HEADER LIGASE 08-JUL-16 5GL7
TITLE CRYSTAL STRUCTURE OF A TRUNCATED HUMAN CYTOSOLIC METHIONYL-TRNA
TITLE 2 SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONINE--TRNA LIGASE, CYTOPLASMIC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 221-834;
COMPND 5 SYNONYM: METHIONYL-TRNA SYNTHETASE,METRS;
COMPND 6 EC: 6.1.1.10;
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: MARS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS MSC, METRS, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.Y.CHO,H.J.LEE,B.S.KANG
REVDAT 2 20-MAR-24 5GL7 1 REMARK
REVDAT 1 12-JUL-17 5GL7 0
JRNL AUTH H.Y.CHO,H.J.LEE,B.S.KANG
JRNL TITL CRYSTAL STRUCTURE OF A TRUNCATED HUMAN CYTOSOLIC
JRNL TITL 2 METHIONYL-TRNA SYNTHETASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1690
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 48889
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 37.2900 - 4.8492 0.98 3563 153 0.1597 0.1615
REMARK 3 2 4.8492 - 3.8502 1.00 3460 147 0.1460 0.1891
REMARK 3 3 3.8502 - 3.3639 1.00 3456 147 0.1744 0.2002
REMARK 3 4 3.3639 - 3.0565 1.00 3403 145 0.1983 0.2343
REMARK 3 5 3.0565 - 2.8375 0.99 3369 144 0.2140 0.2510
REMARK 3 6 2.8375 - 2.6702 0.98 3349 142 0.2211 0.2798
REMARK 3 7 2.6702 - 2.5365 0.98 3343 144 0.2298 0.2588
REMARK 3 8 2.5365 - 2.4261 0.98 3303 140 0.2284 0.3090
REMARK 3 9 2.4261 - 2.3327 0.98 3324 142 0.2364 0.2603
REMARK 3 10 2.3327 - 2.2523 0.98 3291 140 0.2414 0.2619
REMARK 3 11 2.2523 - 2.1818 0.98 3314 142 0.2414 0.2854
REMARK 3 12 2.1818 - 2.1195 0.98 3296 141 0.2604 0.2925
REMARK 3 13 2.1195 - 2.0637 0.98 3302 140 0.2698 0.3110
REMARK 3 14 2.0637 - 2.0133 0.93 3116 133 0.2935 0.3135
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 4910
REMARK 3 ANGLE : 0.698 6676
REMARK 3 CHIRALITY : 0.028 732
REMARK 3 PLANARITY : 0.003 865
REMARK 3 DIHEDRAL : 13.850 1806
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 5GL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1300000956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9756
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48954
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.013
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.1000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.9_1690
REMARK 200 STARTING MODEL: ZINC PHAZING MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS PH 7.5, 200MM MAGNESIUM
REMARK 280 CHLORIDE, 5MM DTT, 21% PEG 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
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 32.51750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.04200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.51500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.04200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.51750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.51500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 219
REMARK 465 SER A 220
REMARK 465 GLU A 221
REMARK 465 GLU A 222
REMARK 465 GLU A 223
REMARK 465 GLU A 224
REMARK 465 LEU A 225
REMARK 465 LYS A 823
REMARK 465 THR A 824
REMARK 465 SER A 825
REMARK 465 PRO A 826
REMARK 465 LYS A 827
REMARK 465 PRO A 828
REMARK 465 ALA A 829
REMARK 465 VAL A 830
REMARK 465 VAL A 831
REMARK 465 GLU A 832
REMARK 465 THR A 833
REMARK 465 VAL A 834
REMARK 465 LEU A 835
REMARK 465 GLU A 836
REMARK 465 HIS A 837
REMARK 465 HIS A 838
REMARK 465 HIS A 839
REMARK 465 HIS A 840
REMARK 465 HIS A 841
REMARK 465 HIS A 842
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 LEU A 250 CG CD1 CD2
REMARK 470 GLN A 253 CG CD OE1 NE2
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 OD1 ASP A 555 OH TYR A 586 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1087 O HOH A 1149 1545 2.19
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 PRO A 249 98.63 -59.06
REMARK 500 CYS A 287 -83.41 -127.78
REMARK 500 ASN A 542 63.05 -153.78
REMARK 500 LEU A 562 -61.80 -120.48
REMARK 500 GLU A 585 -166.34 -78.64
REMARK 500 GLU A 590 -116.72 52.31
REMARK 500 ASN A 649 -80.65 -125.05
REMARK 500 LEU A 789 79.82 -116.81
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 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 389 SG
REMARK 620 2 CYS A 392 SG 104.2
REMARK 620 3 CYS A 435 SG 120.6 119.8
REMARK 620 4 CYS A 438 SG 90.6 105.0 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 405 SG
REMARK 620 2 CYS A 408 SG 111.2
REMARK 620 3 CYS A 418 SG 104.1 107.6
REMARK 620 4 CYS A 421 SG 109.9 115.1 108.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 904
DBREF 5GL7 A 221 834 UNP P56192 SYMC_HUMAN 221 834
SEQADV 5GL7 MET A 219 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 SER A 220 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 LEU A 835 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 GLU A 836 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 HIS A 837 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 HIS A 838 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 HIS A 839 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 HIS A 840 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 HIS A 841 UNP P56192 EXPRESSION TAG
SEQADV 5GL7 HIS A 842 UNP P56192 EXPRESSION TAG
SEQRES 1 A 624 MET SER GLU GLU GLU GLU LEU ALA THR LEU SER GLU GLU
SEQRES 2 A 624 GLU ILE ALA MET ALA VAL THR ALA TRP GLU LYS GLY LEU
SEQRES 3 A 624 GLU SER LEU PRO PRO LEU ARG PRO GLN GLN ASN PRO VAL
SEQRES 4 A 624 LEU PRO VAL ALA GLY GLU ARG ASN VAL LEU ILE THR SER
SEQRES 5 A 624 ALA LEU PRO TYR VAL ASN ASN VAL PRO HIS LEU GLY ASN
SEQRES 6 A 624 ILE ILE GLY CYS VAL LEU SER ALA ASP VAL PHE ALA ARG
SEQRES 7 A 624 TYR SER ARG LEU ARG GLN TRP ASN THR LEU TYR LEU CYS
SEQRES 8 A 624 GLY THR ASP GLU TYR GLY THR ALA THR GLU THR LYS ALA
SEQRES 9 A 624 LEU GLU GLU GLY LEU THR PRO GLN GLU ILE CYS ASP LYS
SEQRES 10 A 624 TYR HIS ILE ILE HIS ALA ASP ILE TYR ARG TRP PHE ASN
SEQRES 11 A 624 ILE SER PHE ASP ILE PHE GLY ARG THR THR THR PRO GLN
SEQRES 12 A 624 GLN THR LYS ILE THR GLN ASP ILE PHE GLN GLN LEU LEU
SEQRES 13 A 624 LYS ARG GLY PHE VAL LEU GLN ASP THR VAL GLU GLN LEU
SEQRES 14 A 624 ARG CYS GLU HIS CYS ALA ARG PHE LEU ALA ASP ARG PHE
SEQRES 15 A 624 VAL GLU GLY VAL CYS PRO PHE CYS GLY TYR GLU GLU ALA
SEQRES 16 A 624 ARG GLY ASP GLN CYS ASP LYS CYS GLY LYS LEU ILE ASN
SEQRES 17 A 624 ALA VAL GLU LEU LYS LYS PRO GLN CYS LYS VAL CYS ARG
SEQRES 18 A 624 SER CYS PRO VAL VAL GLN SER SER GLN HIS LEU PHE LEU
SEQRES 19 A 624 ASP LEU PRO LYS LEU GLU LYS ARG LEU GLU GLU TRP LEU
SEQRES 20 A 624 GLY ARG THR LEU PRO GLY SER ASP TRP THR PRO ASN ALA
SEQRES 21 A 624 GLN PHE ILE THR ARG SER TRP LEU ARG ASP GLY LEU LYS
SEQRES 22 A 624 PRO ARG CYS ILE THR ARG ASP LEU LYS TRP GLY THR PRO
SEQRES 23 A 624 VAL PRO LEU GLU GLY PHE GLU ASP LYS VAL PHE TYR VAL
SEQRES 24 A 624 TRP PHE ASP ALA THR ILE GLY TYR LEU SER ILE THR ALA
SEQRES 25 A 624 ASN TYR THR ASP GLN TRP GLU ARG TRP TRP LYS ASN PRO
SEQRES 26 A 624 GLU GLN VAL ASP LEU TYR GLN PHE MET ALA LYS ASP ASN
SEQRES 27 A 624 VAL PRO PHE HIS SER LEU VAL PHE PRO CYS SER ALA LEU
SEQRES 28 A 624 GLY ALA GLU ASP ASN TYR THR LEU VAL SER HIS LEU ILE
SEQRES 29 A 624 ALA THR GLU TYR LEU ASN TYR GLU ASP GLY LYS PHE SER
SEQRES 30 A 624 LYS SER ARG GLY VAL GLY VAL PHE GLY ASP MET ALA GLN
SEQRES 31 A 624 ASP THR GLY ILE PRO ALA ASP ILE TRP ARG PHE TYR LEU
SEQRES 32 A 624 LEU TYR ILE ARG PRO GLU GLY GLN ASP SER ALA PHE SER
SEQRES 33 A 624 TRP THR ASP LEU LEU LEU LYS ASN ASN SER GLU LEU LEU
SEQRES 34 A 624 ASN ASN LEU GLY ASN PHE ILE ASN ARG ALA GLY MET PHE
SEQRES 35 A 624 VAL SER LYS PHE PHE GLY GLY TYR VAL PRO GLU MET VAL
SEQRES 36 A 624 LEU THR PRO ASP ASP GLN ARG LEU LEU ALA HIS VAL THR
SEQRES 37 A 624 LEU GLU LEU GLN HIS TYR HIS GLN LEU LEU GLU LYS VAL
SEQRES 38 A 624 ARG ILE ARG ASP ALA LEU ARG SER ILE LEU THR ILE SER
SEQRES 39 A 624 ARG HIS GLY ASN GLN TYR ILE GLN VAL ASN GLU PRO TRP
SEQRES 40 A 624 LYS ARG ILE LYS GLY SER GLU ALA ASP ARG GLN ARG ALA
SEQRES 41 A 624 GLY THR VAL THR GLY LEU ALA VAL ASN ILE ALA ALA LEU
SEQRES 42 A 624 LEU SER VAL MET LEU GLN PRO TYR MET PRO THR VAL SER
SEQRES 43 A 624 ALA THR ILE GLN ALA GLN LEU GLN LEU PRO PRO PRO ALA
SEQRES 44 A 624 CYS SER ILE LEU LEU THR ASN PHE LEU CYS THR LEU PRO
SEQRES 45 A 624 ALA GLY HIS GLN ILE GLY THR VAL SER PRO LEU PHE GLN
SEQRES 46 A 624 LYS LEU GLU ASN ASP GLN ILE GLU SER LEU ARG GLN ARG
SEQRES 47 A 624 PHE GLY GLY GLY GLN ALA LYS THR SER PRO LYS PRO ALA
SEQRES 48 A 624 VAL VAL GLU THR VAL LEU GLU HIS HIS HIS HIS HIS HIS
HET ZN A 901 1
HET ZN A 902 1
HET GOL A 903 6
HET GOL A 904 6
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 HOH *345(H2 O)
HELIX 1 AA1 SER A 229 LYS A 242 1 14
HELIX 2 AA2 GLY A 243 LEU A 247 5 5
HELIX 3 AA3 HIS A 280 CYS A 287 1 8
HELIX 4 AA4 CYS A 287 ARG A 301 1 15
HELIX 5 AA5 GLY A 315 GLU A 325 1 11
HELIX 6 AA6 THR A 328 PHE A 347 1 20
HELIX 7 AA7 THR A 359 LYS A 375 1 17
HELIX 8 AA8 ALA A 397 ARG A 399 5 3
HELIX 9 AA9 ASN A 426 LEU A 430 5 5
HELIX 10 AB1 ASP A 453 LEU A 469 1 17
HELIX 11 AB2 THR A 475 GLY A 489 1 15
HELIX 12 AB3 TYR A 516 ALA A 521 1 6
HELIX 13 AB4 ILE A 523 THR A 533 1 11
HELIX 14 AB5 TRP A 536 LYS A 541 1 6
HELIX 15 AB6 ASN A 556 LEU A 562 1 7
HELIX 16 AB7 LEU A 562 GLU A 572 1 11
HELIX 17 AB8 MET A 606 GLY A 611 5 6
HELIX 18 AB9 PRO A 613 ILE A 624 1 12
HELIX 19 AC1 SER A 634 LEU A 646 1 13
HELIX 20 AC2 ASN A 649 PHE A 665 1 17
HELIX 21 AC3 THR A 675 GLU A 697 1 23
HELIX 22 AC4 ARG A 700 GLU A 723 1 24
HELIX 23 AC5 GLU A 723 ILE A 728 1 6
HELIX 24 AC6 SER A 731 LEU A 756 1 26
HELIX 25 AC7 MET A 760 GLN A 772 1 13
HELIX 26 AC8 PRO A 774 SER A 779 1 6
HELIX 27 AC9 GLU A 806 PHE A 817 1 12
SHEET 1 AA1 5 ILE A 353 ARG A 356 0
SHEET 2 AA1 5 ASN A 304 THR A 311 1 N CYS A 309 O GLY A 355
SHEET 3 AA1 5 ASN A 265 SER A 270 1 N ILE A 268 O LEU A 306
SHEET 4 AA1 5 VAL A 546 ALA A 553 1 O TYR A 549 N LEU A 267
SHEET 5 AA1 5 VAL A 578 THR A 584 1 O ILE A 582 N GLN A 550
SHEET 1 AA2 4 ARG A 394 PHE A 395 0
SHEET 2 AA2 4 VAL A 379 CYS A 389 -1 N CYS A 389 O ARG A 394
SHEET 3 AA2 4 VAL A 443 LEU A 452 -1 O PHE A 451 N LEU A 380
SHEET 4 AA2 4 ARG A 493 CYS A 494 -1 O ARG A 493 N LEU A 452
SHEET 1 AA3 3 ALA A 413 ARG A 414 0
SHEET 2 AA3 3 VAL A 401 VAL A 404 -1 N GLY A 403 O ALA A 413
SHEET 3 AA3 3 LYS A 431 CYS A 435 -1 O LYS A 431 N VAL A 404
SHEET 1 AA4 2 THR A 496 ARG A 497 0
SHEET 2 AA4 2 VAL A 514 PHE A 515 -1 O VAL A 514 N ARG A 497
SHEET 1 AA5 2 LEU A 587 TYR A 589 0
SHEET 2 AA5 2 SER A 631 PHE A 633 1 O PHE A 633 N ASN A 588
LINK SG CYS A 389 ZN ZN A 901 1555 1555 2.19
LINK SG CYS A 392 ZN ZN A 901 1555 1555 2.45
LINK SG CYS A 405 ZN ZN A 902 1555 1555 2.33
LINK SG CYS A 408 ZN ZN A 902 1555 1555 2.33
LINK SG CYS A 418 ZN ZN A 902 1555 1555 2.40
LINK SG CYS A 421 ZN ZN A 902 1555 1555 2.36
LINK SG CYS A 435 ZN ZN A 901 1555 1555 2.38
LINK SG CYS A 438 ZN ZN A 901 1555 1555 2.51
CISPEP 1 ASN A 255 PRO A 256 0 3.43
SITE 1 AC1 4 CYS A 389 CYS A 392 CYS A 435 CYS A 438
SITE 1 AC2 4 CYS A 405 CYS A 408 CYS A 418 CYS A 421
SITE 1 AC3 3 ARG A 299 GLN A 302 SER A 779
SITE 1 AC4 6 GLU A 263 GLN A 381 ASP A 382 THR A 383
SITE 2 AC4 6 HOH A1122 HOH A1176
CRYST1 65.035 93.030 122.084 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015376 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010749 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008191 0.00000
(ATOM LINES ARE NOT SHOWN.)
END