 385 GLN A 390 5 6
HELIX 15 AB6 LEU A 393 ASP A 397 5 5
HELIX 16 AB7 PRO A 398 TYR A 418 1 21
HELIX 17 AB8 ASP A 421 PHE A 425 5 5
HELIX 18 AB9 THR A 448 PHE A 453 1 6
HELIX 19 AC1 THR A 455 LEU A 460 1 6
HELIX 20 AC2 GLN B 29 ALA B 31 5 3
HELIX 21 AC3 THR B 32 GLY B 39 1 8
HELIX 22 AC4 ASP B 54 SER B 58 5 5
HELIX 23 AC5 ASN B 132 LEU B 136 5 5
HELIX 24 AC6 SER B 137 THR B 154 1 18
HELIX 25 AC7 ARG B 165 ILE B 169 5 5
HELIX 26 AC8 SER B 183 LYS B 197 1 15
HELIX 27 AC9 ALA B 219 GLN B 240 1 22
HELIX 28 AD1 SER B 281 TRP B 286 5 6
HELIX 29 AD2 SER B 292 GLY B 300 1 9
HELIX 30 AD3 ARG B 321 GLN B 325 5 5
HELIX 31 AD4 GLU B 329 LEU B 337 1 9
HELIX 32 AD5 SER B 354 GLY B 361 1 8
HELIX 33 AD6 SER B 375 LEU B 384 1 10
HELIX 34 AD7 ASN B 385 GLN B 390 5 6
HELIX 35 AD8 LEU B 393 ASP B 397 5 5
HELIX 36 AD9 PRO B 398 TYR B 418 1 21
HELIX 37 AE1 THR B 448 PHE B 453 1 6
HELIX 38 AE2 THR B 455 LEU B 460 1 6
HELIX 39 AE3 GLN C 29 ALA C 31 5 3
HELIX 40 AE4 THR C 32 GLY C 39 1 8
HELIX 41 AE5 ASP C 54 SER C 58 5 5
HELIX 42 AE6 ASN C 132 LEU C 136 5 5
HELIX 43 AE7 SER C 137 THR C 154 1 18
HELIX 44 AE8 ARG C 165 ILE C 169 5 5
HELIX 45 AE9 SER C 183 LYS C 197 1 15
HELIX 46 AF1 ALA C 219 GLN C 240 1 22
HELIX 47 AF2 SER C 281 TRP C 286 5 6
HELIX 48 AF3 SER C 292 GLY C 300 1 9
HELIX 49 AF4 ARG C 321 GLN C 325 5 5
HELIX 50 AF5 GLU C 329 LEU C 337 1 9
HELIX 51 AF6 SER C 354 GLY C 361 1 8
HELIX 52 AF7 SER C 375 LEU C 384 1 10
HELIX 53 AF8 ASN C 385 GLN C 390 5 6
HELIX 54 AF9 LEU C 393 ASP C 397 5 5
HELIX 55 AG1 PRO C 398 TYR C 418 1 21
HELIX 56 AG2 THR C 448 PHE C 453 1 6
HELIX 57 AG3 THR C 455 GLY C 461 1 7
HELIX 58 AG4 GLN D 29 ALA D 31 5 3
HELIX 59 AG5 THR D 32 GLY D 39 1 8
HELIX 60 AG6 ASP D 54 SER D 58 5 5
HELIX 61 AG7 LEU D 133 LEU D 136 5 4
HELIX 62 AG8 SER D 137 THR D 154 1 18
HELIX 63 AG9 ARG D 165 ILE D 169 5 5
HELIX 64 AH1 SER D 183 LYS D 197 1 15
HELIX 65 AH2 ALA D 219 GLN D 240 1 22
HELIX 66 AH3 SER D 281 TRP D 286 5 6
HELIX 67 AH4 SER D 292 GLY D 300 1 9
HELIX 68 AH5 ARG D 321 ARG D 326 5 6
HELIX 69 AH6 GLU D 329 LEU D 337 1 9
HELIX 70 AH7 SER D 354 GLY D 361 1 8
HELIX 71 AH8 SER D 375 LEU D 384 1 10
HELIX 72 AH9 ASN D 385 GLN D 390 5 6
HELIX 73 AI1 LEU D 393 ASP D 397 5 5
HELIX 74 AI2 PRO D 398 TYR D 418 1 21
HELIX 75 AI3 ASN D 449 PHE D 453 5 5
HELIX 76 AI4 THR D 455 LEU D 460 1 6
SHEET 1 AA1 3 PHE A 26 PRO A 27 0
SHEET 2 AA1 3 PHE A 159 ALA A 162 -1 O VAL A 160 N PHE A 26
SHEET 3 AA1 3 PHE A 179 GLU A 180 -1 O GLU A 180 N ILE A 161
SHEET 1 AA2 3 MET A 40 CYS A 41 0
SHEET 2 AA2 3 ARG A 97 CYS A 101 1 O ARG A 97 N CYS A 41
SHEET 3 AA2 3 GLY A 63 ALA A 67 -1 N GLU A 66 O THR A 98
SHEET 1 AA3 2 PHE A 105 SER A 106 0
SHEET 2 AA3 2 THR A 112 CYS A 113 -1 O THR A 112 N SER A 106
SHEET 1 AA4 2 TRP A 117 ARG A 118 0
SHEET 2 AA4 2 GLN A 124 ARG A 125 -1 O GLN A 124 N ARG A 118
SHEET 1 AA5 2 ILE A 128 ARG A 131 0
SHEET 2 AA5 2 TYR A 462 GLU A 465 1 O THR A 463 N ARG A 130
SHEET 1 AA6 3 PHE B 26 PRO B 27 0
SHEET 2 AA6 3 PHE B 159 ALA B 162 -1 O VAL B 160 N PHE B 26
SHEET 3 AA6 3 PHE B 179 GLU B 180 -1 O GLU B 180 N ILE B 161
SHEET 1 AA7 3 MET B 40 CYS B 41 0
SHEET 2 AA7 3 ARG B 97 CYS B 101 1 O ARG B 97 N CYS B 41
SHEET 3 AA7 3 GLY B 63 ALA B 67 -1 N GLU B 66 O THR B 98
SHEET 1 AA8 2 PHE B 105 SER B 106 0
SHEET 2 AA8 2 THR B 112 CYS B 113 -1 O THR B 112 N SER B 106
SHEET 1 AA9 2 TRP B 117 ARG B 118 0
SHEET 2 AA9 2 GLN B 124 ARG B 125 -1 O GLN B 124 N ARG B 118
SHEET 1 AB1 2 ILE B 128 ARG B 130 0
SHEET 2 AB1 2 TYR B 462 TYR B 464 1 O THR B 463 N ARG B 130
SHEET 1 AB2 3 PHE C 26 PRO C 27 0
SHEET 2 AB2 3 PHE C 159 ALA C 162 -1 O VAL C 160 N PHE C 26
SHEET 3 AB2 3 PHE C 179 GLU C 180 -1 O GLU C 180 N ILE C 161
SHEET 1 AB3 3 MET C 40 CYS C 41 0
SHEET 2 AB3 3 ARG C 97 CYS C 101 1 O ARG C 97 N CYS C 41
SHEET 3 AB3 3 GLY C 63 ALA C 67 -1 N GLU C 66 O THR C 98
SHEET 1 AB4 2 PHE C 105 SER C 106 0
SHEET 2 AB4 2 THR C 112 CYS C 113 -1 O THR C 112 N SER C 106
SHEET 1 AB5 2 TRP C 117 ARG C 118 0
SHEET 2 AB5 2 GLN C 124 ARG C 125 -1 O GLN C 124 N ARG C 118
SHEET 1 AB6 2 ILE C 128 ARG C 130 0
SHEET 2 AB6 2 TYR C 462 TYR C 464 1 O THR C 463 N ARG C 130
SHEET 1 AB7 3 PHE D 26 PRO D 27 0
SHEET 2 AB7 3 PHE D 159 ALA D 162 -1 O VAL D 160 N PHE D 26
SHEET 3 AB7 3 PHE D 179 GLU D 180 -1 O GLU D 180 N ILE D 161
SHEET 1 AB8 2 GLY D 63 ALA D 67 0
SHEET 2 AB8 2 ARG D 97 CYS D 101 -1 O HIS D 100 N ARG D 64
SHEET 1 AB9 2 PHE D 105 SER D 106 0
SHEET 2 AB9 2 THR D 112 CYS D 113 -1 O THR D 112 N SER D 106
SHEET 1 AC1 2 TRP D 117 ARG D 118 0
SHEET 2 AC1 2 GLN D 124 ARG D 125 -1 O GLN D 124 N ARG D 118
SHEET 1 AC2 2 ILE D 128 ARG D 131 0
SHEET 2 AC2 2 TYR D 462 GLU D 465 1 O THR D 463 N ARG D 130
SSBOND 1 CYS A 30 CYS A 41 1555 1555 2.07
SSBOND 2 CYS A 42 CYS A 65 1555 1555 2.07
SSBOND 3 CYS A 56 CYS A 99 1555 1555 2.05
SSBOND 4 CYS A 101 CYS A 110 1555 1555 2.04
SSBOND 5 CYS A 113 CYS A 122 1555 1555 2.05
SSBOND 6 CYS A 258 CYS A 261 1555 1555 2.09
SSBOND 7 CYS A 290 CYS A 303 1555 1555 2.04
SSBOND 8 CYS B 30 CYS B 41 1555 1555 2.07
SSBOND 9 CYS B 42 CYS B 65 1555 1555 2.08
SSBOND 10 CYS B 56 CYS B 99 1555 1555 2.05
SSBOND 11 CYS B 101 CYS B 110 1555 1555 2.04
SSBOND 12 CYS B 113 CYS B 122 1555 1555 2.05
SSBOND 13 CYS B 258 CYS B 261 1555 1555 2.08
SSBOND 14 CYS B 290 CYS B 303 1555 1555 2.06
SSBOND 15 CYS C 30 CYS C 41 1555 1555 2.07
SSBOND 16 CYS C 42 CYS C 65 1555 1555 2.06
SSBOND 17 CYS C 56 CYS C 99 1555 1555 2.06
SSBOND 18 CYS C 101 CYS C 110 1555 1555 2.08
SSBOND 19 CYS C 113 CYS C 122 1555 1555 2.06
SSBOND 20 CYS C 258 CYS C 261 1555 1555 2.11
SSBOND 21 CYS C 290 CYS C 303 1555 1555 2.04
SSBOND 22 CYS D 30 CYS D 41 1555 1555 2.05
SSBOND 23 CYS D 42 CYS D 65 1555 1555 2.05
SSBOND 24 CYS D 56 CYS D 99 1555 1555 2.05
SSBOND 25 CYS D 101 CYS D 110 1555 1555 2.07
SSBOND 26 CYS D 113 CYS D 122 1555 1555 2.06
SSBOND 27 CYS D 258 CYS D 261 1555 1555 2.08
SSBOND 28 CYS D 290 CYS D 303 1555 1555 2.06
LINK ND2 ASN A 96 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 181 C1 NAG A 504 1555 1555 1.49
LINK ND2 ASN A 304 C1 NAG A 505 1555 1555 1.45
LINK ND2 ASN A 350 C1 NAG A 506 1555 1555 1.45
LINK ND2 ASN A 385 C1 NAG A 507 1555 1555 1.46
LINK ND2 ASN B 96 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN B 181 C1 NAG B 504 1555 1555 1.42
LINK ND2 ASN B 304 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN B 350 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 385 C1 NAG B 511 1555 1555 1.46
LINK ND2 ASN C 96 C1 NAG I 1 1555 1555 1.45
LINK ND2 ASN C 181 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN C 304 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN C 350 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN C 385 C1 NAG C 513 1555 1555 1.47
LINK ND2 ASN D 96 C1 NAG M 1 1555 1555 1.47
LINK ND2 ASN D 181 C1 NAG D 503 1555 1555 1.43
LINK ND2 ASN D 304 C1 NAG D 504 1555 1555 1.44
LINK ND2 ASN D 350 C1 NAG D 505 1555 1555 1.45
LINK ND2 ASN D 385 C1 NAG D 506 1555 1555 1.46
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.46
LINK O6 NAG E 1 C1 FUC E 3 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.47
LINK O6 NAG F 1 C1 FUC F 3 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.43
LINK O4 NAG H 2 C1 MAN H 3 1555 1555 1.45
LINK O3 MAN H 3 C1 MAN H 4 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O6 NAG I 1 C1 FUC I 3 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK O6 NAG J 1 C1 FUC J 3 1555 1555 1.46
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.43
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG L 2 C1 MAN L 3 1555 1555 1.44
LINK O3 MAN L 3 C1 MAN L 4 1555 1555 1.44
LINK O6 NAG M 1 C1 FUC M 2 1555 1555 1.44
LINK OE2 GLU A 66 ZN ZN A 510 1555 1555 2.23
LINK ND1 HIS A 100 ZN ZN A 510 1555 1555 2.15
LINK NE2 HIS A 192 ZN ZN A 509 1555 1555 2.00
LINK NE2 HIS A 215 ZN ZN A 509 1555 1555 2.05
LINK NE2 HIS A 224 ZN ZN A 509 1555 1555 2.01
LINK NE2 HIS A 377 ZN ZN A 508 1555 1555 2.09
LINK NE2 HIS A 381 ZN ZN A 508 1555 1555 2.10
LINK NE2 HIS A 404 ZN ZN A 508 1555 1555 2.15
LINK ZN ZN A 508 O HOH A 602 1555 1555 2.01
LINK ZN ZN A 509 O HOH A 602 1555 1555 2.08
LINK ZN ZN A 510 OE2 GLU B 66 1555 1555 1.89
LINK ZN ZN A 510 ND1 HIS B 100 1555 1555 2.08
LINK NE2 HIS B 192 ZN ZN B 512 1555 1555 1.99
LINK NE2 HIS B 215 ZN ZN B 512 1555 1555 2.11
LINK NE2 HIS B 224 ZN ZN B 512 1555 1555 2.05
LINK NE2 HIS B 377 ZN ZN B 513 1555 1555 2.03
LINK NE2 HIS B 381 ZN ZN B 513 1555 1555 2.07
LINK NE2 HIS B 404 ZN ZN B 513 1555 1555 2.05
LINK ZN ZN B 512 O HOH B 602 1555 1555 1.96
LINK ZN ZN B 513 O HOH B 602 1555 1555 2.01
LINK NE2 HIS C 192 ZN ZN C 515 1555 1555 2.06
LINK NE2 HIS C 215 ZN ZN C 515 1555 1555 2.09
LINK NE2 HIS C 224 ZN ZN C 515 1555 1555 2.02
LINK NE2 HIS C 377 ZN ZN C 514 1555 1555 2.08
LINK NE2 HIS C 381 ZN ZN C 514 1555 1555 2.10
LINK NE2 HIS C 404 ZN ZN C 514 1555 1555 2.01
LINK ZN ZN C 514 O HOH C 603 1555 1555 1.90
LINK ZN ZN C 515 O HOH C 603 1555 1555 2.01
LINK NE2 HIS D 192 ZN ZN D 507 1555 1555 1.94
LINK NE2 HIS D 215 ZN ZN D 507 1555 1555 2.10
LINK NE2 HIS D 224 ZN ZN D 507 1555 1555 2.09
LINK NE2 HIS D 377 ZN ZN D 508 1555 1555 2.00
LINK NE2 HIS D 381 ZN ZN D 508 1555 1555 2.10
LINK NE2 HIS D 404 ZN ZN D 508 1555 1555 2.01
LINK ZN ZN D 507 O HOH D 606 1555 1555 1.97
LINK ZN ZN D 508 O HOH D 606 1555 1555 1.80
CISPEP 1 TRP A 90 PRO A 91 0 1.75
CISPEP 2 PRO A 345 PRO A 346 0 -2.01
CISPEP 3 VAL A 441 PRO A 442 0 -2.17
CISPEP 4 TRP A 444 PRO A 445 0 -2.15
CISPEP 5 TRP B 90 PRO B 91 0 2.64
CISPEP 6 PRO B 345 PRO B 346 0 5.50
CISPEP 7 VAL B 441 PRO B 442 0 4.13
CISPEP 8 TRP B 444 PRO B 445 0 -6.08
CISPEP 9 TRP C 90 PRO C 91 0 2.70
CISPEP 10 PRO C 345 PRO C 346 0 3.01
CISPEP 11 VAL C 441 PRO C 442 0 0.06
CISPEP 12 TRP C 444 PRO C 445 0 -7.98
CISPEP 13 TRP D 90 PRO D 91 0 2.88
CISPEP 14 PRO D 345 PRO D 346 0 3.50
CISPEP 15 VAL D 441 PRO D 442 0 0.90
CISPEP 16 TRP D 444 PRO D 445 0 -1.47
CRYST1 89.353 139.727 190.951 90.00 90.00 90.00 P 21 21 21 16
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 0.011192 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007157 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005237 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
