HEADER TRANSPORT PROTEIN/INHIBITOR 16-JAN-15 4XPF
TITLE X-RAY STRUCTURE OF DROSOPHILA DOPAMINE TRANSPORTER WITH SUBSITEB
TITLE 2 MUTATIONS (D121G/S426M) BOUND TO RTI-55
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOPAMINE TRANSPORTER-PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ANTIBODY FRAGMENT HEAVY CHAIN-PROTEIN, 9D5-HEAVY CHAIN;
COMPND 7 CHAIN: L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ANTIBODY FRAGMENT LIGHT CHAIN-PROTEIN, 9D5-LIGHT CHAIN;
COMPND 11 CHAIN: H;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_TAXID: 7227;
SOURCE 4 GENE: DDAT;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: GNTI-, HEK293S;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEG BACMAM;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA;
SOURCE 16 OTHER_DETAILS: HYBRIDOMA CELLS;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 19 ORGANISM_COMMON: MOUSE;
SOURCE 20 ORGANISM_TAXID: 10090;
SOURCE 21 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: HYBRIDOMA;
SOURCE 24 OTHER_DETAILS: HYBRIDOMA CELLS
KEYWDS ALL ALPHA-HELICAL INTEGRAL MEMBRANE PROTEIN, TRANSPORT PROTEIN-
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PENMATSA,K.H.WANG,E.GOUAUX
REVDAT 4 27-SEP-23 4XPF 1 REMARK
REVDAT 3 26-AUG-15 4XPF 1 SEQRES
REVDAT 2 19-AUG-15 4XPF 1 JRNL
REVDAT 1 06-MAY-15 4XPF 0
JRNL AUTH K.H.WANG,A.PENMATSA,E.GOUAUX
JRNL TITL NEUROTRANSMITTER AND PSYCHOSTIMULANT RECOGNITION BY THE
JRNL TITL 2 DOPAMINE TRANSPORTER.
JRNL REF NATURE V. 521 322 2015
JRNL REFN ESSN 1476-4687
JRNL PMID 25970245
JRNL DOI 10.1038/NATURE14431
REMARK 2
REMARK 2 RESOLUTION. 3.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 3.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 3 NUMBER OF REFLECTIONS : 32039
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1605
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 48.3289 - 7.2722 0.81 2652 156 0.2148 0.2705
REMARK 3 2 7.2722 - 5.7752 0.86 2742 129 0.2334 0.2693
REMARK 3 3 5.7752 - 5.0461 0.88 2754 143 0.1996 0.2454
REMARK 3 4 5.0461 - 4.5851 0.89 2800 131 0.1809 0.2541
REMARK 3 5 4.5851 - 4.2567 0.91 2788 152 0.1885 0.2499
REMARK 3 6 4.2567 - 4.0058 0.91 2810 144 0.2339 0.3309
REMARK 3 7 4.0058 - 3.8053 0.91 2795 147 0.3079 0.3545
REMARK 3 8 3.8053 - 3.6397 0.91 2774 141 0.3578 0.3872
REMARK 3 9 3.6397 - 3.4997 0.92 2819 151 0.3526 0.4009
REMARK 3 10 3.4997 - 3.3789 0.92 2772 175 0.3929 0.4363
REMARK 3 11 3.3789 - 3.2733 0.89 2728 136 0.4077 0.4422
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) : 0.600
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 114.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 110.3
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 : 0.005 7735
REMARK 3 ANGLE : 0.920 10559
REMARK 3 CHIRALITY : 0.037 1188
REMARK 3 PLANARITY : 0.004 1301
REMARK 3 DIHEDRAL : 13.907 2686
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: RESIDUE H CYS 134 AND RESIDUE H GLY 139
REMARK 3 ARE NOT PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 10.88.
REMARK 4
REMARK 4 4XPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206071.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.24
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32190
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.270
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 (%) : 89.4
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.83800
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: PHASER
REMARK 200 STARTING MODEL: 4M48
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 77.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400 39%, BICINE 0.1M, PH 8.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
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 48.70750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.48100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.15600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.48100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.70750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.15600
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, 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 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 20
REMARK 465 ASN A 21
REMARK 465 SER A 22
REMARK 465 ILE A 23
REMARK 465 SER A 24
REMARK 465 GLN A 600
REMARK 465 GLN A 601
REMARK 465 LEU A 602
REMARK 465 VAL A 603
REMARK 465 PRO A 604
REMARK 465 ARG A 605
REMARK 465 MET L -21
REMARK 465 ASP L -20
REMARK 465 PHE L -19
REMARK 465 GLN L -18
REMARK 465 VAL L -17
REMARK 465 GLN L -16
REMARK 465 ILE L -15
REMARK 465 PHE L -14
REMARK 465 SER L -13
REMARK 465 PHE L -12
REMARK 465 LEU L -11
REMARK 465 LEU L -10
REMARK 465 ILE L -9
REMARK 465 SER L -8
REMARK 465 ALA L -7
REMARK 465 SER L -6
REMARK 465 VAL L -5
REMARK 465 ALA L -4
REMARK 465 MET L -3
REMARK 465 SER L -2
REMARK 465 ARG L -1
REMARK 465 GLY L 0
REMARK 465 CYS L 215
REMARK 465 MET H -18
REMARK 465 ASN H -17
REMARK 465 PHE H -16
REMARK 465 GLY H -15
REMARK 465 LEU H -14
REMARK 465 ARG H -13
REMARK 465 LEU H -12
REMARK 465 VAL H -11
REMARK 465 PHE H -10
REMARK 465 LEU H -9
REMARK 465 VAL H -8
REMARK 465 LEU H -7
REMARK 465 ILE H -6
REMARK 465 LEU H -5
REMARK 465 LYS H -4
REMARK 465 GLY H -3
REMARK 465 VAL H -2
REMARK 465 GLN H -1
REMARK 465 CYS H 0
REMARK 465 GLY H 135
REMARK 465 ASP H 136
REMARK 465 THR H 137
REMARK 465 THR H 138
REMARK 465 GLY H 220
REMARK 465 PRO H 221
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 SER A 162 OG
REMARK 470 GLN A 163 CG CD OE1 NE2
REMARK 470 LYS A 236 CG CD CE NZ
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 TYR A 305 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 306 CG CD CE NZ
REMARK 470 GLU A 308 CG CD OE1 OE2
REMARK 470 VAL A 311 CG1 CG2
REMARK 470 LYS A 343 CG CD CE NZ
REMARK 470 ARG A 442 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 457 CG1 CG2
REMARK 470 ARG A 476 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 517 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 580 CG CD1 CD2
REMARK 470 LEU A 586 CG CD1 CD2
REMARK 470 ARG A 587 CG CD NE CZ NH1 NH2
REMARK 470 SER L 128 OG
REMARK 470 GLU L 155 CG CD OE1 OE2
REMARK 470 LYS L 170 CG CD CE NZ
REMARK 470 LYS L 184 CG CD CE NZ
REMARK 470 ARG L 189 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 1 CG CD OE1 OE2
REMARK 470 GLN H 3 CG CD OE1 NE2
REMARK 470 THR H 28 OG1 CG2
REMARK 470 SER H 30 OG
REMARK 470 ARG H 76 CG CD NE CZ NH1 NH2
REMARK 470 GLN H 111 CG CD OE1 NE2
REMARK 470 VAL H 189 CG1 CG2
REMARK 470 SER H 198 OG
REMARK 470 ARG H 219 CG CD NE CZ NH1 NH2
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 O SER H 192 OG SER H 196 1.71
REMARK 500 CD1 LEU H 130 N CYS H 146 1.76
REMARK 500 CE2 TYR A 124 O 42F A 703 1.95
REMARK 500 CD1 TRP H 194 CD1 ILE H 199 2.05
REMARK 500 CD2 TYR A 124 C15 42F A 703 2.11
REMARK 500 O SER L 31 OG1 THR L 52 2.14
REMARK 500 O THR H 69 N GLU H 82 2.16
REMARK 500 NZ LYS H 211 O HOH H 301 2.17
REMARK 500 O LEU A 254 NH1 ARG A 444 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 PRO A 596 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO L 96 C - N - CD ANGL. DEV. = 17.5 DEGREES
REMARK 500 PRO L 142 C - N - CD ANGL. DEV. = 17.6 DEGREES
REMARK 500 TYR L 187 CB - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO H 132 C - N - CD ANGL. DEV. = -27.8 DEGREES
REMARK 500 PRO H 155 C - N - CD ANGL. DEV. = -31.5 DEGREES
REMARK 500 PRO H 173 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 SER H 198 N - CA - CB ANGL. DEV. = -10.9 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 ARG A 92 -0.57 69.94
REMARK 500 LEU A 102 -66.31 -104.01
REMARK 500 TYR A 123 -50.88 -129.76
REMARK 500 THR A 140 165.03 172.37
REMARK 500 ASN A 217 -62.44 -96.19
REMARK 500 THR A 260 -62.11 -99.16
REMARK 500 HIS A 372 -72.43 -102.60
REMARK 500 VAL A 391 -66.01 -131.81
REMARK 500 ARG A 444 -70.81 -74.61
REMARK 500 GLU A 445 70.31 34.76
REMARK 500 LEU A 446 -10.07 84.44
REMARK 500 TYR A 477 -59.37 -122.50
REMARK 500 ALA A 548 -134.63 57.44
REMARK 500 TRP L 48 -60.39 -103.53
REMARK 500 SER L 51 -131.15 62.01
REMARK 500 THR L 52 -51.59 -122.48
REMARK 500 ALA L 85 -175.05 -171.09
REMARK 500 LYS L 170 -70.93 -90.63
REMARK 500 ASN L 191 -64.47 -130.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 444 GLU A 445 124.75
REMARK 500 ARG H 98 GLY H 99 147.76
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 NA A 707 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 42 O
REMARK 620 2 VAL A 45 O 83.9
REMARK 620 3 LEU A 417 O 165.6 87.0
REMARK 620 4 ASP A 420 OD1 105.2 140.0 75.0
REMARK 620 5 SER A 421 OG 90.1 79.1 99.2 138.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 706 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 44 O
REMARK 620 2 ASN A 49 OD1 77.2
REMARK 620 3 SER A 320 O 78.0 153.4
REMARK 620 4 SER A 320 OG 127.2 125.1 65.2
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 DMU A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 42F A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 708
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XNU RELATED DB: PDB
REMARK 900 RELATED ID: 4XNX RELATED DB: PDB
REMARK 900 RELATED ID: 4XP1 RELATED DB: PDB
REMARK 900 RELATED ID: 4XP4 RELATED DB: PDB
REMARK 900 RELATED ID: 4XP5 RELATED DB: PDB
REMARK 900 RELATED ID: 4XP6 RELATED DB: PDB
REMARK 900 RELATED ID: 4XP9 RELATED DB: PDB
REMARK 900 RELATED ID: 4XPA RELATED DB: PDB
REMARK 900 RELATED ID: 4XPB RELATED DB: PDB
REMARK 900 RELATED ID: 4XPG RELATED DB: PDB
REMARK 900 RELATED ID: 4XPH RELATED DB: PDB
REMARK 900 RELATED ID: 4XPT RELATED DB: PDB
DBREF 4XPF A 20 605 PDB 4XPF 4XPF 20 605
DBREF 4XPF L -21 215 PDB 4XPF 4XPF -21 215
DBREF 4XPF H -18 221 PDB 4XPF 4XPF -18 221
SEQRES 1 A 543 MET ASN SER ILE SER ASP GLU ARG GLU THR TRP SER GLY
SEQRES 2 A 543 LYS VAL ASP PHE LEU LEU SER VAL ILE GLY PHE ALA VAL
SEQRES 3 A 543 ASP LEU ALA ASN VAL TRP ARG PHE PRO TYR LEU CYS TYR
SEQRES 4 A 543 LYS ASN GLY GLY GLY ALA PHE LEU VAL PRO TYR GLY ILE
SEQRES 5 A 543 MET LEU ALA VAL GLY GLY ILE PRO LEU PHE TYR MET GLU
SEQRES 6 A 543 LEU ALA LEU GLY GLN HIS ASN ARG LYS GLY ALA ILE THR
SEQRES 7 A 543 CYS TRP GLY ARG LEU VAL PRO LEU PHE LYS GLY ILE GLY
SEQRES 8 A 543 TYR ALA VAL VAL LEU ILE ALA PHE TYR VAL GLY PHE TYR
SEQRES 9 A 543 TYR ASN VAL ILE ILE ALA TRP SER LEU ARG PHE PHE PHE
SEQRES 10 A 543 ALA SER PHE THR ASN SER LEU PRO TRP THR SER CYS ASN
SEQRES 11 A 543 ASN ILE TRP ASN THR PRO ASN CYS ARG PRO PHE GLU SER
SEQRES 12 A 543 GLN GLY PHE GLN SER ALA ALA SER GLU TYR PHE ASN ARG
SEQRES 13 A 543 TYR ILE LEU GLU LEU ASN ARG SER GLU GLY ILE HIS ASP
SEQRES 14 A 543 LEU GLY ALA ILE LYS TRP ASP MET ALA LEU CYS LEU LEU
SEQRES 15 A 543 ILE VAL TYR LEU ILE CYS TYR PHE SER LEU TRP LYS GLY
SEQRES 16 A 543 ILE SER THR SER GLY LYS VAL VAL TRP PHE THR ALA LEU
SEQRES 17 A 543 PHE PRO TYR ALA VAL LEU LEU ILE LEU LEU ILE ARG GLY
SEQRES 18 A 543 LEU THR LEU PRO GLY SER PHE LEU GLY ILE GLN TYR TYR
SEQRES 19 A 543 LEU THR PRO ASN PHE SER ALA ILE TYR LYS ALA GLU VAL
SEQRES 20 A 543 TRP VAL ASP ALA ALA THR GLN VAL PHE PHE SER LEU GLY
SEQRES 21 A 543 PRO GLY PHE GLY VAL LEU LEU ALA TYR ALA SER TYR ASN
SEQRES 22 A 543 LYS TYR HIS ASN ASN VAL TYR LYS ASP ALA LEU LEU THR
SEQRES 23 A 543 SER PHE ILE ASN SER ALA THR SER PHE ILE ALA GLY PHE
SEQRES 24 A 543 VAL ILE PHE SER VAL LEU GLY TYR MET ALA HIS THR LEU
SEQRES 25 A 543 GLY VAL ARG ILE GLU ASP VAL ALA THR GLU GLY PRO GLY
SEQRES 26 A 543 LEU VAL PHE VAL VAL TYR PRO ALA ALA ILE ALA THR MET
SEQRES 27 A 543 PRO ALA SER THR PHE TRP ALA LEU ILE PHE PHE MET MET
SEQRES 28 A 543 LEU ALA THR LEU GLY LEU ASP SER SER PHE GLY GLY MET
SEQRES 29 A 543 GLU ALA ILE ILE THR ALA LEU SER ASP GLU PHE PRO LYS
SEQRES 30 A 543 ILE LYS ARG ASN ARG GLU LEU PHE VAL ALA GLY LEU PHE
SEQRES 31 A 543 SER LEU TYR PHE VAL VAL GLY LEU ALA SER CYS THR GLN
SEQRES 32 A 543 GLY GLY PHE TYR PHE PHE HIS LEU LEU ASP ARG TYR ALA
SEQRES 33 A 543 ALA GLY TYR SER ILE LEU VAL ALA VAL PHE PHE GLU ALA
SEQRES 34 A 543 ILE ALA VAL SER TRP ILE TYR GLY THR ASN ARG PHE SER
SEQRES 35 A 543 GLU ASP ILE ARG ASP MET ILE GLY PHE PRO PRO GLY ARG
SEQRES 36 A 543 TYR TRP GLN VAL CYS TRP ARG PHE VAL ALA PRO ILE PHE
SEQRES 37 A 543 LEU LEU PHE ILE THR VAL TYR GLY LEU ILE GLY TYR GLU
SEQRES 38 A 543 PRO LEU THR TYR ALA ASP TYR VAL TYR PRO SER TRP ALA
SEQRES 39 A 543 ASN ALA LEU GLY TRP CYS ILE ALA GLY SER SER VAL VAL
SEQRES 40 A 543 MET ILE PRO ALA VAL ALA ILE PHE LYS LEU LEU SER THR
SEQRES 41 A 543 PRO GLY SER LEU ARG GLN ARG PHE THR ILE LEU THR THR
SEQRES 42 A 543 PRO TRP ARG ASP GLN GLN LEU VAL PRO ARG
SEQRES 1 L 237 MET ASP PHE GLN VAL GLN ILE PHE SER PHE LEU LEU ILE
SEQRES 2 L 237 SER ALA SER VAL ALA MET SER ARG GLY GLU ASN VAL LEU
SEQRES 3 L 237 THR GLN SER PRO ALA ILE MET SER THR SER PRO GLY GLU
SEQRES 4 L 237 LYS VAL THR MET THR CYS ARG ALA SER SER SER VAL GLY
SEQRES 5 L 237 SER SER TYR LEU HIS TRP TYR GLN GLN LYS SER GLY ALA
SEQRES 6 L 237 SER PRO LYS LEU TRP ILE TYR SER THR SER ASN LEU ALA
SEQRES 7 L 237 SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SER GLY
SEQRES 8 L 237 THR SER TYR SER LEU THR ILE SER SER VAL GLU ALA GLU
SEQRES 9 L 237 ASP ALA ALA THR TYR TYR CYS GLN GLN PHE SER GLY TYR
SEQRES 10 L 237 PRO LEU THR PHE GLY SER GLY THR LYS LEU GLU MET LYS
SEQRES 11 L 237 ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO PRO
SEQRES 12 L 237 SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL VAL
SEQRES 13 L 237 CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN VAL
SEQRES 14 L 237 LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY VAL
SEQRES 15 L 237 LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER THR
SEQRES 16 L 237 TYR SER MET SER SER THR LEU THR LEU THR LYS ASP GLU
SEQRES 17 L 237 TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR HIS
SEQRES 18 L 237 LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN ARG
SEQRES 19 L 237 ASN GLU CYS
SEQRES 1 H 240 MET ASN PHE GLY LEU ARG LEU VAL PHE LEU VAL LEU ILE
SEQRES 2 H 240 LEU LYS GLY VAL GLN CYS GLU VAL GLN LEU VAL GLU SER
SEQRES 3 H 240 GLY GLY GLY LEU VAL LYS PRO GLY GLY SER LEU LYS LEU
SEQRES 4 H 240 SER CYS ALA ALA SER GLY PHE THR PHE SER SER TYR ALA
SEQRES 5 H 240 MET SER TRP VAL ARG GLN SER PRO GLU LYS ARG LEU GLU
SEQRES 6 H 240 TRP VAL ALA GLU ILE SER SER GLY GLY ARG TYR ILE TYR
SEQRES 7 H 240 TYR SER ASP THR VAL THR GLY ARG PHE THR ILE SER ARG
SEQRES 8 H 240 ASP ASN ALA ARG ASN ILE LEU HIS LEU GLU MET SER SER
SEQRES 9 H 240 LEU ARG SER GLU ASP THR ALA MET TYR TYR CYS ALA ARG
SEQRES 10 H 240 GLY GLU VAL ARG GLN ARG GLY PHE ASP TYR TRP GLY GLN
SEQRES 11 H 240 GLY THR THR LEU THR VAL SER SER ALA LYS THR THR ALA
SEQRES 12 H 240 PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR
SEQRES 13 H 240 THR GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY
SEQRES 14 H 240 TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY
SEQRES 15 H 240 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU
SEQRES 16 H 240 GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL
SEQRES 17 H 240 THR SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN
SEQRES 18 H 240 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS
SEQRES 19 H 240 ILE GLU PRO ARG GLY PRO
HET DMU A 701 33
HET P4G A 702 29
HET 42F A 703 20
HET CLR A 704 28
HET CLR A 705 28
HET NA A 706 1
HET NA A 707 1
HET CL A 708 1
HETNAM DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETNAM P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE
HETNAM 42F METHYL (1R,2S,3S,5S)-3-(4-IODOPHENYL)-8-METHYL-8-
HETNAM 2 42F AZABICYCLO[3.2.1]OCTANE-2-CARBOXYLATE
HETNAM CLR CHOLESTEROL
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETSYN DMU DECYLMALTOSIDE
FORMUL 4 DMU C22 H42 O11
FORMUL 5 P4G C8 H18 O3
FORMUL 6 42F C16 H20 I N O2
FORMUL 7 CLR 2(C27 H46 O)
FORMUL 9 NA 2(NA 1+)
FORMUL 11 CL CL 1-
FORMUL 12 HOH *6(H2 O)
HELIX 1 AA1 GLY A 32 VAL A 45 1 14
HELIX 2 AA2 ASP A 46 ARG A 52 1 7
HELIX 3 AA3 ARG A 52 ASN A 60 1 9
HELIX 4 AA4 GLY A 61 ALA A 64 5 4
HELIX 5 AA5 PHE A 65 VAL A 75 1 11
HELIX 6 AA6 GLY A 76 ASN A 91 1 16
HELIX 7 AA7 GLY A 94 ARG A 101 1 8
HELIX 8 AA8 VAL A 103 PHE A 106 5 4
HELIX 9 AA9 LYS A 107 GLY A 121 1 15
HELIX 10 AB1 PHE A 122 TYR A 124 5 3
HELIX 11 AB2 ASN A 125 ALA A 137 1 13
HELIX 12 AB3 LEU A 143 SER A 147 5 5
HELIX 13 AB4 ALA A 212 TYR A 219 1 8
HELIX 14 AB5 GLU A 222 SER A 226 5 5
HELIX 15 AB6 LYS A 236 TRP A 255 1 20
HELIX 16 AB7 LYS A 256 ALA A 269 1 14
HELIX 17 AB8 LEU A 270 LEU A 286 1 17
HELIX 18 AB9 GLY A 288 THR A 298 1 11
HELIX 19 AC1 ASN A 300 TYR A 305 5 6
HELIX 20 AC2 LYS A 306 GLY A 322 1 17
HELIX 21 AC3 GLY A 326 TYR A 334 1 9
HELIX 22 AC4 ASN A 340 THR A 373 1 34
HELIX 23 AC5 ARG A 377 ALA A 382 1 6
HELIX 24 AC6 GLY A 385 VAL A 391 1 7
HELIX 25 AC7 VAL A 391 ALA A 398 1 8
HELIX 26 AC8 ALA A 402 ASP A 435 1 34
HELIX 27 AC9 PRO A 438 ASN A 443 1 6
HELIX 28 AD1 LEU A 446 GLY A 459 1 14
HELIX 29 AD2 GLY A 466 ALA A 478 1 13
HELIX 30 AD3 TYR A 481 TRP A 496 1 16
HELIX 31 AD4 GLY A 499 GLY A 512 1 14
HELIX 32 AD5 GLY A 516 PHE A 525 1 10
HELIX 33 AD6 PHE A 525 GLY A 541 1 17
HELIX 34 AD7 PRO A 553 VAL A 569 1 17
HELIX 35 AD8 VAL A 569 THR A 582 1 14
HELIX 36 AD9 PHE A 590 THR A 595 1 6
HELIX 37 AE1 GLU L 80 ALA L 84 5 5
HELIX 38 AE2 SER L 122 SER L 128 1 7
HELIX 39 AE3 THR H 28 TYR H 32 5 5
HELIX 40 AE4 ARG H 87 THR H 91 5 5
HELIX 41 AE5 VAL H 101 GLY H 105 5 5
HELIX 42 AE6 SER H 192 GLN H 197 1 6
SHEET 1 AA1 2 CYS A 157 ARG A 158 0
SHEET 2 AA1 2 GLN A 209 SER A 210 1 O GLN A 209 N ARG A 158
SHEET 1 AA2 2 THR A 546 TYR A 547 0
SHEET 2 AA2 2 TYR A 550 VAL A 551 -1 O TYR A 550 N TYR A 547
SHEET 1 AA3 3 LEU L 4 SER L 7 0
SHEET 2 AA3 3 VAL L 19 VAL L 29 -1 O ARG L 24 N THR L 5
SHEET 3 AA3 3 PHE L 63 ILE L 76 -1 O LEU L 74 N MET L 21
SHEET 1 AA4 5 ILE L 10 THR L 13 0
SHEET 2 AA4 5 THR L 103 MET L 107 1 O GLU L 106 N MET L 11
SHEET 3 AA4 5 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103
SHEET 4 AA4 5 LEU L 34 GLN L 39 -1 N TYR L 37 O TYR L 88
SHEET 5 AA4 5 LYS L 46 ILE L 49 -1 O TRP L 48 N TRP L 36
SHEET 1 AA5 4 ILE L 10 THR L 13 0
SHEET 2 AA5 4 THR L 103 MET L 107 1 O GLU L 106 N MET L 11
SHEET 3 AA5 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103
SHEET 4 AA5 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91
SHEET 1 AA6 4 THR L 115 PHE L 119 0
SHEET 2 AA6 4 GLY L 130 PHE L 140 -1 O PHE L 136 N SER L 117
SHEET 3 AA6 4 TYR L 174 THR L 183 -1 O MET L 176 N LEU L 137
SHEET 4 AA6 4 VAL L 160 TRP L 164 -1 N LEU L 161 O THR L 179
SHEET 1 AA7 3 ASN L 146 ILE L 151 0
SHEET 2 AA7 3 SER L 192 THR L 198 -1 O THR L 198 N ASN L 146
SHEET 3 AA7 3 ILE L 206 ASN L 211 -1 O PHE L 210 N TYR L 193
SHEET 1 AA8 4 GLN H 3 SER H 7 0
SHEET 2 AA8 4 SER H 21 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 AA8 4 ILE H 78 MET H 83 -1 O LEU H 79 N CYS H 22
SHEET 4 AA8 4 PHE H 68 ASP H 73 -1 N ASP H 73 O ILE H 78
SHEET 1 AA9 6 LEU H 11 VAL H 12 0
SHEET 2 AA9 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12
SHEET 3 AA9 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113
SHEET 4 AA9 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95
SHEET 5 AA9 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AA9 6 ILE H 58 TYR H 60 -1 O TYR H 59 N GLU H 50
SHEET 1 AB1 4 LEU H 11 VAL H 12 0
SHEET 2 AB1 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12
SHEET 3 AB1 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 113
SHEET 4 AB1 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98
SHEET 1 AB2 4 SER H 126 LEU H 130 0
SHEET 2 AB2 4 SER H 141 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 AB2 4 TYR H 181 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 AB2 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186
SHEET 1 AB3 4 SER H 126 LEU H 130 0
SHEET 2 AB3 4 SER H 141 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 AB3 4 TYR H 181 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 AB3 4 VAL H 175 LEU H 176 -1 N VAL H 175 O THR H 182
SHEET 1 AB4 3 THR H 157 TRP H 160 0
SHEET 2 AB4 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159
SHEET 3 AB4 3 THR H 210 LYS H 215 -1 O THR H 210 N HIS H 205
SSBOND 1 CYS A 148 CYS A 157 1555 1555 2.04
SSBOND 2 CYS L 23 CYS L 89 1555 1555 2.04
SSBOND 3 CYS L 135 CYS L 195 1555 1555 2.03
SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.04
SSBOND 5 CYS H 146 CYS H 201 1555 1555 2.03
LINK CD1 LEU H 130 C GLY H 145 1555 1555 1.10
LINK CD1 LEU H 130 O GLY H 145 1555 1555 1.22
LINK O GLY A 42 NA NA A 707 1555 1555 2.27
LINK O ALA A 44 NA NA A 706 1555 1555 2.76
LINK O VAL A 45 NA NA A 707 1555 1555 2.04
LINK OD1 ASN A 49 NA NA A 706 1555 1555 3.09
LINK O SER A 320 NA NA A 706 1555 1555 3.01
LINK OG SER A 320 NA NA A 706 1555 1555 2.45
LINK O LEU A 417 NA NA A 707 1555 1555 2.35
LINK OD1 ASP A 420 NA NA A 707 1555 1555 2.27
LINK OG SER A 421 NA NA A 707 1555 1555 2.07
CISPEP 1 SER L 7 PRO L 8 0 11.33
CISPEP 2 TYR L 95 PRO L 96 0 -8.39
CISPEP 3 TYR L 141 PRO L 142 0 -9.93
CISPEP 4 PRO H 132 VAL H 133 0 -11.34
CISPEP 5 PHE H 152 PRO H 153 0 -16.16
CISPEP 6 GLU H 154 PRO H 155 0 25.77
CISPEP 7 TRP H 194 PRO H 195 0 11.90
SITE 1 AC1 5 ARG A 133 PHE A 136 TYR A 219 ASP A 238
SITE 2 AC1 5 ARG L 156
SITE 1 AC2 9 PHE A 43 ASP A 46 VAL A 120 GLY A 121
SITE 2 AC2 9 TYR A 123 TYR A 124 ASN A 125 SER A 422
SITE 3 AC2 9 GLY A 425
SITE 1 AC3 2 PHE A 350 TRP A 519
SITE 1 AC4 3 TYR A 273 LEU A 277 ILE A 351
SITE 1 AC5 5 ALA A 44 ASP A 46 ASN A 49 SER A 320
SITE 2 AC5 5 ASN A 352
SITE 1 AC6 5 GLY A 42 VAL A 45 LEU A 417 ASP A 420
SITE 2 AC6 5 SER A 421
SITE 1 AC7 4 TYR A 69 GLN A 316 SER A 320 SER A 356
CRYST1 97.415 140.312 166.962 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 0.010265 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005989 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
