HEADER OXIDOREDUCTASE 29-JUL-14 4UUL
TITLE APO TRICHOMONAS VAGINALIS LACTATE DEHYDROGENASE L91R
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-LACTATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LACTATE DEHYDROGENASE;
COMPND 5 EC: 1.1.1.27;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRICHOMONAS VAGINALIS;
SOURCE 3 ORGANISM_TAXID: 5722;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-21B
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.STEINDEL,E.H.CHEN,D.L THEOBALD
REVDAT 5 10-JAN-24 4UUL 1 REMARK
REVDAT 4 23-OCT-19 4UUL 1 ATOM
REVDAT 3 06-JUL-16 4UUL 1 JRNL
REVDAT 2 02-MAR-16 4UUL 1 JRNL
REVDAT 1 12-AUG-15 4UUL 0
JRNL AUTH P.A.STEINDEL,E.H.CHEN,J.D.WIRTH,D.L.THEOBALD
JRNL TITL GRADUAL NEOFUNCTIONALIZATION IN THE CONVERGENT EVOLUTION OF
JRNL TITL 2 TRICHOMONAD LACTATE AND MALATE DEHYDROGENASES.
JRNL REF PROTEIN SCI. V. 25 1319 2016
JRNL REFN ISSN 0961-8368
JRNL PMID 26889885
JRNL DOI 10.1002/PRO.2904
REMARK 2
REMARK 2 RESOLUTION. 1.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 3 NUMBER OF REFLECTIONS : 175050
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.131
REMARK 3 R VALUE (WORKING SET) : 0.129
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8784
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 30.7206 - 3.9738 0.88 5597 293 0.1570 0.1597
REMARK 3 2 3.9738 - 3.1551 0.99 6197 324 0.1339 0.1567
REMARK 3 3 3.1551 - 2.7566 1.00 6164 331 0.1335 0.1557
REMARK 3 4 2.7566 - 2.5047 1.00 6163 318 0.1209 0.1312
REMARK 3 5 2.5047 - 2.3252 1.00 6182 322 0.1134 0.1355
REMARK 3 6 2.3252 - 2.1882 1.00 6112 321 0.1172 0.1539
REMARK 3 7 2.1882 - 2.0786 1.00 6131 337 0.1198 0.1338
REMARK 3 8 2.0786 - 1.9882 1.00 6106 325 0.1263 0.1699
REMARK 3 9 1.9882 - 1.9116 1.00 6138 312 0.1340 0.1667
REMARK 3 10 1.9116 - 1.8457 0.99 6118 331 0.1265 0.1480
REMARK 3 11 1.8457 - 1.7880 0.99 6108 306 0.1209 0.1521
REMARK 3 12 1.7880 - 1.7369 0.99 6117 311 0.1160 0.1553
REMARK 3 13 1.7369 - 1.6911 0.99 6013 344 0.1154 0.1547
REMARK 3 14 1.6911 - 1.6499 0.99 6090 330 0.1115 0.1537
REMARK 3 15 1.6499 - 1.6124 0.99 6064 293 0.1083 0.1409
REMARK 3 16 1.6124 - 1.5781 0.99 6093 334 0.1041 0.1405
REMARK 3 17 1.5781 - 1.5465 0.99 6037 330 0.1076 0.1457
REMARK 3 18 1.5465 - 1.5173 0.99 6018 310 0.1158 0.1630
REMARK 3 19 1.5173 - 1.4902 0.99 5991 321 0.1123 0.1541
REMARK 3 20 1.4902 - 1.4650 0.99 6076 323 0.1210 0.1629
REMARK 3 21 1.4650 - 1.4413 0.98 6010 325 0.1256 0.1597
REMARK 3 22 1.4413 - 1.4192 0.97 5886 307 0.1284 0.1755
REMARK 3 23 1.4192 - 1.3983 0.92 5642 290 0.1328 0.1763
REMARK 3 24 1.3983 - 1.3786 0.84 5102 278 0.1412 0.2008
REMARK 3 25 1.3786 - 1.3600 0.77 4728 246 0.1676 0.2135
REMARK 3 26 1.3600 - 1.3423 0.71 4308 222 0.1566 0.2248
REMARK 3 27 1.3423 - 1.3255 0.65 3942 220 0.1643 0.2007
REMARK 3 28 1.3255 - 1.3096 0.59 3607 190 0.1684 0.2008
REMARK 3 29 1.3096 - 1.2943 0.52 3153 168 0.2018 0.2654
REMARK 3 30 1.2943 - 1.2798 0.39 2373 122 0.2081 0.2625
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.40
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 : 0.013 5614
REMARK 3 ANGLE : 1.474 7667
REMARK 3 CHIRALITY : 0.099 844
REMARK 3 PLANARITY : 0.010 993
REMARK 3 DIHEDRAL : 12.675 2039
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 4UUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1290061313.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 175089
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 44.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.610
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.82000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.610
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: HOMOLOGY MODEL BASED ON PDB ENTRY 5MDH
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21 MG/ML PROTEIN, 100 MM HEPES PH 7.0,
REMARK 280 10% PEG-6000, 5% MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.80500
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HIS A 336
REMARK 465 HIS A 337
REMARK 465 HIS A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 MET B 1
REMARK 465 HIS B 339
REMARK 465 HIS B 340
REMARK 465 HIS B 341
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 ARG A 91 CG CD NE CZ NH1 NH2
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 GLU B 317 CD GLU B 317 OE2 -0.068
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 219 -66.22 -143.33
REMARK 500 ALA A 241 -52.22 -140.82
REMARK 500 ASP B 219 -66.90 -144.27
REMARK 500 ALA B 241 -56.36 -139.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2049 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A2070 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A2091 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A2119 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A2166 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B2031 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B2095 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B2112 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B2506 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B2507 DISTANCE = 7.22 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UUM RELATED DB: PDB
REMARK 900 APO TRICHOMONAS VAGINALIS LACTATE DEHYDROGENASE
REMARK 900 RELATED ID: 4UUN RELATED DB: PDB
REMARK 900 TRICHOMONAS VAGINALIS LACATATE DEHYDROGENASE IN COMPLEX WITH NADH
REMARK 900 RELATED ID: 4UUO RELATED DB: PDB
REMARK 900 APO TRICHOMONAS VAGINALIS MALATE DEHYDROGENASE
REMARK 900 RELATED ID: 4UUP RELATED DB: PDB
REMARK 900 RECONSTRUCTED ANCESTRAL TRICHOMONAD MALATE DEHYDROGENASE IN COMPLEX
REMARK 900 WITH NADH, SO4, AND PO4
DBREF 4UUL A 1 333 UNP O96445 O96445_TRIVA 1 333
DBREF 4UUL B 1 333 UNP O96445 O96445_TRIVA 1 333
SEQADV 4UUL LEU A 334 UNP O96445 EXPRESSION TAG
SEQADV 4UUL GLU A 335 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS A 336 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS A 337 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS A 338 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS A 339 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS A 340 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS A 341 UNP O96445 EXPRESSION TAG
SEQADV 4UUL ARG A 91 UNP O96445 LEU 91 ENGINEERED MUTATION
SEQADV 4UUL LEU B 334 UNP O96445 EXPRESSION TAG
SEQADV 4UUL GLU B 335 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS B 336 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS B 337 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS B 338 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS B 339 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS B 340 UNP O96445 EXPRESSION TAG
SEQADV 4UUL HIS B 341 UNP O96445 EXPRESSION TAG
SEQADV 4UUL ARG B 91 UNP O96445 LEU 91 ENGINEERED MUTATION
SEQRES 1 A 341 MET SER GLU ALA ALA HIS VAL LEU ILE THR GLY ALA ALA
SEQRES 2 A 341 GLY GLN ILE GLY TYR ILE LEU SER HIS TRP ILE ALA SER
SEQRES 3 A 341 GLY GLU LEU TYR GLY ASP ARG GLN VAL TYR LEU HIS LEU
SEQRES 4 A 341 LEU ASP ILE PRO PRO ALA MET ASN ARG LEU THR ALA LEU
SEQRES 5 A 341 THR MET GLU LEU GLU ASP CYS ALA PHE PRO HIS LEU ALA
SEQRES 6 A 341 GLY PHE VAL ALA THR THR ASP PRO LYS ALA ALA PHE LYS
SEQRES 7 A 341 ASP ILE ASP CYS ALA PHE LEU VAL ALA SER MET PRO ARG
SEQRES 8 A 341 LYS PRO GLY GLN VAL ARG ALA ASP LEU ILE SER SER ASN
SEQRES 9 A 341 SER VAL ILE PHE LYS ASN THR GLY GLU TYR LEU SER LYS
SEQRES 10 A 341 TRP ALA LYS PRO SER VAL LYS VAL LEU VAL ILE GLY ASN
SEQRES 11 A 341 PRO ASP ASN THR ASN CYS GLU ILE ALA MET LEU HIS ALA
SEQRES 12 A 341 LYS ASN LEU LYS PRO GLU ASN PHE SER SER LEU SER MET
SEQRES 13 A 341 LEU ASP GLN ASN ARG ALA TYR TYR GLU VAL ALA SER LYS
SEQRES 14 A 341 LEU GLY VAL ASP VAL LYS ASP VAL HIS ASP ILE ILE VAL
SEQRES 15 A 341 TRP GLY ASN HIS GLY GLU SER MET VAL ALA ASP LEU THR
SEQRES 16 A 341 GLN ALA THR PHE THR LYS GLU GLY LYS THR GLN LYS VAL
SEQRES 17 A 341 VAL ASP VAL LEU ASP HIS ASP TYR VAL PHE ASP THR PHE
SEQRES 18 A 341 PHE LYS LYS ILE GLY HIS ARG ALA TRP ASP ILE LEU GLU
SEQRES 19 A 341 HIS ARG GLY PHE THR SER ALA ALA SER PRO THR LYS ALA
SEQRES 20 A 341 ALA ILE GLN HIS MET LYS ALA TRP LEU PHE GLY THR ALA
SEQRES 21 A 341 PRO GLY GLU VAL LEU SER MET GLY ILE PRO VAL PRO GLU
SEQRES 22 A 341 GLY ASN PRO TYR GLY ILE LYS PRO GLY VAL VAL PHE SER
SEQRES 23 A 341 PHE PRO CYS ASN VAL ASP LYS GLU GLY LYS ILE HIS VAL
SEQRES 24 A 341 VAL GLU GLY PHE LYS VAL ASN ASP TRP LEU ARG GLU LYS
SEQRES 25 A 341 LEU ASP PHE THR GLU LYS ASP LEU PHE HIS GLU LYS GLU
SEQRES 26 A 341 ILE ALA LEU ASN HIS LEU ALA GLN LEU GLU HIS HIS HIS
SEQRES 27 A 341 HIS HIS HIS
SEQRES 1 B 341 MET SER GLU ALA ALA HIS VAL LEU ILE THR GLY ALA ALA
SEQRES 2 B 341 GLY GLN ILE GLY TYR ILE LEU SER HIS TRP ILE ALA SER
SEQRES 3 B 341 GLY GLU LEU TYR GLY ASP ARG GLN VAL TYR LEU HIS LEU
SEQRES 4 B 341 LEU ASP ILE PRO PRO ALA MET ASN ARG LEU THR ALA LEU
SEQRES 5 B 341 THR MET GLU LEU GLU ASP CYS ALA PHE PRO HIS LEU ALA
SEQRES 6 B 341 GLY PHE VAL ALA THR THR ASP PRO LYS ALA ALA PHE LYS
SEQRES 7 B 341 ASP ILE ASP CYS ALA PHE LEU VAL ALA SER MET PRO ARG
SEQRES 8 B 341 LYS PRO GLY GLN VAL ARG ALA ASP LEU ILE SER SER ASN
SEQRES 9 B 341 SER VAL ILE PHE LYS ASN THR GLY GLU TYR LEU SER LYS
SEQRES 10 B 341 TRP ALA LYS PRO SER VAL LYS VAL LEU VAL ILE GLY ASN
SEQRES 11 B 341 PRO ASP ASN THR ASN CYS GLU ILE ALA MET LEU HIS ALA
SEQRES 12 B 341 LYS ASN LEU LYS PRO GLU ASN PHE SER SER LEU SER MET
SEQRES 13 B 341 LEU ASP GLN ASN ARG ALA TYR TYR GLU VAL ALA SER LYS
SEQRES 14 B 341 LEU GLY VAL ASP VAL LYS ASP VAL HIS ASP ILE ILE VAL
SEQRES 15 B 341 TRP GLY ASN HIS GLY GLU SER MET VAL ALA ASP LEU THR
SEQRES 16 B 341 GLN ALA THR PHE THR LYS GLU GLY LYS THR GLN LYS VAL
SEQRES 17 B 341 VAL ASP VAL LEU ASP HIS ASP TYR VAL PHE ASP THR PHE
SEQRES 18 B 341 PHE LYS LYS ILE GLY HIS ARG ALA TRP ASP ILE LEU GLU
SEQRES 19 B 341 HIS ARG GLY PHE THR SER ALA ALA SER PRO THR LYS ALA
SEQRES 20 B 341 ALA ILE GLN HIS MET LYS ALA TRP LEU PHE GLY THR ALA
SEQRES 21 B 341 PRO GLY GLU VAL LEU SER MET GLY ILE PRO VAL PRO GLU
SEQRES 22 B 341 GLY ASN PRO TYR GLY ILE LYS PRO GLY VAL VAL PHE SER
SEQRES 23 B 341 PHE PRO CYS ASN VAL ASP LYS GLU GLY LYS ILE HIS VAL
SEQRES 24 B 341 VAL GLU GLY PHE LYS VAL ASN ASP TRP LEU ARG GLU LYS
SEQRES 25 B 341 LEU ASP PHE THR GLU LYS ASP LEU PHE HIS GLU LYS GLU
SEQRES 26 B 341 ILE ALA LEU ASN HIS LEU ALA GLN LEU GLU HIS HIS HIS
SEQRES 27 B 341 HIS HIS HIS
FORMUL 3 HOH *1005(H2 O)
HELIX 1 1 GLY A 14 SER A 26 1 13
HELIX 2 2 ILE A 42 PRO A 44 5 3
HELIX 3 3 ALA A 45 ASP A 58 1 14
HELIX 4 4 ASP A 72 LYS A 78 1 7
HELIX 5 5 VAL A 96 ALA A 119 1 24
HELIX 6 6 PRO A 131 HIS A 142 1 12
HELIX 7 7 LYS A 147 GLU A 149 5 3
HELIX 8 8 SER A 155 GLY A 171 1 17
HELIX 9 9 ASP A 173 LYS A 175 5 3
HELIX 10 10 HIS A 186 MET A 190 5 5
HELIX 11 11 VAL A 208 LEU A 212 1 5
HELIX 12 12 ASP A 213 ASP A 219 1 7
HELIX 13 13 ASP A 219 GLY A 237 1 19
HELIX 14 14 ALA A 241 GLY A 258 1 18
HELIX 15 15 ASN A 306 GLU A 335 1 30
HELIX 16 16 GLY B 14 SER B 26 1 13
HELIX 17 17 ILE B 42 PRO B 44 5 3
HELIX 18 18 ALA B 45 ASP B 58 1 14
HELIX 19 19 ASP B 72 LYS B 78 1 7
HELIX 20 20 VAL B 96 ALA B 119 1 24
HELIX 21 21 PRO B 131 HIS B 142 1 12
HELIX 22 22 LYS B 147 GLU B 149 5 3
HELIX 23 23 SER B 155 GLY B 171 1 17
HELIX 24 24 ASP B 173 LYS B 175 5 3
HELIX 25 25 HIS B 186 MET B 190 5 5
HELIX 26 26 VAL B 208 LEU B 212 1 5
HELIX 27 27 ASP B 213 PHE B 218 1 6
HELIX 28 28 ASP B 219 GLY B 237 1 19
HELIX 29 29 ALA B 241 GLY B 258 1 18
HELIX 30 30 ASN B 306 HIS B 338 1 33
SHEET 1 AA 6 LEU A 64 THR A 70 0
SHEET 2 AA 6 VAL A 35 LEU A 40 1 O VAL A 35 N ALA A 65
SHEET 3 AA 6 ALA A 5 THR A 10 1 O ALA A 5 N TYR A 36
SHEET 4 AA 6 CYS A 82 LEU A 85 1 O CYS A 82 N LEU A 8
SHEET 5 AA 6 LYS A 124 VAL A 127 1 O LYS A 124 N ALA A 83
SHEET 6 AA 6 PHE A 151 SER A 153 1 O SER A 152 N VAL A 127
SHEET 1 AB 3 VAL A 177 HIS A 178 0
SHEET 2 AB 3 THR A 198 LYS A 201 -1 O THR A 198 N HIS A 178
SHEET 3 AB 3 LYS A 204 LYS A 207 -1 O LYS A 204 N LYS A 201
SHEET 1 AC 2 ILE A 181 TRP A 183 0
SHEET 2 AC 2 VAL A 191 ASP A 193 -1 O VAL A 191 N TRP A 183
SHEET 1 AD 3 LEU A 265 PRO A 270 0
SHEET 2 AD 3 VAL A 284 VAL A 291 -1 O PHE A 285 N ILE A 269
SHEET 3 AD 3 ILE A 297 VAL A 299 -1 O HIS A 298 N ASN A 290
SHEET 1 BA 6 LEU B 64 THR B 70 0
SHEET 2 BA 6 VAL B 35 LEU B 40 1 O VAL B 35 N ALA B 65
SHEET 3 BA 6 ALA B 5 THR B 10 1 O ALA B 5 N TYR B 36
SHEET 4 BA 6 CYS B 82 LEU B 85 1 O CYS B 82 N LEU B 8
SHEET 5 BA 6 LYS B 124 VAL B 127 1 O LYS B 124 N ALA B 83
SHEET 6 BA 6 PHE B 151 SER B 153 1 O SER B 152 N VAL B 127
SHEET 1 BB 3 VAL B 177 HIS B 178 0
SHEET 2 BB 3 THR B 198 LYS B 201 -1 O THR B 198 N HIS B 178
SHEET 3 BB 3 LYS B 204 LYS B 207 -1 O LYS B 204 N LYS B 201
SHEET 1 BC 2 ILE B 181 TRP B 183 0
SHEET 2 BC 2 VAL B 191 ASP B 193 -1 O VAL B 191 N TRP B 183
SHEET 1 BD 3 LEU B 265 PRO B 270 0
SHEET 2 BD 3 VAL B 284 VAL B 291 -1 O PHE B 285 N ILE B 269
SHEET 3 BD 3 ILE B 297 VAL B 299 -1 O HIS B 298 N ASN B 290
CISPEP 1 ASN A 130 PRO A 131 0 -6.18
CISPEP 2 ASN B 130 PRO B 131 0 -1.70
CISPEP 3 ASN B 130 PRO B 131 0 -9.28
CRYST1 82.570 59.610 86.490 90.00 116.18 90.00 P 1 21 1 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 0.012111 0.000000 0.005954 0.00000
SCALE2 0.000000 0.016776 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012884 0.00000
(ATOM LINES ARE NOT SHOWN.)
END